|
Name |
Accession |
Description |
Interval |
E-value |
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-335 |
0e+00 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 586.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR 240
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 241 FVFEAERVDEDERHDDFAHVPGL-----ILRLTFRGEATYAPLLGTVARQTGVDYSILSGRIDRIKDTPYGQLTLALVG- 314
Cdd:PRK11153 240 FIQSTLHLDLPEDYLARLQAEPTtgsgpLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGd 319
|
330 340
....*....|....*....|..
gi 489187600 315 -GDLEAAMSQLNAADVHVEVLR 335
Cdd:PRK11153 320 pGDIQAAIAYLQEHGVKVEVLG 341
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-335 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 553.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR 240
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 241 FVFEAERVDEDERHDDF---AHVPGLILRLTFRGEATYAPLLGTVARQTGVDYSILSGRIDRIKDTPYGQLTLALVGGD- 316
Cdd:COG1135 240 FLPTVLNDELPEELLARlreAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDa 319
|
330 340
....*....|....*....|
gi 489187600 317 -LEAAMSQLNAADVHVEVLR 335
Cdd:COG1135 320 aIDAALAYLREQGVVVEVLG 339
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-234 |
2.59e-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: 393.87 E-value: 2.59e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-334 |
8.27e-116 |
|
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: 338.78 E-value: 8.27e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGGfSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNT-PKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR 240
Cdd:TIGR02314 160 KVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 241 FVFEAERVDEDERHDD------FA-HVPglILRLTFRGEATYAPLLGTVARQTGVDYSILSGRIDRIKDTPYGQLTLALV 313
Cdd:TIGR02314 240 FIRSTLHLSIPEDYQErlqatpFAdSVP--MVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMH 317
|
330 340
....*....|....*....|...
gi 489187600 314 GG--DLEAAMSQLNAADVHVEVL 334
Cdd:TIGR02314 318 GTqqDTQAAIAYLQEHNVKVEVL 340
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-241 |
2.36e-105 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 308.08 E-value: 2.36e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvaGREiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEgLRRF 80
Cdd:COG1126 1 MIEIENLHKSF---GDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD-INKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR 240
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
.
gi 489187600 241 F 241
Cdd:COG1126 235 F 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-240 |
6.16e-102 |
|
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: 309.14 E-value: 6.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGR-EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRR 79
Cdd:COG1123 260 LLEVRNLSKRYPVRGKgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMIFQH----FNllSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGIAR 154
Cdd:COG1123 340 LRRRVQMVFQDpyssLN--PRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
....*.
gi 489187600 235 HPTTRR 240
Cdd:COG1123 498 HPYTRA 503
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-242 |
1.03e-93 |
|
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: 278.40 E-value: 1.03e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:COG1127 5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVfLHPQHPTTRR 240
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL-LASDDPWