|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-339 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 530.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 241 VKEDLNDDF-ETSLTELEPLEKDAYIVKLVFAGSTTTEPIVSSLSTAYDIKINILEANIKNTKNGTVGFLVLHIPYiSSV 319
Cdd:COG1135 241 LPTVLNDELpEELLARLREAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEG-DDA 319
|
330 340
....*....|....*....|
gi 446493357 320 DFGKFEKELIERQVKMEVLR 339
Cdd:COG1135 320 AIDAALAYLREQGVVVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-340 |
7.15e-159 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 448.10 E-value: 7.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 241 VKEDLNDDFETSLTEL---EPLEKDAYIVKLVFAGSTTTEPIVSSLSTAYDIKINILEANIKNTKNGTVGFLVLHIPYiS 317
Cdd:PRK11153 241 IQSTLHLDLPEDYLARlqaEPTTGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTG-D 319
|
330 340
....*....|....*....|...
gi 446493357 318 SVDFGKFEKELIERQVKMEVLRH 340
Cdd:PRK11153 320 PGDIQAAIAYLQEHGVKVEVLGY 342
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
1.94e-139 |
|
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: 394.64 E-value: 1.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-338 |
5.09e-111 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 326.84 E-value: 5.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 241 VKE----DLNDDFETSLTElEPLEKDAYIVKLVFAGSTTTEPIVSSLSTAYDIKINILEANIKNTKNGTVGFLVLHIpYI 316
Cdd:TIGR02314 241 IRStlhlSIPEDYQERLQA-TPFADSVPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEM-HG 318
|
330 340
....*....|....*....|..
gi 446493357 317 SSVDFGKFEKELIERQVKMEVL 338
Cdd:TIGR02314 319 TQQDTQAAIAYLQEHNVKVEVL 340
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-242 |
6.84e-98 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 289.20 E-value: 6.84e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGqLSKNGLRAK 80
Cdd:COG1126 1 MIEIENLHKSF--GDLEVL--KGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMF-PLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKR 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
...
gi 446493357 240 FVK 242
Cdd:COG1126 235 FLS 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
2.08e-94 |
|
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: 289.88 E-value: 2.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNK-EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRA 79
Cdd:COG1123 260 LLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 KRQKVSMIFQH----FNLLWsrTVLKNIMFPLEIAGV-PRRRAKQKALELVELVGLKGR-EKAYPSELSGGQKQRVGIAR 153
Cdd:COG1123 340 LRRRVQMVFQDpyssLNPRM--TVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*.
gi 446493357 234 HTVTKR 239
Cdd:COG1123 498 HPYTRA 503
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
2.16e-90 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 269.61 E-value: 2.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 R-QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIE 221
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
5.38e-87 |
|
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: 260.89 E-value: 5.38e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 -QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKV 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-242 |
1.05e-86 |
|
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: 262.19 E-value: 1.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRA- 79
Cdd:cd03294 20 LLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELREl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 KRQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:cd03294 100 RRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKR 239
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
...
gi 446493357 240 FVK 242
Cdd:cd03294 260 FFR 262
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
6.16e-85 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 256.94 E-value: 6.16e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlsknglRAK 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV--------TGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLL-WsRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG1116 79 GPDRGVVFQEPALLpW-LTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEmhvIR---RICDEVAVMES--GKVIE 221
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDeavFLADRVVVLSArpGRIVE 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-234 |
5.78e-84 |
|
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: 256.90 E-value: 5.78e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAP---TSGEVIIDGDHIGQLSKNGL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 78 RAKR-QKVSMIFQH----FNLLWsrTVLKNIMFPLEI-AGVPRRRAKQKALELVELVGL---KGREKAYPSELSGGQKQR 148
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLNPVM--TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*.
gi 446493357 229 FENPQH 234
Cdd:COG0444 239 FENPRH 244
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-223 |
3.76e-83 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 256.95 E-value: 3.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRA-KRQKVSMIFQHFNLLWS 96
Cdd:COG4175 40 TVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRElRRKKMSMVFQHFALLPH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 97 RTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTT 176
Cdd:COG4175 120 RTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446493357 177 DEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:COG4175 200 REMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIG 246
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
1.67e-82 |
|
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: 249.73 E-value: 1.67e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQH----FNLLWsrTVLKNIMFPLEIAGVPRRRAKQKALELVELVGL---KGREKAYPSELSGGQKQRVGIAR 153
Cdd:cd03257 81 RKEIQMVFQDpmssLNPRM--TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-241 |
6.73e-82 |
|
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: 248.74 E-value: 6.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtkNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:COG1127 5 MIEVRNLTKSFG--DRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPL-EIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPqHTVTKR 239
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQ 239
|
..
gi 446493357 240 FV 241
Cdd:COG1127 240 FL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-221 |
8.60e-82 |
|
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: 247.77 E-value: 8.60e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglrakr 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qKVSMIFQHFNLL-WsRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:cd03293 74 -DRGYVFQQDALLpW-LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMES--GKVIE 221
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
3.74e-79 |
|
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: 242.02 E-value: 3.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDhigQLSKNGLRAK 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR---PVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQH----FNLLWsrTVLKNIMFPLEIAGVPRRRakQKALELVELVGLKG--REKaYPSELSGGQKQRVGIARA 154
Cdd:COG1124 78 RRRVQMVFQDpyasLHPRH--TVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPsfLDR-YPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQH 234
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*...
gi 446493357 235 TVTKRFVK 242
Cdd:COG1124 233 PYTRELLA 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
7.05e-79 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 240.34 E-value: 7.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGP 224
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
1.89e-76 |
|
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: 233.96 E-value: 1.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlSKNGLRAKR 81
Cdd:cd03262 1 IEIKNLHKSF--GDFHVL--KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMF-PLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-238 |
2.41e-76 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 237.71 E-value: 2.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEY-------RTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSK 74
Cdd:COG4608 8 LEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 75 NGLRAKRQKVSMIFQH-FNLLWSR-TVLKNIMFPLEIAGV-PRRRAKQKALELVELVGLKgREKA--YPSELSGGQKQRV 149
Cdd:COG4608 88 RELRPLRRRMQMVFQDpYASLNPRmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLR-PEHAdrYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 150 GIARALANDPTVLLCDEATSALD----PQttdeILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPV 225
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDvsiqAQ----VLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPR 242
|
250
....*....|...
gi 446493357 226 TQVFENPQHTVTK 238
Cdd:COG4608 243 DELYARPLHPYTQ 255
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-233 |
9.64e-76 |
|
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: 232.78 E-value: 9.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKR 81
Cdd:cd03261 1 IELRGLTKSFGGR--TVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPL-EIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF--ENPQ 233
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-233 |
5.77e-75 |
|
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: 230.68 E-value: 5.77e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAKR 81
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
3.11e-74 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 229.56 E-value: 3.11e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIM--------FPLEIAGVPRRRAKQKALELVELVGLKgrEKAY--PSELSGGQKQRVG 150
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLLGLFPPEDRERALEALERVGLA--DKAYqrADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-241 |
1.29e-70 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 223.82 E-value: 1.29e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAK 80
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITH---E-MhvirRICDEVAVMESGKVIEHGPVTQVFENPQHtv 236
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdqeEaL----ALADRIAVMNDGRIEQVGTPEEIYERPAT-- 229
|
....*
gi 446493357 237 tkRFV 241
Cdd:COG3842 230 --RFV 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-228 |
1.64e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 216.85 E-value: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglRAKR 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
2.80e-69 |
|
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: 215.46 E-value: 2.80e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRtknkEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAKR 81
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
1.18e-68 |
|
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: 214.74 E-value: 1.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKR 81
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPL--------EIAGVPRRRAKQKALELVELVGLkgREKAYP--SELSGGQKQRVGI 151
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGL--LDKAYQraDQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 152 ARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGP 224
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
1.97e-68 |
|
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: 212.05 E-value: 1.97e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNgLRAKR 81
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLeiagvprrrakqkalelvelvglkgrekaypselSGGQKQRVGIARALANDPTV 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGK 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
1.08e-67 |
|
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: 220.93 E-value: 1.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPT---SGEVIIDGDHIGQLSkNGL 77
Cdd:COG1123 4 LLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS-EAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 78 RAKRqkVSMIFQHF-NLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALA 156
Cdd:COG1123 81 RGRR--IGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 157 NDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-233 |
6.91e-67 |
|
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: 211.54 E-value: 6.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNK-EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQhF--NLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKgrEKAY---PSELSGGQKQRVGIARAL 155
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLD--EEYLersPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 156 ANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-247 |
3.00e-66 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 209.22 E-value: 3.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSG-----EVIIDGD-HIGQlSK 74
Cdd:PRK11264 3 AIEVKNLVKKF--HGQTVL--HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTArSLSQ-QK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 75 NGLRAKRQKVSMIFQHFNLLWSRTVLKNIM-FPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIAR 153
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIIeGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDlllKIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFEN 231
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLN---TIRQlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
250
....*....|....*.
gi 446493357 232 PQHTVTKRFVKEDLND 247
Cdd:PRK11264 235 PQQPRTRQFLEKFLLQ 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-239 |
7.76e-66 |
|
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: 216.47 E-value: 7.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 11 YRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKS----TLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKR-QKVS 85
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 86 MIFQH----FNLLWsrTVLKNIMFPLEI-AGVPRRRAKQKALELVELVGL---KGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:COG4172 96 MIFQEpmtsLNPLH--TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVT 237
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYT 253
|
..
gi 446493357 238 KR 239
Cdd:COG4172 254 RK 255
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
8.68e-66 |
|
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: 207.29 E-value: 8.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGL-RA 79
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARaRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 KRQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGvpRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVT 226
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
1.38e-64 |
|
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: 203.95 E-value: 1.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRtkNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHL-----EAPTSGEVIIDGDHIGQLSKNG 76
Cdd:cd03260 1 IELRDLNVYYG--DKHAL--KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 77 LRAKRQkVSMIFQHFNLLWSrTVLKNIMFPLEIAGV-PRRRAKQKALELVELVGLKGREK--AYPSELSGGQKQRVGIAR 153
Cdd:cd03260 77 LELRRR-VGMVFQKPNPFPG-SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQqnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-242 |
1.58e-64 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 204.17 E-value: 1.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKnkEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlSKNGLRAK 80
Cdd:PRK09493 1 MIEFKNVSKHFGPT--QVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMF-PLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKR 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
...
gi 446493357 240 FVK 242
Cdd:PRK09493 235 FLQ 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
2.19e-64 |
|
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: 202.70 E-value: 2.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 3 ELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGdhiGQLSKNGLRAKRQ 82
Cdd:cd03225 1 ELKNLSFSYPDGARPAL--DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDG---KDLTKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 83 KVSMIFQHFNL-LWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03225 76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGK 218
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-233 |
4.67e-64 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 203.88 E-value: 4.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 17 EVLAvdHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgQLSKNG-----------LRAKRQKVS 85
Cdd:COG4598 22 EVLK--GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDRdgelvpadrrqLQRIRTRLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 86 MIFQHFNLlWS-RTVLKNIMF-PLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLL 163
Cdd:COG4598 99 MVFQSFNL-WShMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 164 CDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:COG4598 178 FDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-239 |
1.95e-63 |
|
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: 209.93 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTK-------NKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEaPTSGEVIIDGDHIGQLSK 74
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 75 NGLRAKRQKVSMIFQH-FNLLWSR-TVLKNIMFPLEIAGVPRRRA--KQKALELVELVGLKG--REKaYPSELSGGQKQR 148
Cdd:COG4172 355 RALRPLRRRMQVVFQDpFGSLSPRmTVGQIIAEGLRVHGPGLSAAerRARVAEALEEVGLDPaaRHR-YPHEFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
250
....*....|.
gi 446493357 229 FENPQHTVTKR 239
Cdd:COG4172 514 FDAPQHPYTRA 524
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
8.38e-63 |
|
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: 199.17 E-value: 8.38e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKR 81
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-244 |
2.54e-62 |
|
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: 198.68 E-value: 2.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKA--YPSELSGGQKQRVGIARALANDP 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdrYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKR 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....*
gi 446493357 240 FVKED 244
Cdd:cd03295 235 FVGAD 239
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-228 |
7.16e-62 |
|
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: 197.52 E-value: 7.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPL--------EIAGVPRRRAKQKALELVELVGLKgrEKAY--PSELSGGQKQRVG 150
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLA--DKAYqrADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.86e-60 |
|
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: 194.49 E-value: 1.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNgLRAk 80
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH-RIA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIM----------FPLEIAGVPR-----RRAKQKALELVELVGLKGREKAYPSELSGGQ 145
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLvaaharlgrgLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 146 KQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPV 225
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 446493357 226 TQVFENPQ 233
Cdd:COG0411 238 AEVRADPR 245
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-233 |
2.15e-60 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 197.29 E-value: 2.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNkevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGdhigQLSKNGLRAKR 81
Cdd:COG1118 3 IEVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDLFTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-241 |
6.57e-60 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 192.94 E-value: 6.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHL-----EAPTSGEVIIDGDHI--GQLSKNGLRAKrqkVSMIFQHFN 92
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIydPDVDVVELRRR---VGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 93 LLwSRTVLKNIMFPLEIAGVprrRAKQKALELVE----LVGL----KGREKAYPSELSGGQKQRVGIARALANDPTVLLC 164
Cdd:COG1117 103 PF-PKSIYDNVAYGLRLHGI---KSKSELDEIVEeslrKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 165 DEATSALDPQTTDEILDLLLKIREQqnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:COG1117 179 DEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
24-240 |
2.39e-59 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 191.00 E-value: 2.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHI---GQLSKNGLRAKRQKVSMIFQHFNLLWSRTVL 100
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KN-IMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEI 179
Cdd:PRK11124 101 QNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 180 LDLllkIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQvFENPQhtvTKRF 240
Cdd:PRK11124 181 VSI---IRElaETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ---TEAF 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-240 |
8.99e-59 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 189.45 E-value: 8.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNkevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIG---QLSKNGLR 78
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 AKRQKVSMIFQHFNLLWSRTVLKN-IMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLllkIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTqVFENPQht 235
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEI---IRElsQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQPQ-- 232
|
....*
gi 446493357 236 vTKRF 240
Cdd:COG4161 233 -TEAF 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-245 |
4.14e-58 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 188.64 E-value: 4.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHI-------GQLS 73
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 74 ---KNGLRAKRQKVSMIFQHFNLLWSRTVLKNIM-FPLEIAGVPRRRAKQKALELVELVGLKGREKA-YPSELSGGQKQR 148
Cdd:PRK10619 81 vadKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
250
....*....|....*..
gi 446493357 229 FENPQHTVTKRFVKEDL 245
Cdd:PRK10619 240 FGNPQSPRLQQFLKGSL 256
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
4.34e-58 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 189.46 E-value: 4.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNK-EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIdGDHIGQLSKNG--LR 78
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkkLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 AKRQKVSMIFQhF--NLLWSRTVLKNIMF-PLEIaGVPRRRAKQKALELVELVGL--KGREKAyPSELSGGQKQRVGIAR 153
Cdd:PRK13634 82 PLRKKVGIVFQ-FpeHQLFEETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLpeELLARS-PFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-233 |
4.64e-58 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 187.64 E-value: 4.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNglRAKRQKVSMIFQHFNLLWSR 97
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH--EIARLGIGRTFQIPRLFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNIM----------FPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEA 167
Cdd:cd03219 91 TVLENVMvaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 168 TSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:cd03219 171 AAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-229 |
6.94e-58 |
|
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: 188.02 E-value: 6.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGdhIGQLSKNGLRAKR 81
Cdd:TIGR04520 1 IEVENVSFSY--PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPR---RRAKQKALELVELVGLKGREkayPSELSGGQKQRVGIARALAN 157
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPReemRKRVDEALKLVGMEDFRDRE---PHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEM-HVIRriCDEVAVMESGKVIEHGPVTQVF 229
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVL--ADRVIVMNKGKIVAEGTPREIF 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-241 |
8.06e-58 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 190.67 E-value: 8.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAK 80
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHE----MhvirRICDEVAVMESGKVIEHGPVTQVFENPQHTv 236
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPANL- 228
|
....*
gi 446493357 237 tkrFV 241
Cdd:COG3839 229 ---FV 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-243 |
1.64e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 183.42 E-value: 1.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKevlavdHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglrAK 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL------RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RqKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:COG3840 71 R-PVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRF 240
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
...
gi 446493357 241 VKE 243
Cdd:COG3840 230 LGI 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-253 |
2.00e-56 |
|
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: 183.52 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglRAK 80
Cdd:COG4555 1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP----REA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFEnpqhtvtkRF 240
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE--------EI 223
|
250
....*....|...
gi 446493357 241 VKEDLNDDFETSL 253
Cdd:COG4555 224 GEENLEDAFVALI 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
2.52e-56 |
|
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: 182.82 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNglraKR 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH----KR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QkVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03300 73 P-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-242 |
1.18e-55 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 186.39 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 19 LAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLR-AKRQKVSMIFQHFNLLWSR 97
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELReVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTD 177
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 178 EILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFVK 242
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
4.83e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 177.59 E-value: 4.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKnkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlsknglraK 80
Cdd:COG1121 6 AIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR--------A 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSrtvlknimFPL---EIA-----------GVPRRRAKQKALELVELVGLKGREKAYPSELSGGQK 146
Cdd:COG1121 74 RRRIGYVPQRAEVDWD--------FPItvrDVVlmgrygrrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 147 QRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMeSGKVIEHGPVT 226
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPE 223
|
...
gi 446493357 227 QVF 229
Cdd:COG1121 224 EVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
1.11e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.39 E-value: 1.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVvkEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:COG4619 1 LELEGL--SFRVGGKPIL--SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFPLEIAGvpRRRAKQKALELVELVGLKGREKAYP-SELSGGQKQRVGIARALANDPT 160
Cdd:COG4619 74 RQVAYVPQE-PALWGGTVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-238 |
3.33e-53 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 177.85 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKRQKVSMIFQH-FNLLWS 96
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYGSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 97 RTVLKNIMF-PLEI-AGVPRRRAKQKALELVELVGLK----GRekaYPSELSGGQKQRVGIARALANDPTVLLCDEATSA 170
Cdd:PRK11308 108 RKKVGQILEePLLInTSLSAAERREKALAMMAKVGLRpehyDR---YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 171 LDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTK 238
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-243 |
5.85e-53 |
|
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: 174.45 E-value: 5.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglrAKR 81
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-----VQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRR----RAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVT 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....*.
gi 446493357 238 KRFVKE 243
Cdd:cd03296 234 YSFLGE 239
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-243 |
2.19e-52 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 173.87 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRT-----KNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgQLSKNG 76
Cdd:COG4167 5 LEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 77 LRAKRqkVSMIFQHFN--LLWSRTVLKNIMFPLEIAG--VPRRRaKQKALELVELVGLKgREKA--YPSELSGGQKQRVG 150
Cdd:COG4167 84 YRCKH--IRMIFQDPNtsLNPRLNIGQILEEPLRLNTdlTAEER-EERIFATLRLVGLL-PEHAnfYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFE 230
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|...
gi 446493357 231 NPQHTVTKRFVKE 243
Cdd:COG4167 240 NPQHEVTKRLIES 252
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
3.84e-52 |
|
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: 169.89 E-value: 3.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNkevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGqlsKNGLRAKR 81
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK---KEPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qKVSMIFQHFNLLWSRTVLKNImfpleiagvprrrakqkalelvelvglkgrekaypsELSGGQKQRVGIARALANDPTV 161
Cdd:cd03230 74 -RIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-220 |
7.18e-52 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 171.15 E-value: 7.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlsknGLRAKR 81
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
2.42e-51 |
|
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: 167.95 E-value: 2.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVL--KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFnLLWSRTVLKNImfpleiagvprrrakqkalelvelvglkgrekaypseLSGGQKQRVGIARALANDPTV 161
Cdd:cd03228 76 KNIAYVPQDP-FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRiCDEVAVMESGK 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALA--KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-229 |
5.57e-51 |
|
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: 169.84 E-value: 5.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtkNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAK 80
Cdd:COG1120 1 MLEAENLSVGYG--GRPVL--DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS---RREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIM---FP-LEIAGVPR---RRAKQKALELVELVGLKGRekaYPSELSGGQKQRVGIAR 153
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVAlgrYPhLGLFGRPSaedREAVEEALERTGLEHLADR---PVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF 229
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
1.87e-50 |
|
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: 178.49 E-value: 1.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLrakR 81
Cdd:COG2274 474 IELENVSFRYPGDSPPVL--DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---R 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFpleiaGVPRRRaKQKALELVELVGLKGREKAYP-----------SELSGGQKQRVG 150
Cdd:COG2274 549 RQIGVVLQD-VFLFSGTIRENITL-----GDPDAT-DEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGP 224
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGT 692
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-290 |
5.20e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 168.75 E-value: 5.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKN----- 75
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 76 ----GLRAKrqkvsMifqhfnllwsrTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGI 151
Cdd:COG4152 77 peerGLYPK-----M-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 152 ARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFEn 231
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR- 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 232 pQHTVTKRFVKEDLNDDFETSLTELEPLEKDAYIVKLVFAGSTTTEPIVSSLSTAYDIK 290
Cdd:COG4152 219 -QFGRNTLRLEADGDAGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARGPVR 276
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
1.01e-49 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 166.96 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAK 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVsmiFQHFNLL-WsRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG4525 78 RGVV---FQKDALLpW-LNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITH 199
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-251 |
6.81e-49 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 165.61 E-value: 6.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 17 EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNgLRAKRQKVSMIFQHFNL-LW 95
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLVFQYPEYqLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 96 SRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKG---REKAyPSELSGGQKQRVGIARALANDPTVLLCDEATSALD 172
Cdd:PRK13637 98 EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedyKDKS-PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 173 PQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFEN-----------PQHTVTKRFV 241
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvetlesiglavPQVTYLVRKL 256
|
250
....*....|...
gi 446493357 242 KE---DLNDDFET 251
Cdd:PRK13637 257 RKkgfNIPDDIFT 269
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-207 |
1.85e-47 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 159.98 E-value: 1.85e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 9 KEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKR-QKVSMI 87
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 88 FQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEA 167
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446493357 168 TSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRI 207
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
2.00e-47 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 167.13 E-value: 2.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTknkeVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGD--HIgqlsKNGLR 78
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRI----RSPRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 AKRQKVSMIFQHFNLLWSRTVLKNIMFPLEIAG---VPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARAL 155
Cdd:COG3845 77 AIALGIGMVHQHFMLVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 156 ANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEG-KSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-241 |
3.66e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 160.08 E-value: 3.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 5 KEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHL-----EAPTSGEVIIDGDHIGQLSKNGLRa 79
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 krQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAK-----QKALELVELVG-LKGREKAYPSELSGGQKQRVGIAR 153
Cdd:PRK14247 82 --RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqervRWALEKAQLWDeVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELK--KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
....*...
gi 446493357 234 HTVTKRFV 241
Cdd:PRK14247 238 HELTEKYV 245
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
7.92e-47 |
|
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: 157.80 E-value: 7.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAKR 81
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-227 |
1.53e-46 |
|
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: 157.15 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNglraKR 81
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03265 73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQ 227
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.78e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 158.62 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDhigQLSKNGLRAK 80
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGI---TISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEM-HVIrrICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAI--LADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-254 |
2.10e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 159.22 E-value: 2.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 17 EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHI-GQLSKNGLRAKRQKVSMIFQhF--NL 93
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQ-FpeAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 94 LWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGR--EKAyPSELSGGQKQRVGIARALANDPTVLLCDEATSAL 171
Cdd:PRK13641 98 LFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDliSKS-PFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 172 DPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHtVTKRFVKEDLNDDFET 251
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEW-LKKHYLDEPATSRFAS 254
|
...
gi 446493357 252 SLT 254
Cdd:PRK13641 255 KLE 257
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
11-223 |
2.13e-46 |
|
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: 155.67 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 11 YRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKRQKVSMIFQh 90
Cdd:cd03214 7 VGYGGRTVL--DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 91 fnllwsrtvlknimfpleiagvprrrakqkALELVELVGLKGRekaYPSELSGGQKQRVGIARALANDPTVLLCDEATSA 170
Cdd:cd03214 81 ------------------------------ALELLGLAHLADR---PFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493357 171 LDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
1.29e-45 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 162.11 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTknkeVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKngLRAK 80
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP--RDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAG---VPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
1.95e-45 |
|
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: 152.03 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAKRQKVSMIFQHFNLLWSRTVL 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 101 KNIMFPLEIAGVPRRRAKQKALELVELVGLKGREK----AYPSELSGGQKQRVGIARALANDPTVLLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-230 |
2.22e-45 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 155.94 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVkeYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDhigQLSKNGLRAKR 81
Cdd:PRK13635 6 IRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPR----RRAKQkALELVELVGLKGREkayPSELSGGQKQRVGIARALA 156
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPReemvERVDQ-ALRQVGMEDFLNRE---PHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 157 NDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFE 230
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
13-238 |
2.23e-45 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 157.56 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 13 TKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKRQKVSMIFQhfN 92
Cdd:PRK15079 29 QPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQ--D 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 93 LLWS----RTVLKNIMFPLEI--AGVPRRRAKQKALELVELVGLK----GRekaYPSELSGGQKQRVGIARALANDPTVL 162
Cdd:PRK15079 107 PLASlnprMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLpnliNR---YPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 163 LCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTK 238
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-223 |
2.67e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 153.84 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlsknglraKRQKVSMIFQHFNLLWSR-- 97
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--------ERKRIGYVPQRRSIDRDFpi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 ----TVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDP 173
Cdd:cd03235 86 svrdVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493357 174 QTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMEsGKVIEHG 223
Cdd:cd03235 166 KTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-232 |
5.63e-45 |
|
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: 157.18 E-value: 5.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGdHIGQLSKNG--LRAKRQKVSMIFQHFNLLWSRTVLK 101
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGifLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIMFpleiaGVPRRRAKQKAL---ELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDE 178
Cdd:COG4148 97 NLLY-----GRKRAPRAERRIsfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493357 179 ILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
1.10e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 150.47 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 3 ELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKRQ 82
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 83 KVSMIFQhfnllwsrtvlknimfpleiagvprrrakqkalelvelvglkgrekaypseLSGGQKQRVGIARALANDPTVL 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 163 LCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGK 218
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELA-EEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-232 |
1.18e-44 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 154.07 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKN-------KEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLS 73
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhqhQTVL--NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 74 KNGLRAKRQKVSMIFQH----FNLlwSRTVLKNIMFPLE-IAGVPRRRAKQKALELVELVGLK-GREKAYPSELSGGQKQ 147
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDsisaVNP--RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 148 RVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVT- 226
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGd 238
|
....*..
gi 446493357 227 -QVFENP 232
Cdd:PRK10419 239 kLTFSSP 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-241 |
4.85e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 160.02 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 16 KEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKRQKVSMIFQ--HFNL 93
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 94 LWSRTVLKNIMFPLEIAGV-PRRRAKQKALELVELVGLKGrEKA--YPSELSGGQKQRVGIARALANDPTVLLCDEATSA 170
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLP-EHAwrYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 171 LDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-247 |
1.95e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 152.93 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEY-RTKnkeVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglrAK 80
Cdd:PRK10851 3 IEIANIKKSFgRTQ---VL--NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH-----AR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIagVPRRR------AKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARA 154
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPqh 234
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP-- 228
|
250
....*....|...
gi 446493357 235 tvTKRFVKEDLND 247
Cdd:PRK10851 229 --ATRFVLEFMGE 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-267 |
4.20e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 152.68 E-value: 4.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNkevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglrAK 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-----PY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPqhtvTKRF 240
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP----TTRY 245
|
250 260
....*....|....*....|....*....
gi 446493357 241 VKEDLN--DDFETSLTELEPlekDAYIVK 267
Cdd:PRK11607 246 SAEFIGsvNVFEGVLKERQE---DGLVID 271
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-241 |
8.00e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 148.84 E-value: 8.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHL-----EAPTSGEVIIDGDHIGQLSKNGLRAkRQKVSMIFQHFNLLWSRT 98
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEV-RREVGMVFQYPNPFPHLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 99 VLKNIMFPLEIAGVPRrrAKQKALELVELV--------GLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSA 170
Cdd:PRK14267 102 IYDNVAIGVKLNGLVK--SKKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 171 LDPQTTDEILDLLLKIREQqnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-230 |
8.57e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 149.51 E-value: 8.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNK-EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKN-GLRA 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 KRQKVSMIFQhF--NLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKG--REKAyPSELSGGQKQRVGIARAL 155
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 156 ANDPTVLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFE 230
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
9.99e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 149.11 E-value: 9.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDhigQLSKNGLRAK 80
Cdd:PRK13650 4 IIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIrRICDEVAVMESGKV 219
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
1.40e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 155.32 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:COG1132 340 IEFENVSFSYP-GDRPVL--KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLR--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFnLLWSRTVLKNIMFpleiaGVPR------RRAKQKA--LELVE--------LVGLKGrekaypSELSGGQ 145
Cdd:COG1132 414 RQIGVVPQDT-FLFSGTIRENIRY-----GRPDatdeevEEAAKAAqaHEFIEalpdgydtVVGERG------VNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 146 KQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGP 224
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-223 |
1.44e-42 |
|
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: 146.87 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 23 HVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglrAKRQKVSMIFQHFNLLWSRTVLKN 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 103 ImfplEIAGVPRRR---AKQKALE-LVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDE 178
Cdd:cd03298 91 V----GLGLSPGLKltaEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446493357 179 ILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-201 |
2.40e-42 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 147.54 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNkevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAK 80
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RqkvSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:PRK11248 72 R---GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEM 201
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
3.73e-42 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 145.41 E-value: 3.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkevLAVDHVNLSIRAGsIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlsKNGLRAKR 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqqNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-241 |
3.91e-42 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 147.24 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVK--EYRT---KNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDgDHigQLSKN 75
Cdd:PRK15112 4 LLEVRNLSKtfRYRTgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID-DH--PLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 76 GLRAKRQKVSMIFQH-FNLLWSRTVLKNIM-FPL----EIAGVPRRRAKQKALELVELvgLKGREKAYPSELSGGQKQRV 149
Cdd:PRK15112 81 DYSYRSQRIRMIFQDpSTSLNPRQRISQILdFPLrlntDLEPEQREKQIIETLRQVGL--LPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 150 GIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF 229
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
250
....*....|..
gi 446493357 230 ENPQHTVTKRFV 241
Cdd:PRK15112 239 ASPLHELTKRLI 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-241 |
2.89e-41 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.46 E-value: 2.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKS-TLIRMFNHLEA---PTSGEVIIDGDHIgqlSKNGLRAKrqKVSMIFQH----FN 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPV---APCALRGR--KIATIMQNprsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 93 LLwsRTVLKNIMFPLEIAGVPRRRAKqkALELVELVGLKGRE---KAYPSELSGGQKQRVGIARALANDPTVLLCDEATS 169
Cdd:PRK10418 94 PL--HTMHTHARETCLALGKPADDAT--LTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 170 ALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
15-232 |
7.45e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 145.38 E-value: 7.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 15 NKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQ-----------LSKNGLRAK--R 81
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhelitnpYSKKIKNFKelR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNL-LWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGR--EKAyPSELSGGQKQRVGIARALAND 158
Cdd:PRK13631 116 RRVSMVFQFPEYqLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSylERS-PFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 159 PTVLLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-203 |
9.74e-41 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 151.03 E-value: 9.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGL-RA 79
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 KRQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHV 203
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQV 206
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-231 |
1.03e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 144.07 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYR--TKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGdhIGQLSKNGLR 78
Cdd:PRK13633 4 MIKCKNVSYKYEsnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 AKRQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFEN 231
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
1.15e-40 |
|
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: 140.26 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTknkeVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNglRAKR 81
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR--DARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQhfnllwsrtvlknimfpleiagvprrrakqkalelvelvglkgrekaypseLSGGQKQRVGIARALANDPTV 161
Cdd:cd03216 75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-241 |
3.55e-40 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 141.32 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAKRQKVSMIFQHFNLLWSRTVL 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEIL 180
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 181 DLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-223 |
3.99e-40 |
|
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: 140.51 E-value: 3.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 31 GSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKN-GLRAKRQKVSMIFQHFNLLWSRTVLKNIMFPLEi 109
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 110 aGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQ 189
Cdd:cd03297 102 -RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 446493357 190 QNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03297 181 LNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
4.19e-40 |
|
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: 148.37 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:COG4988 337 IELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD---PASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFpleiaGVPR--RRAKQKALELVEL--------------VGLKGREkaypseLSGGQ 145
Cdd:COG4988 411 RQIAWVPQN-PYLFAGTIRENLRL-----GRPDasDEELEAALEAAGLdefvaalpdgldtpLGEGGRG------LSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 146 KQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnlTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPV 225
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
..
gi 446493357 226 TQ 227
Cdd:COG4988 556 EE 557
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-229 |
4.72e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 142.23 E-value: 4.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 17 EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNG-LRAKRQKVSMIFQhF--NL 93
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKRIGMVFQ-FpeSQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 94 LWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGL-KGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALD 172
Cdd:PRK13646 98 LFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 173 PQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF 229
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
4.91e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 142.14 E-value: 4.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgQLSKNGLRAK 80
Cdd:PRK13639 1 ILETRDLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHF-NLLWSRTVLKNIMF-PLEIaGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALAND 158
Cdd:PRK13639 77 RKTVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 159 PTVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-232 |
6.93e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 143.71 E-value: 6.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrTKNkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlsknglRAKR 81
Cdd:PRK11432 7 VVLKNITKRF-GSN---TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QK-VSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:PRK11432 77 QRdICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 161 VLLCDEATSALDPQTTDEILDlllKIREQQ---NLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMRE---KIRELQqqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-223 |
6.96e-40 |
|
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: 140.37 E-value: 6.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:cd03249 1 IEFKNVSFRYPSR-PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFPLEIAGVP-RRRAKQKAL--ELVE--------LVGLKGrekaypSELSGGQKQRVG 150
Cdd:cd03249 77 SQIGLVSQE-PVLFDGTIAENIRYGKPDATDEeVEEAAKKANihDFIMslpdgydtLVGERG------SQLSGGQKQRIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREqqNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHG 223
Cdd:cd03249 150 IARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
8.47e-40 |
|
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: 146.87 E-value: 8.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVL-AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIID-GDHIGQLSKNGL- 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 78 ---RAKRQkVSMIFQHFNLLWSRTVLKNIMFPLEIAgVPRRRAKQKALELVELVGLKgREKA------YPSELSGGQKQR 148
Cdd:TIGR03269 359 grgRAKRY-IGILHQEYDLYPHRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFD-EEKAeeildkYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
..
gi 446493357 229 FE 230
Cdd:TIGR03269 516 VE 517
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-223 |
1.08e-39 |
|
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: 139.93 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAkr 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIL--DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qKVSMIFQHfNLLWSRTVLKNImfPLEIAGVPRRRAKQKA---------LELVE----LVGLKGrekaypSELSGGQKQR 148
Cdd:cd03252 77 -QVGVVLQE-NVLFNRSIRDNI--ALADPGMSMERVIEAAklagahdfiSELPEgydtIVGEQG------AGLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIreQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHG 223
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQG 218
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-206 |
1.51e-39 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 139.24 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLlkirEQQN---LTIVLITHEMHVIRR 206
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLF----EEFNrvgVTVLMATHDIGLISR 202
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-243 |
2.05e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 142.78 E-value: 2.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAKR 81
Cdd:PRK09452 15 VELRGISKSF--DGKEVI--SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPAEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
..
gi 446493357 242 KE 243
Cdd:PRK09452 246 GE 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-223 |
2.95e-39 |
|
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: 138.18 E-value: 2.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNkevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlsknglrAKR 81
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
3.08e-39 |
|
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: 137.73 E-value: 3.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNkevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglraKR 81
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKqkalELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03268 72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
3.55e-39 |
|
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: 137.88 E-value: 3.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAK 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV---VKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RqKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:cd03266 78 R-RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-234 |
1.49e-38 |
|
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: 136.83 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLrakrqkvsMIFQHFNLLWSRTVL 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMFPLEIAGVPRRRAKQKAL--ELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDE 178
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 179 ILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV-FENPQH 234
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
1.65e-38 |
|
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: 143.75 E-value: 1.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:COG4987 334 LELEDVSFRYPGAGRPVL--DGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMfpleIAgvpRRRAKQKALELV-ELVGLKGREKAYP-----------SELSGGQKQRV 149
Cdd:COG4987 409 RRIAVVPQR-PHLFDTTLRENLR----LA---RPDATDEELWAAlERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 150 GIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnlTIVLITHEMHVIRRiCDEVAVMESGKVIEHGP 224
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGT 552
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-219 |
2.88e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.73 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 4 LKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEViidgdhigqLSKNG-LRAKRQ 82
Cdd:PRK11247 15 LNAVSKRY--GERTVL--NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTApLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 83 KVSMIFQHFNLLWSRTVLKNIMFPLeiagvpRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVL 162
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 163 LCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-234 |
3.58e-38 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 138.70 E-value: 3.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAP---TSGEVIIDGDHIGQLSK--- 74
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEkel 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 75 NGLRAkrQKVSMIFQHfnllwSRTVLKNIMFP----LEIAGVPRRRAKQKA-------LELVELVGLKGREKAYPSELSG 143
Cdd:PRK09473 92 NKLRA--EQISMIFQD-----PMTSLNPYMRVgeqlMEVLMLHKGMSKAEAfeesvrmLDAVKMPEARKRMKMYPHEFSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 144 GQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYG 244
|
250
....*....|.
gi 446493357 224 PVTQVFENPQH 234
Cdd:PRK09473 245 NARDVFYQPSH 255
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
4.23e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 137.91 E-value: 4.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNK-EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 ---------------------RQKVSMIFQHFNL-LWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLkgrEKAY- 137
Cdd:PRK13651 83 vleklviqktrfkkikkikeiRRRVGVVFQFAEYqLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL---DESYl 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 138 ---PSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVM 214
Cdd:PRK13651 160 qrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|....*..
gi 446493357 215 ESGKVIEHGPVTQVFEN 231
Cdd:PRK13651 239 KDGKIIKDGDTYDILSD 255
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-233 |
4.48e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 137.24 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGE---VIIDGDHIGQlskNGLR 78
Cdd:PRK13640 6 VEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA---KTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 AKRQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIrRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
5.53e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 135.54 E-value: 5.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtKNKEVlaVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNgLRAK 80
Cdd:COG1137 3 TLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH-KRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 R------QKVSmIFQhfNLlwsrTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARA 154
Cdd:COG1137 78 LgigylpQEAS-IFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnltI-VLIT-HEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG---IgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNP 227
|
.
gi 446493357 233 Q 233
Cdd:COG1137 228 L 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
6.29e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 136.90 E-value: 6.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgQLSKNGLRAK 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK13636 81 RESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF 229
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
10-238 |
1.39e-37 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 136.96 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 10 EYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKStLI-----------------RMFnhleaptsgeviIDGDHIGQL 72
Cdd:COG4170 12 EIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKS-LIakaicgitkdnwhvtadRFR------------WNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 73 SKNGLRA-KRQKVSMIFQHFN--LLWSRTVLKNIMFPL---EIAGVPRRRA---KQKALELVELVGLKGRE---KAYPSE 140
Cdd:COG4170 79 SPRERRKiIGREIAMIFQEPSscLDPSAKIGDQLIEAIpswTFKGKWWQRFkwrKKRAIELLHRVGIKDHKdimNSYPHE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 141 LSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
250
....*....|....*...
gi 446493357 221 EHGPVTQVFENPQHTVTK 238
Cdd:COG4170 239 ESGPTEQILKSPHHPYTK 256
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-236 |
1.47e-37 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 135.28 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 22 DHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKRQKVSMIFQHFNLLWSRTVLK 101
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIMFPL-EIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEIL 180
Cdd:PRK11831 104 NVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 181 DLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTV 236
Cdd:PRK11831 184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRV 239
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-232 |
1.10e-36 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 139.86 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTK-NKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRak 80
Cdd:TIGR00958 479 IEFQDVSFSYPNRpDVPVL--KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH-- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 rQKVSMIFQHfNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGlkGREKAYPSE-------LSGGQKQRVGIAR 153
Cdd:TIGR00958 555 -RQVALVGQE-PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDTEvgekgsqLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 154 ALANDPTVLLCDEATSALDPQttdeILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAE----CEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-241 |
1.13e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 132.59 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 11 YRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHL-----EAPTSGEVIIDGDHIGQLSKNGLRAkRQKVS 85
Cdd:PRK14239 14 YYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL-RKEIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 86 MIFQHFNLlWSRTVLKNIMFPLEIAGVprrRAKQKALELVE--LVG------LKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:PRK14239 90 MVFQQPNP-FPMSIYENVVYGLRLKGI---KDKQVLDEAVEksLKGasiwdeVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREQqnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVT 237
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKET 243
|
....
gi 446493357 238 KRFV 241
Cdd:PRK14239 244 EDYI 247
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
1.62e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.00 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTkNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDhigQLSKNGLRAK 80
Cdd:PRK13652 3 LIETRDLCYSYSG-SKEAL--NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFN-LLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK13652 77 RKFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-239 |
1.75e-36 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 137.91 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 11 YRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKS-TLIRMFNHLEAP----TSGEVIIDGDHIGQLSKNGLRAKR-QKV 84
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 85 SMIFQH----FNLLwsRTVLKNIMFPLEI-AGVPRRRAKQKALELVELVGL---KGREKAYPSELSGGQKQRVGIARALA 156
Cdd:PRK15134 95 AMIFQEpmvsLNPL--HTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 157 NDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTV 236
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
...
gi 446493357 237 TKR 239
Cdd:PRK15134 253 TQK 255
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-242 |
1.94e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 133.71 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKS----TLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglRAKRQ----KVSMIFQH- 90
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISE---KERRNlvgaEVAMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 91 -FNLLWSRTVLKNIMFPLEI-AGVPRRRAKQKALELVELVGL---KGREKAYPSELSGGQKQRVGIARALANDPTVLLCD 165
Cdd:PRK11022 99 mTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 166 EATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFVK 242
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-266 |
2.74e-36 |
|
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: 137.24 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEA--PTSGEVI---------------- 63
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVL--KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 64 ---------------IDGDHIGqLSKNGLRAKRQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVEL 127
Cdd:TIGR03269 77 kvgepcpvcggtlepEEVDFWN-LSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 128 VGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRI 207
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 208 CDEVAVMESGKVIEHGPVTQVFENPQHTVTKrfVKEDLNDDFETSLTELEPLEKDAYIV 266
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVFMEGVSE--VEKECEVEVGEPIIKVRNVSKRYISV 292
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-244 |
3.23e-36 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 131.27 E-value: 3.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 19 LAVDHVNLSIRAGSIYGVIGFSGAGKSTLirmFNHLEA---PTSGEVIIDGDHIGQLSknGLRAKRQKVSMIFQHFNLLW 95
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTV---FNCLTGfykPTGGTILLRGQHIEGLP--GHQIARMGVVRTFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 96 SRTVLKNIMFPLE-------IAGV---PR-RRAKQKALEL----VELVGLKGREKAYPSELSGGQKQRVGIARALANDPT 160
Cdd:PRK11300 94 EMTVIENLLVAQHqqlktglFSGLlktPAfRRAESEALDRaatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQhtVTKRF 240
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD--VIKAY 251
|
....
gi 446493357 241 VKED 244
Cdd:PRK11300 252 LGEA 255
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-223 |
4.94e-36 |
|
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: 130.43 E-value: 4.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKr 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVL--RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qkVSMIFQHfNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVEL-----------VGLKGrekaypSELSGGQKQRVG 150
Cdd:cd03251 78 --IGLVSQD-VFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFimelpegydtvIGERG------VKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLKIreQQNLTIVLITHEMHVIRRIcDEVAVMESGKVIEHG 223
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERL--MKNRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-283 |
9.77e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 131.47 E-value: 9.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglRAKR 81
Cdd:PRK13537 8 IDFRNVEKRYGDK----LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHGPvtqvfenPQHTVTKRF- 240
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGA-------PHALIESEIg 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446493357 241 --VKEDLNDDFETSLTELEPLEKDAYIV-KLVFAGSTTTEPIVSSL 283
Cdd:PRK13537 232 cdVIEIYGPDPVALRDELAPLAERTEISgETLFCYVRDPEPLHARL 277
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-232 |
1.26e-35 |
|
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: 129.20 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGlRAkR 81
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RA-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 162 LLCDEATSALDPQTTDEILDLllkIREQQNLTI-VLIT-HEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKI---IKILKDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-224 |
1.32e-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: 128.71 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNgLRAKRqKVSMIFQHFNLLWSRTVLKNi 103
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARA-GIGYVPEGRRIFPELTVEEN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 mfpLEIAGVPRRRAKQKAL--ELVELV-GLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEIL 180
Cdd:cd03224 96 ---LLLGAYARRRAKRKARleRVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446493357 181 DLLLKIREQQnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGP 224
Cdd:cd03224 173 EAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-238 |
1.42e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 130.90 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNK-EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIdGDHI--GQLSK-NGL 77
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAipANLKKiKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 78 RAKRQKVSMIFQHFNL-LWSRTVLKNIMF-PLEIaGVPRRRAKQKALELVELVGL-KGREKAYPSELSGGQKQRVGIARA 154
Cdd:PRK13645 86 KRLRKEIGLVFQFPEYqLFQETIEKDIAFgPVNL-GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENpQH 234
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN-QE 243
|
....
gi 446493357 235 TVTK 238
Cdd:PRK13645 244 LLTK 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-229 |
1.54e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.51 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVkeYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnGLRAK 80
Cdd:PRK13548 2 MLEARNLS--VRLGGRTLL--DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQkvSMIFQHFNLLWSRTVLKNI-M--FPLEIAGVPRRRAKQKALELVELVGLKGRekAYPsELSGGQKQRVGIARALA- 156
Cdd:PRK13548 77 RR--AVLPQHSSLSFPFTVEEVVaMgrAPHGLSRAEDDALVAAALAQVDLAHLAGR--DYP-QLSGGEQQRVQLARVLAq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 157 -----NDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF 229
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
1.57e-35 |
|
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: 128.48 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLrakR 81
Cdd:cd03245 3 IEFRNVSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMF------------PLEIAGVPRRRAKQ-KALELveLVGLKGRekaypsELSGGQKQR 148
Cdd:cd03245 78 RNIGYVPQD-VTLFYGTLRDNITLgapladderilrAAELAGVTDFVNKHpNGLDL--QIGERGR------GLSGGQRQA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnlTIVLITHEMHVIrRICDEVAVMESGKVIEHG 223
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.85e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.87 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKnkEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAK 80
Cdd:PRK13648 7 IIVFKNVSFQYQSD--ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHE----MHvirriCDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDlseaME-----ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-238 |
1.98e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 134.83 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKST----LIRMFNhleapTSGEVIIDGDHIGQLSKNGLRAKRQKVSMIFQHFN-LL 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 95 WSR-TVLKNIMFPLEI--AGVPRRRAKQKALELVELVGL--KGREKaYPSELSGGQKQRVGIARALANDPTVLLCDEATS 169
Cdd:PRK15134 376 NPRlNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLdpETRHR-YPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 170 ALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTK 238
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-230 |
2.91e-35 |
|
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: 134.84 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPAL--DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFnLLWSRTVLKNIMFPlEIAGVPR---RRAKQKA--LELVE--------LVGLKGrekaypSELSGGQKQR 148
Cdd:TIGR02203 406 RQVALVSQDV-VLFNDTIANNIAYG-RTEQADRaeiERALAAAyaQDFVDklplgldtPIGENG------VLLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLkiREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQV 228
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALE--RLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
..
gi 446493357 229 FE 230
Cdd:TIGR02203 555 LA 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-221 |
3.01e-35 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 127.97 E-value: 3.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNG---LRAkrQKVSMIFQHFNLLWSRTVL 100
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRA--KHVGFVFQSFMLIPTLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEIL 180
Cdd:PRK10584 107 ENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446493357 181 DLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIE 221
Cdd:PRK10584 187 DLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-232 |
3.37e-35 |
|
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: 131.39 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgQLSKNG--LRAKRQKVSMIFQHFNLLWSRTVLK 101
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTL-FDSRKGifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIMFPLEIAGVPRRRAKQKalELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILD 181
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493357 182 LLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-298 |
1.01e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 129.05 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNK-----------------EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVI 63
Cdd:COG4586 1 IIEVENLSKTYRVYEKepglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 64 IDGdHIGQLSKNGLRakrQKVSMIF-QHFNLLW------SRTVLKnimfplEIAGVPRRRAKQKALELVELVGLKG---- 132
Cdd:COG4586 81 VLG-YVPFKRRKEFA---RRIGVVFgQRSQLWWdlpaidSFRLLK------AIYRIPDAEYKKRLDELVELLDLGElldt 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 133 --REkaypseLSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDE 210
Cdd:COG4586 151 pvRQ------LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 211 VAVMESGKVIEHGPVTQVFEN--PQHTVTKRFvKEDLNDDFETSLTELepLEKDAYIVKLVFAGSTTTEPIVSSLSTAYD 288
Cdd:COG4586 225 VIVIDHGRIIYDGSLEELKERfgPYKTIVLEL-AEPVPPLELPRGGEV--IEREGNRVRLEVDPRESLAEVLARLLARYP 301
|
330
....*....|.
gi 446493357 289 IK-INILEANI 298
Cdd:COG4586 302 VRdLTIEEPPI 312
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-230 |
1.09e-34 |
|
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: 126.57 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtkNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:cd03254 3 IEFENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVglKGREKAYPSE-------LSGGQKQRVGIARA 154
Cdd:cd03254 77 SMIGVVLQD-TFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFI--MKLPNGYDTVlgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnlTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFE 230
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-229 |
1.42e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.46 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVvkEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK 80
Cdd:COG4559 1 MLEAENL--SVRLGGRTLL--DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 R----QKVSMIFqHFnllwsrTVLKNIMFPLEIAGVPRRRAKQ---KALELVELVGLKGRekAYPsELSGGQKQRVGIAR 153
Cdd:COG4559 77 RavlpQHSSLAF-PF------TVEEVVALGRAPHGSSAAQDRQivrEALALVGLAHLAGR--SYQ-TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 154 ALA-------NDPTVLLCDEATSALDP---QTTdeiLDLLlkiRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVIE 221
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLahqHAV---LRLA---RQlaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLVA 220
|
....*...
gi 446493357 222 HGPVTQVF 229
Cdd:COG4559 221 QGTPEEVL 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
1.96e-33 |
|
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: 122.59 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtknkEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSknglRAK 80
Cdd:COG4133 2 MLEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR----EDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFqHFNLLWSR-TVLKNIMFPLEIAGVPRRRAKqkALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG4133 74 RRRLAYLG-HADGLKPElTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLllkIRE--QQNLTIVLITHE 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAEL---IAAhlARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-230 |
2.66e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 124.85 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNK-EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNG-LR 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 AKRQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGR--EKAyPSELSGGQKQRVGIARAL 155
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfwEKS-PFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 156 ANDPTVLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFE 230
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-220 |
3.79e-33 |
|
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: 121.98 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 3 ELKEVVKEYRtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlsknglRAKRQ 82
Cdd:cd03226 1 RIENISFSYK-KGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 83 KVSMIFQHFNL-LWSRTVLKNIMFPLEIAGVPRRRAkQKALELVELVGLKGRekaYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03226 72 SIGYVMQDVDYqLFTDSVREELLLGLKELDAGNEQA-ETVLKDLDLYALKER---HPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
4.48e-33 |
|
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: 122.72 E-value: 4.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTkNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:cd03253 1 IEFENVTFAYDP-GRPVL--KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVglKGREKAYPSE-------LSGGQKQRVGIARA 154
Cdd:cd03253 75 RAIGVVPQD-TVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKI--MRFPDGYDTIvgerglkLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGP 224
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
6.55e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 123.28 E-value: 6.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSG-----EVIIDGDHIgqLSKNGLRAKRQKVSMIFQHFNLlW 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNP-F 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 96 SRTVLKNIMFPLEIAG-VPRRRAKQKALELVELVGL----KGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSA 170
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 171 LDPQTTDEILDLLLKIREQqnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
9.79e-33 |
|
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: 127.40 E-value: 9.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFpleiagvprRRAKQKALEL---VELVGLKGREKAYP-----------SELSGGQKQ 147
Cdd:TIGR02857 396 DQIAWVPQH-PFLFAGTIAENIRL---------ARPDASDAEIreaLERAGLDEFVAALPqgldtpigeggAGLSGGQAQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 148 RVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRiCDEVAVM 214
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-219 |
1.50e-32 |
|
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: 119.24 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVkeYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLsknGLRAKR 81
Cdd:cd03246 1 LEVENVS--FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLwSRTVLKNImfpleiagvprrrakqkalelvelvglkgrekaypseLSGGQKQRVGIARALANDPTV 161
Cdd:cd03246 76 DHVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRiCDEVAVMESGKV 219
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
2.59e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 121.30 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHL-----EAPTSGEVIIDGDHIGQLSKNGLRAKRQkVSMIFQHFNLlW 95
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLRRQ-VSMVHPKPNL-F 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 96 SRTVLKNIMFPLEIAGVPRR-------RAKQKALELVELVGLKGREKAYpsELSGGQKQRVGIARALANDPTVLLCDEAT 168
Cdd:PRK14258 101 PMSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 169 SALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMES-----GKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYV 256
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-241 |
2.60e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 121.31 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHL------EAPTSGEVIIDGDHIGQLSKNGLRakrQKVSMIFQHFNLLWSR 97
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLR---KEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNIMFPLEIAGVPRRRAKQKALE-LVELVGL----KGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALD 172
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 173 PQTTDEILDLLLKIREQqnLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-224 |
4.56e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.69 E-value: 4.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 23 HVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDG-DHigqlsKNGLRAKRqKVSMIFQHFNLLWSRTVLK 101
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqDH-----TTTPPSRR-PVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIMFPLEiagvP--RRRAKQKAL--ELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTD 177
Cdd:PRK10771 91 NIGLGLN----PglKLNAAQREKlhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446493357 178 EILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGP 224
Cdd:PRK10771 167 EMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-224 |
6.04e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 126.22 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglRAKR 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLIL--DDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDV---QAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLwSRTVLKNImfpleIAGVPRrrAKQKALELVELVGLKGREKAYP-------SE----LSGGQKQRVG 150
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENI-----AGGAPL--TLDEAWEAARMAGLAEDIRAMPmgmhtviSEgggtLSGGQRQRLL 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLlkirEQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGP 224
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-230 |
1.65e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 118.65 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYR------------------TKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEV 62
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 63 IIDGDHIGQLSknglrakrqkVSMIFQHfnllwSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGRE----KAYP 138
Cdd:COG1134 84 EVNGRVSALLE----------LGAGFHP-----ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIdqpvKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 139 SelsgGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGK 218
Cdd:COG1134 149 S----GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|..
gi 446493357 219 VIEHGPVTQVFE 230
Cdd:COG1134 224 LVMDGDPEEVIA 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-233 |
1.77e-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: 118.16 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 17 EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIR-MFNHLeAPTSGEVIIDGDHIGQLS-----KNGL------Rakrqkv 84
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPphriaRLGIgyvpegR------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 85 sMIFQHFnllwsrTVLKNIMfpleiAGVPRRRAKQKALELVELVG-----LKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:COG0410 88 -RIFPSL------TVEENLL-----LGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNR-EGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-231 |
1.81e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.96 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtKNKEVLAVDhvnLSIRAGSIYGVIGFSGAGKSTLIRmfnHLEAPTSGEVIIdGDHI----------G 70
Cdd:PRK09984 4 IIRVEKLAKTFN-QHQALHAVD---LNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKSA-GSHIellgrtvqreG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 71 QLSKNgLRAKRQKVSMIFQHFNLLWSRTVLKNIMFPlEIAGVP---------RRRAKQKALELVELVGLKGREKAYPSEL 141
Cdd:PRK09984 76 RLARD-IRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 142 SGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIE 221
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFY 233
|
250
....*....|
gi 446493357 222 HGpVTQVFEN 231
Cdd:PRK09984 234 DG-SSQQFDN 242
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
5.01e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.55 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIdgdhIGQLSKNGLRAKR 81
Cdd:PRK13536 42 IDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV----LGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-242 |
2.19e-30 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 117.60 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAP----TSGEVIIDGDHIGQLSKng 76
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSP-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 77 lRAKRQ----KVSMIFQHFN--LLWSRTVLKNIMFPL---EIAGVPRRR---AKQKALELVELVGLKGRE---KAYPSEL 141
Cdd:PRK15093 81 -RERRKlvghNVSMIFQEPQscLDPSERVGRQLMQNIpgwTYKGRWWQRfgwRKRRAIELLHRVGIKDHKdamRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 142 SGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIE 221
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260
....*....|....*....|.
gi 446493357 222 HGPVTQVFENPQHTVTKRFVK 242
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIR 260
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
2.24e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.63 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKngLRAK 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLW-SRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK13644 76 RKLVGIVFQNPETQFvGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITH---EMHVirriCDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHnleELHD----ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
12-241 |
2.32e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.03 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 12 RTKNKEV-----LAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLE-----APTSGEVIIDGDHIGQLSKNGLRAKR 81
Cdd:PRK14243 12 RTENLNVyygsfLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLYAPDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qKVSMIFQHFNLlWSRTVLKNIMFPLEIAG-------VPRRRAKQKAL--ELvelvglKGREKAYPSELSGGQKQRVGIA 152
Cdd:PRK14243 92 -RIGMVFQKPNP-FPKSIYDNIAYGARINGykgdmdeLVERSLRQAALwdEV------KDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 153 RALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQqnLTIVLITHEMHVIRRICDEVAVMES---------GKVIEHG 223
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFD 241
|
250
....*....|....*...
gi 446493357 224 PVTQVFENPQHTVTKRFV 241
Cdd:PRK14243 242 RTEKIFNSPQQQATRDYV 259
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-224 |
3.94e-30 |
|
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: 114.13 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLsknGLRAKR 81
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVL--KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMfPLEIAGVPRRrakQKALELVEL--------VGLKGREKAYPSELSGGQKQRVGIAR 153
Cdd:cd03244 78 SRISIIPQD-PVLFSGTIRSNLD-PFGEYSDEEL---WQALERVGLkefveslpGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLllkIREQ-QNLTIVLITHEMHVIrrI-CDEVAVMESGKVIEHGP 224
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKT---IREAfKDCTVLTIAHRLDTI--IdSDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-236 |
5.36e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 115.58 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDhigQLSKNGLRAK 80
Cdd:PRK13642 4 ILEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQK---ALELVELVGLKGREkayPSELSGGQKQRVGIARALA 156
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRvdeALLAVNMLDFKTRE---PARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 157 NDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFENPQHTV 236
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMV 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-223 |
5.45e-30 |
|
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: 114.35 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKE-----------------VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVII 64
Cdd:cd03267 1 IEVSNLSKSYRVYSKEpgligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 65 DGDHIGQLSKNGLRakrqKVSMIF-QHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSG 143
Cdd:cd03267 81 AGLVPWKRRKKFLR----RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 144 GQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-227 |
6.00e-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: 114.03 E-value: 6.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHigqLSKNGLRakr 81
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP---WTRKDLH--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPrrraKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:TIGR03740 71 -KIGSLIESPPLYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQ 227
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPE-QGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
6.92e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.41 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtkNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlSKNGLRAK 80
Cdd:COG4604 1 MIEIKNVSKRYG--GKVVL--DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RqkVSMIFQ--HFNllwSR-TVLKNIMFpleiaGvpR------------RRAKQKALELVELVGLKGRekaYPSELSGGQ 145
Cdd:COG4604 76 R--LAILRQenHIN---SRlTVRELVAF-----G--RfpyskgrltaedREIIDEAIAYLDLEDLADR---YLDELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 146 KQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPV 225
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTP 220
|
...
gi 446493357 226 TQV 228
Cdd:COG4604 221 EEI 223
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-217 |
1.09e-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: 113.30 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKN---KEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDH----IGQLS 73
Cdd:COG4778 4 LLEVENLSKTFTLHLqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 74 KNGLRAKRQK----VSmifQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGR-EKAYPSELSGGQKQR 148
Cdd:COG4778 84 PREILALRRRtigyVS---QFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESG 217
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-233 |
1.41e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 116.13 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIdGDHIGQLSKNG--LRAKRQKVSMIFQHFNLLWSRTVLK 101
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGicLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIMFpleiaGVpRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILD 181
Cdd:PRK11144 96 NLRY-----GM-AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493357 182 LLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-232 |
1.54e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.86 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglRAK 80
Cdd:PRK09536 3 MIDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWS---RTVLKNIMFP----LEIAGVPRRRAKQKALELVELVGLKGREKaypSELSGGQKQRVGIAR 153
Cdd:PRK09536 76 SRRVASVPQDTSLSFEfdvRQVVEMGRTPhrsrFDTWTETDRAAVERAMERTGVAQFADRPV---TSLSGGERQRVLLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-223 |
5.00e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.37 E-value: 5.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakrQKVSMIFQHfNLLWSRTV 99
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR---RNIAVVFQD-AGLFNRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 100 LKNIMF------PLEIAGVPRRRAkqkALELVE--------LVGLKGREkaypseLSGGQKQRVGIARALANDPTVLLCD 165
Cdd:PRK13657 426 EDNIRVgrpdatDEEMRAAAERAQ---AHDFIErkpdgydtVVGERGRQ------LSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 166 EATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHG 223
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-219 |
1.39e-28 |
|
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: 110.25 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:cd03248 12 VKFQNVTFAYPTR-PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFPLeiAGVPRRR---AKQKA----------LELVELVGLKGrekaypSELSGGQKQR 148
Cdd:cd03248 88 SKVSLVGQE-PVLFARSLQDNIAYGL--QSCSFECvkeAAQKAhahsfiselaSGYDTEVGEKG------SQLSGGQKQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnlTIVLITHEMHVIRRiCDEVAVMESGKV 219
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-211 |
1.66e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.19 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVvkEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglRAK 80
Cdd:PRK10247 7 LLQLQNV--GYLAGDAKIL--NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---EIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHfNLLWSRTVLKNIMFPLEIAGV-PRRRAKQKALELVELvGLKGREKAYpSELSGGQKQRVGIARALANDP 159
Cdd:PRK10247 80 RQQVSYCAQT-PTLFGDTVYDNLIFPWQIRNQqPDPAIFLDDLERFAL-PDTILTKNI-AELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEV 211
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-241 |
4.65e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.05 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 4 LKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAKRQK 83
Cdd:PRK11000 6 LRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-----NDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 84 VSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQK---ALELVELVGLKGREkayPSELSGGQKQRVGIARALANDPT 160
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRvnqVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 161 VLLCDEATSALDP----QTTDEIldllLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHtv 236
Cdd:PRK11000 154 VFLLDEPLSNLDAalrvQMRIEI----SRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN-- 227
|
....*
gi 446493357 237 tkRFV 241
Cdd:PRK11000 228 --RFV 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-229 |
5.01e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 109.40 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRtkNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSG-EVIIDGDHIGQLSkngLRA 79
Cdd:COG1119 3 LLELRNVTVRRG--GKTIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 KRQK---VSMIFQHfNLLWSRTVLknimfplEIA--------GVPRR---RAKQKALELVELVGLKGREKAYPSELSGGQ 145
Cdd:COG1119 76 LRKRiglVSPALQL-RFPRDETVL-------DVVlsgffdsiGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 146 KQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPV 225
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPK 227
|
....
gi 446493357 226 TQVF 229
Cdd:COG1119 228 EEVL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-238 |
5.70e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.57 E-value: 5.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 11 YRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDG----------DHIGQLSKNGLRAK 80
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 R-QKVSMIFQHfnllwSRTVLkNIMFPL--EIA-------GVPRRRAKQKALELVELVGLKGREKA---YPSELSGGQKQ 147
Cdd:PRK10261 102 RgADMAMIFQE-----PMTSL-NPVFTVgeQIAesirlhqGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 148 RVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQ 227
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQ 255
|
250
....*....|.
gi 446493357 228 VFENPQHTVTK 238
Cdd:PRK10261 256 IFHAPQHPYTR 266
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-222 |
1.13e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 112.70 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHigQLSKNGLRAKRQKVSMIFQHFNLLWSR 97
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTAALAAGVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNIM---FPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQ 174
Cdd:PRK11288 95 TVAENLYlgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446493357 175 TTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEH 222
Cdd:PRK11288 175 EIEQLFRVIRELR-AEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-202 |
1.98e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.25 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKeyrTKNK----EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNG 76
Cdd:COG1101 1 MLELKNLSK---TFNPgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 77 lRAKRqkVSMIFQH------FNLlwsrTVLKNIM--------FPLEIAGVPRRRAK-QKALELVELvGLKGREKAYPSEL 141
Cdd:COG1101 78 -RAKY--IGRVFQDpmmgtaPSM----TIEENLAlayrrgkrRGLRRGLTKKRRELfRELLATLGL-GLENRLDTKVGLL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 142 SGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMH 202
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME 210
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-232 |
4.08e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.16 E-value: 4.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKnkeVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlskNGLRAK 80
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NELEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPR----RRAKQ--KALELVELVGLKgrekayPSELSGGQKQRVGIARA 154
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKaeieERVAEaaRILELEPLLDRK------PRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 155 LANDPTVLLCDEATSALDP----QTTDEILDLllkireQQNL--TIVLITHE----MhvirRICDEVAVMESGKVIEHGP 224
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAklrvQMRLEIQRL------HRRLktTSLYVTHDqveaM----TLADRVVVMNGGVAEQIGT 218
|
....*...
gi 446493357 225 VTQVFENP 232
Cdd:PRK11650 219 PVEVYEKP 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-223 |
5.75e-27 |
|
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: 111.76 E-value: 5.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakrqkvsmifQHFNLL----- 94
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR----------QFINYLpqepy 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 95 -WSRTVLKNImfpleIAGVPRRRAKQKALELVELVGLKGREKAYP-----------SELSGGQKQRVGIARALANDPTVL 162
Cdd:TIGR01193 559 iFSGSILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 163 LCDEATSALDPQTTDEILDLLLKIREQqnlTIVLITHEMHVIRRIcDEVAVMESGKVIEHG 223
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-223 |
5.80e-27 |
|
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: 105.57 E-value: 5.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAKR 81
Cdd:cd03369 7 IEVENLSVRYAPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLwSRTVLKNimfpLEIAGVPRRRAKQKALELVElvglKGrekaypSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03369 82 SSLTIIPQDPTLF-SGTIRSN----LDPFDEYSDEEIYGALRVSE----GG------LNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 162 LLCDEATSALDPQTTDEILDLllkIREQ-QNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHG 223
Cdd:cd03369 147 LVLDEATASIDYATDALIQKT---IREEfTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-232 |
7.87e-27 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 106.80 E-value: 7.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglRAKRQKVSMIFQHFNLLWSRTVLKNI 103
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 M---FPLEIA-GVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEI 179
Cdd:PRK10575 107 AigrYPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493357 180 LDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:PRK10575 187 LALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-223 |
7.90e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 110.88 E-value: 7.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:PRK11176 342 IEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLlWSRTVLKNIMFPleiagvprrRAKQKALELVElvglKGREKAYPSE-------------------LS 142
Cdd:PRK11176 417 NQVALVSQNVHL-FNDTIANNIAYA---------RTEQYSREQIE----EAARMAYAMDfinkmdngldtvigengvlLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 143 GGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEI---LDLLlkireQQNLTIVLITHEMHVIRRiCDEVAVMESGKV 219
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIqaaLDEL-----QKNRTSLVIAHRLSTIEK-ADEILVVEDGEI 556
|
....
gi 446493357 220 IEHG 223
Cdd:PRK11176 557 VERG 560
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-223 |
8.69e-27 |
|
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: 111.07 E-value: 8.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 22 DHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKrqkVSMIFQH---FNllwsRT 98
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA---IGIVPQDtvlFN----DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 99 VLKNIMF------PLEIagvprRRAKQKA--LELVE--------LVG---LKgrekaypseLSGGQKQRVGIARALANDP 159
Cdd:COG5265 448 IAYNIAYgrpdasEEEV-----EAAARAAqiHDFIEslpdgydtRVGergLK---------LSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIReqQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHG 223
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVA--RGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
24-241 |
1.15e-26 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 105.30 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGlRAKR------QKvSMIFQHFnllwsr 97
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAgiayvpQG-REIFPRL------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNIMFPLEIAGVPRRRAKQKALELV----ELVGLKGrekaypSELSGGQKQRVGIARALANDPTVLLCDEATSALDP 173
Cdd:TIGR03410 91 TVEENLLTGLAALPRRSRKIPDEIYELFpvlkEMLGRRG------GDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 174 QTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVfenpQHTVTKRFV 241
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYL 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-229 |
1.46e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 106.24 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 11 YRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgQLSKNGLRAKRQKVSMIFQH 90
Cdd:PRK13638 9 FRYQDEPVL--KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 91 FNL-LWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATS 169
Cdd:PRK13638 86 PEQqIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 170 ALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF 229
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-219 |
1.55e-26 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 110.87 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlsKNGLRAKRQKVSMIFQHFNLLWSRTV 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 100 LKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEI 179
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446493357 180 LDLLLKIREQQnlTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:TIGR01257 1101 WDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-229 |
2.37e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLrAKRqkVSMIFQH---------- 90
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL-ARR--LALLPQHhltpegitvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 91 ---------FNLLWSRTVLKNimfpleiagvprRRAKQKALELVELVGLKGREKaypSELSGGQKQRVGIARALANDPTV 161
Cdd:PRK11231 95 elvaygrspWLSLWGRLSAED------------NARVNQAMEQTRINHLADRRL---TDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 162 LLCDEATSALDPQTTDEILDlLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVF 229
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMR-LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-227 |
5.90e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 107.83 E-value: 5.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTknkeVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNglRAK 80
Cdd:PRK15439 11 LLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA--KAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNIMFpleiaGVPRR-RAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDP 159
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKENILF-----GLPKRqASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 160 TVLLCDEATSALDPQTTDEildLLLKIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQ 227
Cdd:PRK15439 160 RILILDEPTASLTPAETER---LFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-228 |
9.15e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.56 E-value: 9.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNglRAKRQKVSMIFQHFNLLWSR 97
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAAQLGIGIIYQELSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNI----MFPLEIAGVP---RRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSA 170
Cdd:PRK09700 96 TVLENLyigrHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 171 LdpqtTDEILDLLLKIREQ---QNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:PRK09700 176 L----TNKEVDYLFLIMNQlrkEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
1.03e-25 |
|
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: 101.24 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKnglrAKR 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVL--KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLlWSRTVLKNImfpleiagvprrrakqkalelvelvglkGREkaypseLSGGQKQRVGIARALANDPTV 161
Cdd:cd03247 75 SLISVLNQRPYL-FDTTLRNNL----------------------------GRR------FSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqqNLTIVLITHEMHVIRRIcDEVAVMESGKVIEHG 223
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
1.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 103.66 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKevlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAKR 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQH-FNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKG-REKAyPSELSGGQKQRVGIARALANDP 159
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDfRDKP-PYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHG 223
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-223 |
1.54e-25 |
|
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: 101.09 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 5 KEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFN--HLEAPTSGEVIIDGdhigqlSKNGLRAKRQ 82
Cdd:cd03213 11 VTVKSSPSKSGKQLL--KNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING------RPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 83 KVSMIFQHFNLLWSRTVLKNIMFPLEIAGvprrrakqkalelvelvglkgrekaypseLSGGQKQRVGIARALANDPTVL 162
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 163 LCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHE-MHVIRRICDEVAVMESGKVIEHG 223
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-223 |
1.68e-25 |
|
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: 101.84 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNK------------------EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVI 63
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 64 IDGdhigqlsknglrakrqKVSMIFQ-----HFNLlwsrTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLkGREKAYP 138
Cdd:cd03220 81 VRG----------------RVSSLLGlgggfNPEL----TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSEL-GDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 139 -SELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESG 217
Cdd:cd03220 140 vKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKG 218
|
....*.
gi 446493357 218 KVIEHG 223
Cdd:cd03220 219 KIRFDG 224
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-230 |
3.21e-25 |
|
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: 105.99 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakR------QKVSmifqhfnlLWSR 97
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG--RhigylpQDVE--------LFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNI-MFPLEIAgvprrrakQKALELVELVGL--------KGrekaYPSE-------LSGGQKQRVGIARALANDPTV 161
Cdd:COG4618 421 TIAENIaRFGDADP--------EKVVAAAKLAGVhemilrlpDG----YDTRigeggarLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIrRICDEVAVMESGKVIEHGPVTQVFE 230
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
6.53e-25 |
|
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: 99.04 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKngLRAKRQKVSMI---FQHFNLLWS 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSP--RDAIRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 97 RTVLKNIMFPleiagvprrrakqkalelvelvglkgrekaypSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTT 176
Cdd:cd03215 93 LSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446493357 177 DEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:cd03215 141 AEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-223 |
6.80e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.29 E-value: 6.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVvkEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:PRK11160 339 LTLNNV--SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLwSRTVLKNIMFPLEIAGvprrraKQKALELVELVGLK----------------GREkaypseLSGGQ 145
Cdd:PRK11160 414 QAISVVSQRVHLF-SATLRDNLLLAAPNAS------DEALIEVLQQVGLEklleddkglnawlgegGRQ------LSGGE 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 146 KQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIreQQNLTIVLITHEMHVIRRIcDEVAVMESGKVIEHG 223
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
24-241 |
2.61e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 99.62 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKRQKVSM------IFQHfnllwSR 97
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLLrtewgfVHQH-----PR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLK-------NIMFPLEIAGVpR-----RRAKQKALELVELVGlkGREKAYPSELSGGQKQRVGIARALANDPTVLLCD 165
Cdd:PRK11701 100 DGLRmqvsaggNIGERLMAVGA-RhygdiRATAGDWLERVEIDA--ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 166 EATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQHTVTKRFV 241
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLV 252
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
1.11e-23 |
|
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: 101.67 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKrqkVSMIFQ--HfnlLWSR 97
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQdaH---LFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNIMFPLEIAgvprrrAKQKALELVELVGLKGREKAYP-----------SELSGGQKQRVGIARALANDPTVLLCDE 166
Cdd:TIGR02868 424 TVRENLRLARPDA------TDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 446493357 167 ATSALDPQTTDEILDLLLKIreQQNLTIVLITH 199
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-225 |
1.13e-23 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 101.34 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGqlSKNGLRAKRQKVSMIFQHFNLLWSR 97
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEID--FKSSKEALENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKNI---MFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQ 174
Cdd:PRK10982 89 SVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493357 175 TTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPV 225
Cdd:PRK10982 169 EVNHLFTIIRKLKE-RGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPL 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-220 |
4.95e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.20 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEV-----IIDGDHIgqlsknglrAKRQKVSMIFQHFNLL 94
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDI---------ATRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 95 WSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQ 174
Cdd:NF033858 352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446493357 175 TTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVI 220
Cdd:NF033858 432 ARDMFWRLLIELSREDGVTIFISTHFMNEAER-CDRISLMHAGRVL 476
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-230 |
6.11e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.41 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRtKNKEVLAvdHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRakr 81
Cdd:PRK10790 341 IDIDNVSFAYR-DDNLVLQ--NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLwSRTVLKNIMFPLEIAgvprRRAKQKALELVELV--------GLKGREKAYPSELSGGQKQRVGIAR 153
Cdd:PRK10790 415 QGVAMVQQDPVVL-ADTFLANVTLGRDIS----EEQVWQALETVQLAelarslpdGLYTPLGEQGNNLSVGQKQLLALAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQnlTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFE 230
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLA 563
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-233 |
8.45e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.26 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGlRAKRqKVSMIFQHFNLLWSRTVL 100
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARR-GIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMFPLEI-AGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEI 179
Cdd:PRK10895 97 DNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493357 180 LDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK10895 177 KRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-222 |
1.44e-21 |
|
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: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVII-DGDHIGQLSknglra 79
Cdd:COG0488 315 VLELEGLSKSY--GDKTLL--DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFD------ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 krqkvsmifQHFNLL-WSRTVLKNImfpleiagvprRRAKQKALElVELVGLKGR-----EKAY-P-SELSGGQKQRVGI 151
Cdd:COG0488 385 ---------QHQEELdPDKTVLDEL-----------RDGAPGGTE-QEVRGYLGRflfsgDDAFkPvGVLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 152 ARALANDPTVLLCDEATSALDPQTTDEILDLLlkireqQNL--TIVLITHEMHVIRRICDEVAVMESGKVIEH 222
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEAL------DDFpgTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-220 |
3.54e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.23 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTknkeVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFN--HLEAPTSGEVIIDGDhigQLSKNGLR 78
Cdd:PRK13549 5 LLEMKNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEGE---ELQASNIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 AKRQK-VSMIFQHFNLLWSRTVLKNIMFPLEI--AGVPRRRAK-QKALELVELVGLKGREKAYPSELSGGQKQRVGIARA 154
Cdd:PRK13549 78 DTERAgIAIIHQELALVKELSVLENIFLGNEItpGGIMDYDAMyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-231 |
4.38e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.91 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDhigQLSKNGLRAKRQK-VSMIFQHFNLLWS 96
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK---EVTFNGPKSSQEAgIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 97 RTVLKNIMFPLEI----AGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALd 172
Cdd:PRK10762 94 LTIAENIFLGREFvnrfGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 173 pqTTDEILDLLLKIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFEN 231
Cdd:PRK10762 173 --TDTETESLFRVIRElkSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-228 |
6.07e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 89.63 E-value: 6.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 9 KEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMF--NHLEAPTSGEVIIDGDHIGQlsknglrakrqkvsm 86
Cdd:COG2401 36 VELRVVERYVL--RDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGR--------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 87 ifqhfnllwSRTVLKNImfpleiagvPRRRAKQKALELVELVGLKgreKAY-----PSELSGGQKQRVGIARALANDPTV 161
Cdd:COG2401 99 ---------EASLIDAI---------GRKGDFKDAVELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESgkvieHGPVTQV 228
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG-----YGGVPEE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
1.95e-20 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 91.81 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFN--HLEAPTSGEVIIDGDhigQLSKNGLR 78
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGS---PLKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 79 -AKRQKVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAK----QKALELVELVGLKGREKAYP-SELSGGQKQRVGIA 152
Cdd:TIGR02633 74 dTERAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYnamyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 153 RALANDPTVLLCDEATSALDPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-220 |
2.32e-20 |
|
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: 88.10 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 3 ELKEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLI-----RMFNHleAPTSGEVIIDGDhigQLSkngl 77
Cdd:cd03234 5 PWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILFNGQ---PRK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 78 RAKRQK-VSMIFQHFNLLWSRTVLKNIMFPLEIAGvPRRRAKQKALELVELVGLKG------REKAYPSeLSGGQKQRVG 150
Cdd:cd03234 76 PDQFQKcVAYVRQDDILLPGLTVRETLTYTAILRL-PRKSSDAIRKKRVEDVLLRDlaltriGGNLVKG-ISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-228 |
3.00e-20 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 88.72 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRT----------------KNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIID 65
Cdd:PRK13546 5 VNIKNVTKEYRIyrtnkermkdalipkhKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 66 GDhigqlsknglrakrqkVSMIFQHFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQ 145
Cdd:PRK13546 85 GE----------------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 146 KQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPV 225
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
...
gi 446493357 226 TQV 228
Cdd:PRK13546 228 DDV 230
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-232 |
1.10e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 89.77 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAKRQKVSMIfqhfNLLWSRTV 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT----PFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 100 LKNImfpleiaGVPRRRAKQKALELV--------ELVGLKgreKAYPSE-------LSGGQKQRVGIARALANDPTVLLC 164
Cdd:PRK10789 406 ANNI-------ALGRPDATQQEIEHVarlasvhdDILRLP---QGYDTEvgergvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 165 DEATSALDPQTTDEILDLLLKIREQQnlTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFENP 232
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-199 |
1.24e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 12 RTKNKEVLaVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVII-DGDHIGQLSknglrakrQKVSMIFQh 90
Cdd:COG4178 371 RTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP--------QRPYLPLG- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 91 fNLlwsRTVLkniMFPLEIAGVPRRRAKQkALELVELVGLKGR---EKAYPSELSGGQKQRVGIARALANDPTVLLCDEA 167
Cdd:COG4178 441 -TL---REAL---LYPATAEAFSDAELRE-ALEAVGLGHLAERldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|..
gi 446493357 168 TSALDPQTTDEILDLLLkiREQQNLTIVLITH 199
Cdd:COG4178 513 TSALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
24-218 |
1.36e-19 |
|
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: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIR-MFNHLEaPTSGEVIIDGdHIGQLSKNGlrakrqkvsmifqhfnllW--SRTVL 100
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPG-SIAYVSQEP------------------WiqNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMFpleiaGVPRRRAK-QKALELVEL--------------VGLKGrekaypSELSGGQKQRVGIARALANDPTVLLCD 165
Cdd:cd03250 84 ENILF-----GKPFDEERyEKVIKACALepdleilpdgdlteIGEKG------INLSGGQKQRISLARAVYSDADIYLLD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493357 166 EATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGK 218
Cdd:cd03250 153 DPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-199 |
1.38e-19 |
|
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: 85.10 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLsknglRAKRQKVSMIFQHFNLLWSR-TVLKN 102
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-----RDEPHENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 103 IMFPLEIAGVPRRrakqKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQtTDEILDL 182
Cdd:TIGR01189 94 LHFWAAIHGGAQR----TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAG 168
|
170
....*....|....*..
gi 446493357 183 LLKIREQQNLTIVLITH 199
Cdd:TIGR01189 169 LLRAHLARGGIVLLTTH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-220 |
1.56e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 22 DHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGD-HIGQLSknglrakrqkvsmifQHFNLLWSRTVL 100
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlRIGYLP---------------QEPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMfpleiAGVPRRRAKQKALELVEL-------------------------------------VGLKGREKAYP-SELS 142
Cdd:COG0488 80 DTVL-----DGDAELRALEAELEELEAklaepdedlerlaelqeefealggweaearaeeilsgLGFPEEDLDRPvSELS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 143 GGQKQRVGIARALANDPTVLLCDEATSALDPQTTdEILDLLLKireQQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLEEFLK---NYPGTVLVVSHDRYFLDRVATRILELDRGKLT 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-229 |
1.59e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.86 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLrakrqkVSMIFQHFNLLWSRTV 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------VAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 100 L---------KNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAypsELSGGQKQRVGIARALANDPTVLLCDEATSA 170
Cdd:PRK15056 96 LvedvvmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIG---ELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 171 LDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDeVAVMESGKVIEHGPVTQVF 229
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-223 |
2.10e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.41 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLsknGLRAKR 81
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVL--HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQ---------HFNL----------LW---SRTVLKNIMfpleiagvpRRRAKQKALELVElvglkGREKayps 139
Cdd:PLN03130 1313 KVLGIIPQapvlfsgtvRFNLdpfnehndadLWeslERAHLKDVI---------RRNSLGLDAEVSE-----AGEN---- 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 140 eLSGGQKQRVGIARALANDPTVLLCDEATSALDPQTtdeilDLLLK--IREQ-QNLTIVLITHEMHVIrrI-CDEVAVME 215
Cdd:PLN03130 1375 -FSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-----DALIQktIREEfKSCTMLIIAHRLNTI--IdCDRILVLD 1446
|
....*...
gi 446493357 216 SGKVIEHG 223
Cdd:PLN03130 1447 AGRVVEFD 1454
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-221 |
2.47e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 88.69 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFN--HLEAPTSGEVIIDGDhIGQLSknGLRAKRQK-VSMIFQHFNLL 94
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFDGE-VCRFK--DIRDSEALgIVIIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 95 WSRTVLKNIMFPLEIA--GV-PRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSAL 171
Cdd:NF040905 91 PYLSIAENIFLGNERAkrGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493357 172 DPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVIE 221
Cdd:NF040905 171 NEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-220 |
3.82e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 20 AVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDG-----DHIGQLSKNGL------RaKRQkvsmif 88
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpvriRSPRDAIRAGIayvpedR-KGE------ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 89 qhfNLLWSRTVLKNIMFP----LEIAG-VPRRRAKQKALELVELVGLKGREKAYP-SELSGGQKQRVGIARALANDPTVL 162
Cdd:COG1129 340 ---GLVLDLSIRENITLAsldrLSRGGlLDRRRERALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 163 LCDEATSALDPQTTDEILDLllkIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:COG1129 417 ILDEPTRGIDVGAKAEIYRL---IRElaAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-220 |
4.25e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.77 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 18 VLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK--------RQKV----- 84
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRglvpd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 85 -----SMIFQHFNL--LWSRTVLKnimfpleiagvpRRRAKQKALELVELVGLKGREKAYP-SELSGGQKQRVGIARALA 156
Cdd:COG3845 351 msvaeNLILGRYRRppFSRGGFLD------------RKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 157 NDPTVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-205 |
7.51e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.78 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHigQLSKNGLRAKR 81
Cdd:PTZ00265 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHfNLLWSRTVLKNIMFPL---------------------------------------------EIAGVPRRR 116
Cdd:PTZ00265 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 117 AKQKALELVELVGLKGRE------KAYP-----------SELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEI 179
Cdd:PTZ00265 539 KNYQTIKDSEVVDVSKKVlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260
....*....|....*....|....*.
gi 446493357 180 LDLLLKIREQQNLTIVLITHEMHVIR 205
Cdd:PTZ00265 619 QKTINNLKGNENRITIIIAHRLSTIR 644
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-243 |
1.80e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 83.88 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 22 DHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLrAKRqkVSMIFQHFNLLWSRTVLK 101
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV-ARR--IGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIM---FPLEIAGVPRRRAKQKAL-ELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTD 177
Cdd:PRK10253 101 LVArgrYPHQPLFTRWRKEDEEAVtKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 178 EILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPvtqvfenPQHTVTKRFVKE 243
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA-------PKEIVTAELIER 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-223 |
2.07e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 86.72 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 23 HVNLSIRAGSIYGVIGFSGAGKSTLIR-MFNHLEAPTSGEVIIdgdhigqlskNGLRAKRQKVSMIFqhfnllwSRTVLK 101
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI----------RGTVAYVPQVSWIF-------NATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIMFpleiaGVPRRRAK-QKALELVELVG----LKGREKAYPSE----LSGGQKQRVGIARALANDPTVLLCDEATSALD 172
Cdd:PLN03130 698 NILF-----GSPFDPERyERAIDVTALQHdldlLPGGDLTEIGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493357 173 PQTTDEILDLLLKiREQQNLTIVLITHEMHVIRRIcDEVAVMESGKVIEHG 223
Cdd:PLN03130 773 AHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-223 |
2.76e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.67 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRM---FnhleAPTSGEVIIDGDHIGQLSkngLRAKRQKVSMIFQHFNLLWSrTVL 100
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNAllgF----LPYQGSLKINGIELRELD---PESWRKHLSWVGQNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMFPLEIAGVPRRR---AKQKALELVELV--GLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQT 175
Cdd:PRK11174 441 DNVLLGNPDASDEQLQqalENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446493357 176 TDEILDLLLKIREQQnlTIVLITHEMHVIRRiCDEVAVMESGKVIEHG 223
Cdd:PRK11174 521 EQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-219 |
3.52e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 16 KEVLAVD--------HVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLS-KNGLRA------- 79
Cdd:PRK15439 266 APVLTVEdltgegfrNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARglvylpe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 80 KRQkVSMIFQHFNLLWSRTVLKNIMFPLEIagvprRRAKQKALelVE----LVGLKGREKAYPSE-LSGGQKQRVGIARA 154
Cdd:PRK15439 346 DRQ-SSGLYLDAPLAWNVCALTHNRRGFWI-----KPARENAV--LEryrrALNIKFNHAEQAARtLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
1.27e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNglRAK 80
Cdd:PRK11614 5 MLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLLWSRTVLKNimfpLEIAG--VPRRRAKQKALELVELVG-LKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEEN----LAMGGffAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-207 |
2.23e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.46 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 22 DHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEViidgdhigqlSKNGLRAKRQKVSMifqHFNLLW------ 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV----------LWQGEPIRRQRDEY---HQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 96 ---SRTVLKNIMFPLEIAGVPRRRAKQKALELVelvGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALD 172
Cdd:PRK13538 85 iktELTALENLRFYQRLHGPGDDEALWEALAQV---GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446493357 173 PQTTDEILDLLLKiREQQNLTIVLITH-EMHVI----RRI 207
Cdd:PRK13538 162 KQGVARLEALLAQ-HAEQGGMVILTTHqDLPVAsdkvRKL 200
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-223 |
2.50e-17 |
|
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: 83.46 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLAvdHVNLSIRAGSIYGVIGFSGAGKSTL-IRMFNHLEApTSGEVIIDGDHIGQLsknGLRAK 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLR--HINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINES-AEGEIIIDGLNIAKI---GLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHfNLLWSRTVLKNiMFPLEiagvprRRAKQKALELVELVGLKGREKAYPSE-----------LSGGQKQRV 149
Cdd:TIGR00957 1359 RFKITIIPQD-PVLFSGSLRMN-LDPFS------QYSDEEVWWALELAHLKTFVSALPDKldhecaeggenLSVGQRQLV 1430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 150 GIARALANDPTVLLCDEATSALDPQTTDEILDlllKIREQ-QNLTIVLITHEMHVIRRICdEVAVMESGKVIEHG 223
Cdd:TIGR00957 1431 CLARALLRKTKILVLDEATAAVDLETDNLIQS---TIRTQfEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-227 |
3.43e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 28 IRAGSIYGVIGFSGAGKSTLIRMFNHLEAP---TSGEVIIDGDHIGqlsknglRAKRQKVSMIFQHFNLLW-SRTVLKNI 103
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID-------AKEMRAISAYVQQDDLFIpTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 MFPLEIAgVPRRRAKQKALELVE--------------LVGLKGREKAypseLSGGQKQRVGIARALANDPTVLLCDEATS 169
Cdd:TIGR00955 121 MFQAHLR-MPRRVTKKEKRERVDevlqalglrkcantRIGVPGRVKG----LSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 170 ALDPQTTDEILDLLLKIrEQQNLTIVLITHE-MHVIRRICDEVAVMESGKVIEHGPVTQ 227
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
4.11e-17 |
|
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: 77.10 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIidgdhigqlsknglRAKR 81
Cdd:cd03221 1 IELENLSKTY--GGKLLL--KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT--------------WGST 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVsmifqhfnllwsrtvlknimfpleiagvprrrakqkalelvelvglkgrekAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:cd03221 63 VKI---------------------------------------------------GYFEQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 162 LLCDEATSALDPQTTDEILDLLlkirEQQNLTIVLITHEMHVIRRICDEVAVMESGK 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-233 |
5.32e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 82.13 E-value: 5.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLsknGLRAKRQKVSMIFQHfNLLWSRTVLKNI 103
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLRELRRQFSMIPQD-PVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 MFPLEIAGVPRRRAkqkalelVELVGLKGReKAYPSE------LSG------GQKQRVGIARA-LANDPTVLLCDEATSA 170
Cdd:PTZ00243 1405 DPFLEASSAEVWAA-------LELVGLRER-VASESEgidsrvLEGgsnysvGQRQLMCMARAlLKKGSGFILMDEATAN 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 171 LDPQTTDEILDLLLKirEQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PTZ00243 1477 IDPALDRQIQATVMS--AFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-242 |
5.46e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 82.38 E-value: 5.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 59 SGEVIIDGDHIGQLSkngLRAKRQKVSMIFQHfNLLWSRTVLKNIMFPLEIAGVP--RRRAKQKAL-ELVELVGLKGREK 135
Cdd:PTZ00265 1276 SGKILLDGVDICDYN---LKDLRNLFSIVSQE-PMLFNMSIYENIKFGKEDATREdvKRACKFAAIdEFIESLPNKYDTN 1351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 136 A--YPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAV 213
Cdd:PTZ00265 1352 VgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
170 180 190
....*....|....*....|....*....|...
gi 446493357 214 M----ESGKVIEHGPVTQVFENPQHTVTKRFVK 242
Cdd:PTZ00265 1431 FnnpdRTGSFVQAHGTHEELLSVQDGVYKKYVK 1463
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-234 |
1.17e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 78.72 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMF-NHLEAPT-------SGEVIIDGDHIGQLSKNGLRAKRQKVSMIFQHFN 92
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 93 LLWSRTVLKNIMFP-LEIAGVPRRRAKQ---KALELVELVGLKGREKaypSELSGGQKQRVGIARALAN---------DP 159
Cdd:PRK13547 97 AFSAREIVLLGRYPhARRAGALTHRDGEiawQALALAGATALVGRDV---TTLSGGELARVQFARVLAQlwpphdaaqPP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQVFEnPQH 234
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT-PAH 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-199 |
2.92e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 15 NKEVLAvdHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDG------DHIGQLS----KNGLRAkrqkv 84
Cdd:PRK13539 14 GRVLFS--GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpDVAEACHylghRNAMKP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 85 smifqhfNLlwsrTVLKNIMFPLEIAGVPRRRAkQKALELVELVGLKGREKAYpseLSGGQKQRVGIARALANDPTVLLC 164
Cdd:PRK13539 87 -------AL----TVAENLEFWAAFLGGEELDI-AAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 446493357 165 DEATSALDPqTTDEILDLLLKIREQQNLTIVLITH 199
Cdd:PRK13539 152 DEPTAALDA-AAVALFAELIRAHLAQGGIVIAATH 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-221 |
7.91e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.09 E-value: 7.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAKR 81
Cdd:PRK10522 323 LELRNVTFAYQDNG---FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFNLLwsRTVLKNIMFPLEIAGVprrRAKQKALELVELVGLKGrEKAYPSELSGGQKQRVGIARALANDPTV 161
Cdd:PRK10522 397 KLFSAVFTDFHLF--DQLLGPEGKPANPALV---EKWLERLKMAHKLELED-GRISNLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 162 LLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIE 221
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-217 |
1.16e-15 |
|
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: 78.52 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEvlAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlsknglrak 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----------- 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHF----------NLLWSRtvlKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVG 150
Cdd:TIGR01257 2004 LTNISDVHQNMgycpqfdaidDLLTGR---EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLS 2080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 151 IARALANDPTVLLCDEATSALDPQTTDEILDLLLK-IREQQnlTIVLITHEMHVIRRICDEVAVMESG 217
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGR--AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-211 |
1.80e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYrtKNKEVLAvdHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIidgdhigqlsknglRAK 80
Cdd:PRK09544 4 LVSLENVSVSF--GQRRVLS--DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHFNLlwsrtvlkNIMFPLEIAGVPRRRAKQK------ALELVELVGLKgreKAYPSELSGGQKQRVGIARA 154
Cdd:PRK09544 66 KLRIGYVPQKLYL--------DTTLPLTVNRFLRLRPGTKkedilpALKRVQAGHLI---DAPMQKLSGGETQRVLLARA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEV 211
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
262-338 |
2.98e-15 |
|
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 197998 [Multi-domain] Cd Length: 76 Bit Score: 69.85 E-value: 2.98e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 262 DAYIVKLVFAGSTTTEPIVSSLSTAYDIKINILEANIKNTKNGTVGFLVLHIPyISSVDFGKFEKELIERQVKMEVL 338
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELT-GDEEDIEAALAYLREQGVEVEVL 76
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-229 |
4.47e-15 |
|
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: 73.79 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAkr 81
Cdd:cd03288 20 IKIHDLCVRYENNLKPVL--KHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qKVSMIFQHfNLLWSRTvlknIMFPLEiagvPRRRAKQKAL-ELVELVGLKGREKAYPSEL-----------SGGQKQRV 149
Cdd:cd03288 96 -RLSIILQD-PILFSGS----IRFNLD----PECKCTDDRLwEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 150 GIARALANDPTVLLCDEATSALDpQTTDEILDLLLkIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGPVTQVF 229
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-225 |
4.51e-15 |
|
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: 72.56 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 11 YRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTL--IRMFNHLEAPTSGEVIIDGDHIGQLSKNgLRAKRqKVSMIF 88
Cdd:cd03217 8 VSVGGKEIL--KGVNLTIKKGEVHALMGPNGSGKSTLakTIMGHPKYEVTEGEILFKGEDITDLPPE-ERARL-GIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 89 QHfnllwsrtvlknimfPLEIAGVprrrakqKALELVELVGLKgrekaypseLSGGQKQRVGIARALANDPTVLLCDEAT 168
Cdd:cd03217 84 QY---------------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 169 SALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRI-CDEVAVMESGKVIEHGPV 225
Cdd:cd03217 133 SGLDIDALRLVAEVINKLRE-EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-207 |
4.57e-15 |
|
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: 72.91 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLsknglRAKRQKVSMIFQHFNLLWSR-TVLKN 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ-----RDSIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 103 IMFPLEIAGvprrraKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDL 182
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170 180 190
....*....|....*....|....*....|
gi 446493357 183 LLKiREQQNLTIVLITH-----EMHVIRRI 207
Cdd:cd03231 168 MAG-HCARGGMVVLTTHqdlglSEAGAREL 196
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-199 |
4.82e-15 |
|
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: 71.80 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHigqlsknglrakrqkvsmifqhfnllwsrtvl 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 kNIMFpleiagVPRRrAKQKALELVELVglkgrekAYP--SELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDE 178
Cdd:cd03223 65 -DLLF------LPQR-PYLPLGTLREQL-------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 446493357 179 ILDLLlkirEQQNLTIVLITH 199
Cdd:cd03223 130 LYQLL----KELGITVISVGH 146
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-222 |
8.57e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.78 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 1 MIELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlSKNGLRAK 80
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVL--HGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV---AKFGLTDL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVSMIFQHfNLLWSRTVLKNIMFPLEIAGVPRRRAKQKAlELVELV-----GLKGREKAYPSELSGGQKQRVGIARAL 155
Cdd:PLN03232 1309 RRVLSIIPQS-PVLFSGTVRFNIDPFSEHNDADLWEALERA-HIKDVIdrnpfGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 156 ANDPTVLLCDEATSALDPQTtdeilDLLLK--IREQ-QNLTIVLITHEMHVIRRiCDEVAVMESGKVIEH 222
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRT-----DSLIQrtIREEfKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEY 1450
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-231 |
9.05e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.40 E-value: 9.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIR-MFNHLEAPTSGEVIIDGDhigqlsknglRAKRQKVSMIFqhfnllwSRTVLKN 102
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS----------VAYVPQVSWIF-------NATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 103 IMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSE----LSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDE 178
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446493357 179 ILDLLLKiREQQNLTIVLITHEMHVIRRIcDEVAVMESGKVIEHGPVTQVFEN 231
Cdd:PLN03232 779 VFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-228 |
3.82e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.46 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtknKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIrMFNHLEAPTSGEVIIdgdHIGQLSKNgLRAKR 81
Cdd:NF000106 14 VEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPW---RF*TWCAN-RRALR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMifqHFNLLWSR----TVLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALAN 157
Cdd:NF000106 85 RTIG*---HRPVR*GRresfSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDlllKIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWD---EVRSmvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-219 |
4.47e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLS-KNGLRAKRQKVSMIFQHFNLLWSRTV 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 100 LKNIMFPL-----EIAGVPRRRAKQKALE-LVELVGLK--GREKAYpSELSGGQKQRVGIARALANDPTVLLCDEATSAL 171
Cdd:PRK10762 348 KENMSLTAlryfsRAGGSLKHADEQQAVSdFIRLFNIKtpSMEQAI-GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446493357 172 DPQTTDEILDLLLKIReQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PRK10762 427 DVGAKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-208 |
1.94e-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: 71.12 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIdGDHIgqlsknglrakr 81
Cdd:TIGR03719 323 IEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 qKVSMIFQ-HFNLLWSRTVLKNIMFPLEIAGVPRRRAKQKAleLVELVGLKGREKAYP-SELSGGQKQRVGIARALANDP 159
Cdd:TIGR03719 386 -KLAYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGG 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493357 160 TVLLCDEATSALDPQTTDEILDLLLKIREqqnlTIVLITHEMHVIRRIC 208
Cdd:TIGR03719 463 NVLLLDEPTNDLDVETLRALEEALLNFAG----CAVVISHDRWFLDRIA 507
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-219 |
2.25e-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: 70.62 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 3 ELKEVVKE------YRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIR-MFNHLEAPTSGEVIIDGDHIGqlSKN 75
Cdd:TIGR02633 252 EIGDVILEarnltcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 76 GLRAKRQKVSMI---FQHFNLLWSRTVLKNIMFPL--EIAGVPR--RRAKQKAL-ELVELVGLKGREKAYP-SELSGGQK 146
Cdd:TIGR02633 330 PAQAIRAGIAMVpedRKRHGIVPILGVGKNITLSVlkSFCFKMRidAAAELQIIgSAIQRLKVKTASPFLPiGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 147 QRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-229 |
3.23e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 68.33 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 19 LAVDH----VNLSIRAGSIYGVIGFSGAGKSTLI-RMFNHLeaPTSGEVIIDGDHIGQLSKNGLRAKRqkvSMIFQHFNL 93
Cdd:COG4138 6 VAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 94 LWSRTVLKNIMfpLEIAGVPRRRAKQKAL-ELVELVGLkgrEKAYP---SELSGGQKQRVGIARALAN-DPTV------L 162
Cdd:COG4138 81 PFAMPVFQYLA--LHQPAGASSEAVEQLLaQLAEALGL---EDKLSrplTQLSGGEWQRVRLAAVLLQvWPTInpegqlL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 163 LCDEATSALD--PQTTdeiLDLLLKIREQQNLTIVLITHEM-HVIRRiCDEVAVMESGKVIEHGPVTQVF 229
Cdd:COG4138 156 LLDEPMNSLDvaQQAA---LDRLLRELCQQGITVVMSSHDLnHTLRH-ADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
28-174 |
1.36e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 28 IRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGqlsknglRAKRQKVSMIFQHF-NLLWSRTVLKNIMFp 106
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-------RGDRSRFMAYLGHLpGLKADLSTLENLHF- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 107 leIAGVPRRRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQ 174
Cdd:PRK13543 106 --LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
265-337 |
2.09e-12 |
|
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 462781 [Multi-domain] Cd Length: 73 Bit Score: 61.70 E-value: 2.09e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 265 IVKLVFAGSTTTEPIVSSLSTAYDIKINILEANIKNTKNGTVGFLVLHIPYiSSVDFGKFEKELIERQVKMEV 337
Cdd:pfam09383 2 LVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPG-DPEQIEAALAYLREQGVEVEV 73
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-226 |
3.64e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 14 KNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMF-NHleaP----TSGEVIIDGDHIGQLSKNgLRAKRQkvsmIF 88
Cdd:CHL00131 18 NENEIL--KGLNLSINKGEIHAIMGPNGSGKSTLSKVIaGH---PaykiLEGDILFKGESILDLEPE-ERAHLG----IF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 89 QHFNllwsrtvlknimFPLEIAGVPRR-------RAKQKALELVE---------------LVGLKgrekayPSEL----- 141
Cdd:CHL00131 88 LAFQ------------YPIEIPGVSNAdflrlayNSKRKFQGLPEldplefleiineklkLVGMD------PSFLsrnvn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 142 ---SGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRIC-DEVAVMESG 217
Cdd:CHL00131 150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYVHVMQNG 228
|
....*....
gi 446493357 218 KVIEHGPVT 226
Cdd:CHL00131 229 KIIKTGDAE 237
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-233 |
4.39e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.95 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLI-RMFNHLeaPTSGEVIIDGDHIGQLSKNGLRAKRQKVSmifQHFNLLWSRTVLKn 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLEAWSAAELARHRAYLS---QQQTPPFAMPVFQ- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 103 iMFPLEIAGVPRRRAKQKAL-ELVELVGLKGREKAYPSELSGGQKQRVGIARA-LANDPTV------LLCDEATSALDpQ 174
Cdd:PRK03695 89 -YLTLHQPDKTRTEAVASALnEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLD-V 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 175 TTDEILDLLLKIREQQNLTIVLITHEM-HVIRRiCDEVAVMESGKVIEHGPVTQVFENPQ 233
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-231 |
4.93e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.84 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEV----------------LAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIID 65
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFdklkdlffrskdgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 66 GDHIGQLSKNGLRAKRQKVSMIfqhfnllwsrtVLKNIMFpleiaGVPRRRAKQKALELVELVGLkGREKAYPSE-LSGG 144
Cdd:PRK13545 85 GSAALIAISSGLNGQLTGIENI-----------ELKGLMM-----GLTKEKIKEIIPEIIEFADI-GKFIYQPVKtYSSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 145 QKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRICDEVAVMESGKVIEHGP 224
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
....*..
gi 446493357 225 VTQVFEN 231
Cdd:PRK13545 227 IKEVVDH 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-223 |
5.64e-12 |
|
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: 64.74 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 27 SIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQlsknglraKRQKVS---------MIFQHFNLLWSR 97
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--------KPQYIKadyegtvrdLLSSITKDFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 98 TVLKN-IMFPLEIAGVPRRRAkqkalelvelvglkgrekaypSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTT 176
Cdd:cd03237 93 PYFKTeIAKPLQIEQILDREV---------------------PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446493357 177 DEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMEsGKVIEHG 223
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNG 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-231 |
7.05e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLS-----KNGLR--AKRQKVSMIFQHF-- 91
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavKKGMAyiTESRRDNGFFPNFsi 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 92 --NLLWSRTvLKNIMFPLEIAGVPRRRAKQKALELVELVGLKGRE-KAYPSELSGGQKQRVGIARALANDPTVLLCDEAT 168
Cdd:PRK09700 359 aqNMAISRS-LKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 169 SALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKviehgpVTQVFEN 231
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGR------LTQILTN 493
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-219 |
7.38e-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: 66.47 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLeAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVL--QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT---LQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFnLLWSRTVLKNiMFPLEiagvprRRAKQKALELVELVGLKGREKAYPSEL-----------SGGQKQRVG 150
Cdd:TIGR01271 1292 KAFGVIPQKV-FIFSGTFRKN-LDPYE------QWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMC 1363
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 151 IARALANDPTVLLCDEATSALDPqTTDEILDLLLKiREQQNLTIVLITHEMHVIRRiCDEVAVMESGKV 219
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLK-QSFSNCTVILSEHRVEALLE-CQQFLVIEGSSV 1429
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
5-217 |
3.06e-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: 62.35 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 5 KEVVKEYRTKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLRAK-RQK 83
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 84 VSMIFQHFNLLwSRTVLKNIMFpleiaGVPRRRAKQKALelVELVGLKGREKAYPS-----------ELSGGQKQRVGIA 152
Cdd:cd03290 81 VAYAAQKPWLL-NATVEENITF-----GSPFNKQRYKAV--TDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 153 RALANDPTVLLCDEATSALDPQTTDEILDL-LLKIREQQNLTIVLITHEMHVIRRiCDEVAVMESG 217
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-224 |
3.74e-11 |
|
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: 64.58 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGdhigqlsknglrakrqKVSMIFQHfnlLWSR--TVLK 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------------SVAYVPQQ---AWIQndSLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 NIMF--PLEiagVPRRRAKQKALELV-ELVGLKGREKAYPSE----LSGGQKQRVGIARALANDPTVLLCDEATSALDPQ 174
Cdd:TIGR00957 718 NILFgkALN---EKYYQQVLEACALLpDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493357 175 TTDEILDLLLKIREQ-QNLTIVLITHEMHVIRRIcDEVAVMESGKVIEHGP 224
Cdd:TIGR00957 795 VGKHIFEHVIGPEGVlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-219 |
9.76e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 9.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 17 EVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEV-IIDGDHIGQLSKNGLRAKRQKVSMIfQHfnllw 95
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRADESPL-QH----- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 96 srtvlknimfpleIAGVPRRRAKQKALELVELVGLKGREKAYPSE-LSGGQKQRVGIARALANDPTVLLCDEATSALDpq 174
Cdd:PRK10636 398 -------------LARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD-- 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493357 175 ttdeiLDLllkireQQNLT---------IVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PRK10636 463 -----LDM------RQALTealidfegaLVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-219 |
1.05e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIR-MFNHLEAPTSGEVIIDGDHIGqlSKNGLRAKRQKVSMIFQ---HFNLLWS 96
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVK--IRNPQQAIAQGIAMVPEdrkRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 97 RTVLKNIMFP----LEIAGVPRRRAKQKALElVELVGLKGReKAYP----SELSGGQKQRVGIARALANDPTVLLCDEAT 168
Cdd:PRK13549 356 MGVGKNITLAaldrFTGGSRIDDAAELKTIL-ESIQRLKVK-TASPelaiARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446493357 169 SALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-219 |
1.27e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLS-KNGLRA------KRQKVSMIFQHfnllws 96
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAgimlcpEDRKAEGIIPV------ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 97 RTVLKNImfplEI--------AG--VPRRRAKQKALELVELVGLKGREKAYP-SELSGGQKQRVGIARALANDPTVLLCD 165
Cdd:PRK11288 346 HSVADNI----NIsarrhhlrAGclINNRWEAENADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446493357 166 EATSALDPQTTDEILDLLLKIREqQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-175 |
1.93e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKnkevLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIdGD-----HIGQlSKNG 76
Cdd:PRK11819 325 IEAENLSKSFGDR----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvklaYVDQ-SRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 77 LRAKrqkvsmifqhfnllwsRTVLKNIMFPLEIAGVPRRRAKQKAleLVELVGLKGREKAYP-SELSGGQKQRVGIARAL 155
Cdd:PRK11819 399 LDPN----------------KTVWEEISGGLDIIKVGNREIPSRA--YVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTL 460
|
170 180
....*....|....*....|
gi 446493357 156 ANDPTVLLCDEATSALDPQT 175
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDVET 480
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-219 |
1.17e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIR-MFNHLEApTSGEVIidgdhigqlsknglrAKRQkVSMIFQHfnlLW--SRTVL 100
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEGRVW---------------AERS-IAYVPQQ---AWimNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIMF-----PLEIAGVPRrrAKQKALELVEL-------VGLKGrekaypSELSGGQKQRVGIARALANDPTVLLCDEAT 168
Cdd:PTZ00243 739 GNILFfdeedAARLADAVR--VSQLEADLAQLgggleteIGEKG------VNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446493357 169 SALDPQTTDEIL-DLLL-----KIReqqnltiVLITHEMHVIRRiCDEVAVMESGKV 219
Cdd:PTZ00243 811 SALDAHVGERVVeECFLgalagKTR-------VLATHQVHVVPR-ADYVVALGDGRV 859
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-219 |
1.80e-09 |
|
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: 57.94 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRTKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLeAPTSGEVIIDGDHIGQLSkngLRAKR 81
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVL--ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP---LQKWR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 82 QKVSMIFQHFnLLWSRTVLKNimfpLEIAGvprRRAKQKALELVELVGLKGREKAYPSEL-----------SGGQKQRVG 150
Cdd:cd03289 77 KAFGVIPQKV-FIFSGTFRKN----LDPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMC 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 151 IARALANDPTVLLCDEATSALDPqTTDEILDLLLKiREQQNLTIVLITHEMHVIRRiCDEVAVMESGKV 219
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLK-QAFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-218 |
1.90e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 25 NLSIR--AGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIID-GDHIGQLSKNglrakrqkvSMIFQHFNLLwsRTVlk 101
Cdd:PRK15064 19 NISVKfgGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQD---------QFAFEEFTVL--DTV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 nIMFPLEIAGVPRRR-------------------------------AKQKALELVELVGLkGREKAYP--SELSGGQKQR 148
Cdd:PRK15064 86 -IMGHTELWEVKQERdriyalpemseedgmkvadlevkfaemdgytAEARAGELLLGVGI-PEEQHYGlmSEVAPGWKLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 149 VGIARALANDPTVLLCDEATSALDPQTTDEILDLLlkirEQQNLTIVLITHEMHVIRRICDEVAVMESGK 218
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL----NERNSTMIIISHDRHFLNSVCTHMADLDYGE 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-172 |
2.37e-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: 58.64 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 29 RAGSIYGVIGFSGAGKSTLIRM--------FNHLEAPTSGEVIID-------GDHIGQLSKNGLRA--KRQKVSMIFQHF 91
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKIlsgelkpnLGDYDEEPSWDEVLKrfrgtelQDYFKKLANGEIKVahKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 92 NLLwSRTVLKNImfpleiagvprrRAKQKALELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSAL 171
Cdd:COG1245 177 KGT-VRELLEKV------------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
.
gi 446493357 172 D 172
Cdd:COG1245 244 D 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
23-219 |
2.70e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.33 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 23 HVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEViidgdhigqlskngLRAKRQKVSMIFQHF--NLLWSRTVL 100
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHHvdGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNIM--FPleiaGVPrrraKQKALELVELVGLKGREKAYPS-ELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTD 177
Cdd:PLN03073 593 LYMMrcFP----GVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE 664
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446493357 178 EILDLLLKIREqqnlTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PLN03073 665 ALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-222 |
2.88e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 28 IRAGSIYGVIGFSGAGKSTLIRM--------FNHLEAPTSGEVIID-------GDHIGQLSKNGLRA--KRQKVSMIFQH 90
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKIlsgelipnLGDYEEEPSWDEVLKrfrgtelQNYFKKLYNGEIKVvhKPQYVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 91 FNLLwSRTVLKNImfpleiagvprrRAKQKALELVELVGLK---GREKaypSELSGGQKQRVGIARALANDPTVLLCDEA 167
Cdd:PRK13409 176 FKGK-VRELLKKV------------DERGKLDEVVERLGLEnilDRDI---SELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 168 TSALDpqttdeildlllkIREQQNLTIvlithemhVIRRICDEVAVMesgkVIEH 222
Cdd:PRK13409 240 TSYLD-------------IRQRLNVAR--------LIRELAEGKYVL----VVEH 269
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-220 |
6.91e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 22 DHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGD---------------------------HIGQLSK 74
Cdd:PRK11147 20 DNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlivarlqqdpprnvegtvydfvaegieEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 75 NGLRAKRQkVSMIFQHFNLlwsrTVLKNIMFPLEIAGVPRRRAKQKalELVELVGLKGREKAypSELSGGQKQRVGIARA 154
Cdd:PRK11147 100 RYHDISHL-VETDPSEKNL----NELAKLQEQLDHHNLWQLENRIN--EVLAQLGLDPDAAL--SSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446493357 155 LANDPTVLLCDEATSALDPQTTDEILDLLLKIREqqnlTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-212 |
7.88e-09 |
|
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: 56.87 E-value: 7.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 15 NKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIdgdhigqlsknglrAKRQKVSMIFQHFNLL 94
Cdd:TIGR03719 17 KKEIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--------------QPGIKVGYLPQEPQLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 95 WSRTVLKNIMfpleiAGVPRRRAKQKALELV------------ELVGLKGR-----------------EKAY-----P-- 138
Cdd:TIGR03719 81 PTKTVRENVE-----EGVAEIKDALDRFNEIsakyaepdadfdKLAAEQAElqeiidaadawdldsqlEIAMdalrcPpw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 139 ----SELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEIldlllkireQQNL-----TIVLITHEmhviRRICD 209
Cdd:TIGR03719 156 dadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL---------ERHLqeypgTVVAVTHD----RYFLD 222
|
...
gi 446493357 210 EVA 212
Cdd:TIGR03719 223 NVA 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-200 |
9.32e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 9.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 19 LAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIgqlsKNGLRAKRQKVSMIFQHFNLLWSRT 98
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 99 VLKNIMFPLEIAgvprrrakQKALELVELVGLKGREKA--YPSE-LSGGQKQRVGIARALANDPTVLLCDEATSALDPQT 175
Cdd:PRK13540 91 LRENCLYDIHFS--------PGAVGITELCRLFSLEHLidYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....*..
gi 446493357 176 tdeILDLLLKIREQ--QNLTIVLITHE 200
Cdd:PRK13540 163 ---LLTIITKIQEHraKGGAVLLTSHQ 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-217 |
1.04e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEViidgDHIGQLSKNglrakrqkvsmifQHFNLLWSRTVLKNI 103
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----KHSGRISFS-------------PQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 MFPLEIAGVpRRRAKQKALELVE-LVGLKGREKAYPSE----LSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDE 178
Cdd:TIGR01271 508 IFGLSYDEY-RYTSVIKACQLEEdIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190
....*....|....*....|....*....|....*....
gi 446493357 179 ILDLLLkIREQQNLTIVLITHEMHVIRRiCDEVAVMESG 217
Cdd:TIGR01271 587 IFESCL-CKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-173 |
1.12e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYrtKNKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMF---------NHL----EAPTSGEVIID-GD 67
Cdd:PRK10938 261 IVLNNGVVSY--NDRPIL--HNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgRRRGSGETIWDiKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 68 HIGQLSkNGLrakrqkvsmifqHFNLLWSRTVLKNIM--FPLEIaGVPRR---RAKQKALELVELVGLKGREKAYP-SEL 141
Cdd:PRK10938 337 HIGYVS-SSL------------HLDYRVSTSVRNVILsgFFDSI-GIYQAvsdRQQKLAQQWLDILGIDKRTADAPfHSL 402
|
170 180 190
....*....|....*....|....*....|..
gi 446493357 142 SGGQKQRVGIARALANDPTVLLCDEATSALDP 173
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-223 |
1.42e-08 |
|
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: 54.19 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLIRmfnHLEAPTSGEVIIDGDhigqLSKNGLRAKrqkvsmIFQHFnllwsrtvl 100
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLK---ALANRTEGNVSVEGD----IHYNGIPYK------EFAEK--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 knimFPLEIAGVPRRRAKQKAL---ELVELVgLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTD 177
Cdd:cd03233 81 ----YPGEIIYVSEEDVHFPTLtvrETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446493357 178 EILDLLLKIREQQNLTIVLITHEMHV-IRRICDEVAVMESGKVIEHG 223
Cdd:cd03233 156 EILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQIYYG 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-254 |
1.46e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 4 LKEVVKEYR--TKNKEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMfnhleapTSGEviIDGDHI---GQLSKNGL- 77
Cdd:TIGR00956 58 LTRGFRKLKkfRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKT-------IASN--TDGFHIgveGVITYDGIt 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 78 -----RAKRQKVSMIFQ---HFNLLwsrTVLKNIMFPLEIAGVPRR--------RAKQKALELVELVGLK-------GRE 134
Cdd:TIGR00956 129 peeikKHYRGDVVYNAEtdvHFPHL---TVGETLDFAARCKTPQNRpdgvsreeYAKHIADVYMATYGLShtrntkvGND 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 135 kaYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLlkiREQQNLT----IVLITHEMHVIRRICDE 210
Cdd:TIGR00956 206 --FVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL---KTSANILdttpLVAIYQCSQDAYELFDK 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446493357 211 VAVMESGKVIEHGPVTQV---FEN-----PQHTVTKrfvkedlndDFETSLT 254
Cdd:TIGR00956 281 VIVLYEGYQIYFGPADKAkqyFEKmgfkcPDRQTTA---------DFLTSLT 323
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-224 |
1.57e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.93 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLI----------RMFNHLEAPTSGEVI-----------IDGDHIGQLSK-------- 74
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDRIeglehidkvivIDQSPIGRTPRsnpatytg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 75 -------------NGLRAKRQKVSMIFQHfnllwsrtvlKNIMFPLEI---------AGVPRRRAKQKALELVELVGLKG 132
Cdd:cd03271 94 vfdeirelfcevcKGKRYNRETLEVRYKG----------KSIADVLDMtveealeffENIPKIARKLQTLCDVGLGYIKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 133 REKAypSELSGGQKQRVGIARAL---ANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIrRICD 209
Cdd:cd03271 164 GQPA--TTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVI-KCAD 239
|
250
....*....|....*
gi 446493357 210 EvavmesgkVIEHGP 224
Cdd:cd03271 240 W--------IIDLGP 246
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-206 |
1.76e-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: 52.76 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 31 GSIYGVIGFSGAGKSTLIRMF-NHLEAPTSGEVIIDGDHIgqlsknglrakrqkvsmifqhfnllwsrtvlknimfplei 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDI---------------------------------------- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 110 agvprrrakqkaLELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDL-----LL 184
Cdd:smart00382 42 ------------LEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180
....*....|....*....|..
gi 446493357 185 KIREQQNLTIVLITHEMHVIRR 206
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGP 131
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-223 |
1.93e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 54.86 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEViidgDHIGQLSknglrakrqkvsmIFQHFNLLWSRTVLKNI 103
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----KHSGRIS-------------FSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 MFpleiaGVP----RRRAKQKALELVE-LVGLKGREKAYPSE----LSGGQKQRVGIARALANDPTVLLCDEATSALDPQ 174
Cdd:cd03291 119 IF-----GVSydeyRYKSVVKACQLEEdITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446493357 175 TTDEILDLLLkIREQQNLTIVLITHEMHVIRRiCDEVAVMESGKVIEHG 223
Cdd:cd03291 194 TEKEIFESCV-CKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYG 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-228 |
3.64e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 19 LAVDHvnLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSkngLRAKRQKVSMIFQHFN--LL-- 94
Cdd:PRK10938 19 LQLPS--LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS---FEQLQKLVSDEWQRNNtdMLsp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 95 ----WSRTVLKNIMfpLEIagvprrRAKQKALELVELVG---LKGREKAYpseLSGGQKQRVGIARALANDPTVLLCDEA 167
Cdd:PRK10938 94 geddTGRTTAEIIQ--DEV------KDPARCEQLAQQFGitaLLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446493357 168 TSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKVIEHGPVTQV 228
Cdd:PRK10938 163 FDGLDVASRQQLAELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-199 |
3.87e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.75 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 13 TKNKEVLaVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLeAPTSGeviidgdhiGQLSKNglraKRQKVSMIFQ--H 90
Cdd:TIGR00954 461 TPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYG---------GRLTKP----AKGKLFYVPQrpY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 91 FNLlwsRTVLKNIMFPLEIAGVPRRRAKQKALE----LVELVGLKGREKAYPS------ELSGGQKQRVGIARALANDPT 160
Cdd:TIGR00954 526 MTL---GTLRDQIIYPDSSEDMKRRGLSDKDLEqildNVQLTHILEREGGWSAvqdwmdVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 446493357 161 VLLCDEATSALDPQTTDEILDLLLKIreqqNLTIVLITH 199
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
24-206 |
4.79e-08 |
|
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: 51.94 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIrmFNHLEAptSGEVIIdgdhIGQLSKNGlrakRQKVSMIFQhfnllwsrtvLKNI 103
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA--SGKARL----ISFLPKFS----RNKLIFIDQ----------LQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 MfpleiagvprrrakQKALELVELvglkGREKaypSELSGGQKQRVGIARALANDP--TVLLCDEATSALDPQTTDEILD 181
Cdd:cd03238 72 I--------------DVGLGYLTL----GQKL---STLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLE 130
|
170 180
....*....|....*....|....*
gi 446493357 182 LLLKIREQQNlTIVLITHEMHVIRR 206
Cdd:cd03238 131 VIKGLIDLGN-TVILIEHNLDVLSS 154
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-224 |
5.15e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 2 IELKEVVKEYRtknkEVLAVDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEV-IIDGDhIGQlsknglRAK 80
Cdd:NF033858 2 ARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGD-MAD------ARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 81 RQKVS-----MIfQHF--NLLWSRTVLKNIMFPLEIAGVPRRRAKQKALELVELVGLkgrekaYP------SELSGGQKQ 147
Cdd:NF033858 71 RRAVCpriayMP-QGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL------APfadrpaGKLSGGMKQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 148 RVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQ-NLTIVLITHEMHVIRRiCDEVAVMESGKVIEHGP 224
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGT 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-219 |
2.41e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 2.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 141 LSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIRRICDEVAVMESGKV 219
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-230 |
2.58e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 31 GSIYGVIGFSGAGKSTLIR-MFNHLEAPT-SGEVIIDGdhiGQLSKNGLRakrqKVSMIFQHFNLLWSRTVLKNIMFpLE 108
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANN---RKPTKQILK----RTGFVTQDDILYPHLTVRETLVF-CS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 109 IAGVPRRRAKQKALELVELV----GLKGRE-----KAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEI 179
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAESViselGLTKCEntiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446493357 180 LDLLLKIrEQQNLTIVLITHE-MHVIRRICDEVAVMESGKVIEHGPVTQ---VFE 230
Cdd:PLN03211 246 VLTLGSL-AQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSDamaYFE 299
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-205 |
1.77e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGQLSKNGLrakrqkvSMIFQHFNLLWSRTVLKNI 103
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-------TYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 MFPLEI-AGVPRRRAKQKALELVELVGlkgrEKAYpsELSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDeILDL 182
Cdd:PRK13541 92 KFWSEIyNSAETLYAAIHYFKLHDLLD----EKCY--SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD-LLNN 164
|
170 180
....*....|....*....|...
gi 446493357 183 LLKIREQQNLTIVLITHEMHVIR 205
Cdd:PRK13541 165 LIVMKANSGGIVLLSSHLESSIK 187
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
24-228 |
1.92e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLE--APTSGEVIIDGDHIGQLSKNGlRAKrQKVSMIFQhfnllwsrtvlk 101
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED-RAG-EGIFMAFQ------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 102 nimFPLEIAGVPRRRAKQKALELV---------------ELVGLKGREKAYPSEL---------SGGQKQRVGIARALAN 157
Cdd:PRK09580 86 ---YPVEIPGVSNQFFLQTALNAVrsyrgqepldrfdfqDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446493357 158 DPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIRRI-CDEVAVMESGKVIEHGPVTQV 228
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGDFTLV 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-186 |
3.29e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 14 KNKEVLaVDHVNLSIRAGSIYGVIGFSGAGKSTLIrmfNHLEAPTSGEVIIDGDHIgqlsKNG--LRAKRQKVSMIFQHF 91
Cdd:TIGR00956 773 KEKRVI-LNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRL----VNGrpLDSSFQRSIGYVQQQ 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 92 NL-LWSRTVLKNIMF------PLEIAGVPRRRAKQKALELVE-------LVGLKGrekaypSELSGGQKQRVGIARALAN 157
Cdd:TIGR00956 845 DLhLPTSTVRESLRFsaylrqPKSVSKSEKMEYVEEVIKLLEmesyadaVVGVPG------EGLNVEQRKRLTIGVELVA 918
|
170 180 190
....*....|....*....|....*....|
gi 446493357 158 DPTVLL-CDEATSALDPQTTDEILDLLLKI 186
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-223 |
3.33e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 26 LSIRAGSIY-----GVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDgdhigqlsknglrakrQKVSMIFQHFNLLWSRTVL 100
Cdd:COG1245 356 LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----------------LKISYKPQYISPDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 101 KNImfpleiagvprRRAKQKAL-------ELVELVGLKGREKAYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDP 173
Cdd:COG1245 420 EFL-----------RSANTDDFgssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446493357 174 QTTDEILDLLLKIREQQNLTIVLITHEMHVIRRICDEVAVMEsGKVIEHG 223
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHG 537
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-245 |
4.44e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 141 LSGGQKQRVGIARALAND---PTVLLcDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIrRICDEVAVMESG 217
Cdd:PRK00635 477 LSGGEQERTALAKHLGAEligITYIL-DEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRIIDIGPG 553
|
90 100 110
....*....|....*....|....*....|...
gi 446493357 218 KVIEHGPVT-----QVFENPQHTVTKRFVKEDL 245
Cdd:PRK00635 554 AGIFGGEVLfngspREFLAKSDSLTAKYLRQEL 586
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-212 |
5.66e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 15 NKEVLavDHVNLSIRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVII-DGDHIGQLSknglrakrqkvsmifQHFNL 93
Cdd:PRK11819 19 KKQIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGYLP---------------QEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 94 LWSRTVLKNIMfpleiAGVPRRRAKQKALElvELVGLKGREKAYPSE--------------------------------- 140
Cdd:PRK11819 82 DPEKTVRENVE-----EGVAEVKAALDRFN--EIYAAYAEPDADFDAlaaeqgelqeiidaadawdldsqleiamdalrc 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 141 ---------LSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEIldlllkireQQNL-----TIVLITHEmhviRR 206
Cdd:PRK11819 155 ppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWL---------EQFLhdypgTVVAVTHD----RY 221
|
....*.
gi 446493357 207 ICDEVA 212
Cdd:PRK11819 222 FLDNVA 227
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-224 |
5.77e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 139 SELSGGQKQRVGIARALAN---DPTVLLCDEATSALDPQTTDEILDLLLKIrEQQNLTIVLITHEMHVIrRICDEvavme 215
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSL-THQGHTVVIIEHNMHVV-KVADY----- 880
|
....*....
gi 446493357 216 sgkVIEHGP 224
Cdd:PRK00635 881 ---VLELGP 886
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
6-205 |
9.64e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.32 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 6 EVVKEYRTKNKEVLAV--------DHVNLSIRAGSIYGVIGFSGAGKSTLI---------RMFNHLEAPTSGEVIIDG-- 66
Cdd:TIGR00630 601 EVPAERRPGNGKFLTLkgarennlKNITVSIPLGLFTCITGVSGSGKSTLIndtlypalaNRLNGAKTVPGRYTSIEGle 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 67 ----------------------------DHIGQLSKNGLRAKRQ-------------------------KVSMIF----- 88
Cdd:TIGR00630 681 hldkvihidqspigrtprsnpatytgvfDEIRELFAETPEAKVRgytpgrfsfnvkggrceacqgdgviKIEMHFlpdvy 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 89 --------QHFNllwsRTVL------KNIMFPLEI---------AGVPRRRAKQKALELVELVGLKGREKAYpsELSGGQ 145
Cdd:TIGR00630 761 vpcevckgKRYN----RETLevkykgKNIADVLDMtveeayeffEAVPSISRKLQTLCDVGLGYIRLGQPAT--TLSGGE 834
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446493357 146 KQRVGIARAL---ANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIR 205
Cdd:TIGR00630 835 AQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 896
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-222 |
1.56e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 28 IRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDgdhigqlsknglrakrQKVSMIFQHFNLLWSRTV---LKNI- 103
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----------------LKISYKPQYIKPDYDGTVedlLRSIt 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 104 ------MFPLEIAgvprrrakqKALELVELVglkgrEKaYPSELSGGQKQRVGIARALANDPTVLLCDEATSALDPqttd 177
Cdd:PRK13409 426 ddlgssYYKSEII---------KPLQLERLL-----DK-NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV---- 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446493357 178 eildlllkirEQQnltiVLIThemHVIRRICDE--VAVMesgkVIEH 222
Cdd:PRK13409 487 ----------EQR----LAVA---KAIRRIAEEreATAL----VVDH 512
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-224 |
1.58e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 24 VNLSIRAGSIYGVIGFSGAGKSTL--------------------IRMF-NHLEAPtsgeviiDGDHIGQLS-------KN 75
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryveslsayARQFlGQMDKP-------DVDSIEGLSpaiaidqKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 76 GLRAKRQKV---SMIFQHFNLLWSRtvlknimfpleiAGVPRRrakqkaLELVELVGLK----GREKaypSELSGGQKQR 148
Cdd:cd03270 87 TSRNPRSTVgtvTEIYDYLRLLFAR------------VGIRER------LGFLVDVGLGyltlSRSA---PTLSGGEAQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 149 VGIARALANDPTVLL--CDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHemhvirricDEVAVMESGKVIEHGP 224
Cdd:cd03270 146 IRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEH---------DEDTIRAADHVIDIGP 213
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-199 |
2.21e-05 |
|
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: 44.27 E-value: 2.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 141 LSGGQKQRVGIARALAN-----DPTVLLcDEATSALDPQTTDEILDLLLKIREQQNLTIVlITH 199
Cdd:cd03227 78 LSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITH 139
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-172 |
1.18e-04 |
|
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: 43.12 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 29 RAGSIYGVIGFSGAGKSTLIRM--------FNHLEAPTSGEVIIDGDHIGQLSK--NGLRAKRQKVSMIFQHFNLLwSRT 98
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKIlagklkpnLGKFDDPPDWDEILDEFRGSELQNyfTKLLEGDVKVIVKPQYVDLI-PKA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 99 VLKNIMFPLEiaGVPRRRAKQKALELVELVGLKGREKaypSELSGGQKQRVGIARALANDPTVLLCDEATSALD 172
Cdd:cd03236 103 VKGKVGELLK--KKDERGKLDELVDQLELRHVLDRNI---DQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-215 |
1.36e-04 |
|
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: 42.17 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 28 IRAGSIYGVIGFSGAGKSTLIRMFNHLEAPTSGEVIIDGDHIGqlsknglrAKRQKVSmifqhfnllwsrtvlknimfpl 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV--------YKPQYID---------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 108 eiagvprrrakqkalelvelvglkgrekaypseLSGGQKQRVGIARALANDPTVLLCDEATSALDPQTTDEILDLLLKIR 187
Cdd:cd03222 72 ---------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*...
gi 446493357 188 EQQNLTIVLITHEMHVIRRICDEVAVME 215
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-220 |
7.94e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 7.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 21 VDHVNLSIRAGSIYGVIGFSGAGKSTLI-----RMFNHleaPTSGEVIIDGDHIgQLS------KNGLrakrQKVSMIFQ 89
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAmsvfgRSYGR---NISGTVFKDGKEV-DVStvsdaiDAGL----AYVTEDRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 90 HFNLLWSRTVLKNIMFP----------------LEIAGVPRRRAKQKALELVELVGlkgrekaypsELSGGQKQRVGIAR 153
Cdd:NF040905 348 GYGLNLIDDIKRNITLAnlgkvsrrgvideneeIKVAEEYRKKMNIKTPSVFQKVG----------NLSGGNQQKVVLSK 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446493357 154 ALANDPTVLLCDEATSALDPQTTDEILDLllkIRE--QQNLTIVLITHEMHVIRRICDEVAVMESGKVI 220
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
141-207 |
3.65e-03 |
|
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: 37.97 E-value: 3.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446493357 141 LSGGQKQ------RVGIARALANDPTVLLCDEATSALDPQTTDE-ILDLLLKIREQQNLTIVLITHEMHVIRRI 207
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
141-205 |
4.74e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 4.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446493357 141 LSGGQKQRVGIARALA---NDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIR 205
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGN-TVVVIEHNLDVIK 893
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
141-246 |
7.42e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446493357 141 LSGGQKQRVGIARAL---ANDPTVLLCDEATSALDPQTTDEILDLLLKIREQQNlTIVLITHEMHVIrRICDEVAVM--- 214
Cdd:PRK00349 831 LSGGEAQRVKLAKELskrSTGKTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGN-TVVVIEHNLDVI-KTADWIIDLgpe 908
|
90 100 110
....*....|....*....|....*....|....*
gi 446493357 215 ---ESGKVIEHGPVTQVFENPqHTVTKRFVKEDLN 246
Cdd:PRK00349 909 ggdGGGEIVATGTPEEVAKVE-ASYTGRYLKPVLE 942
|
|
| |
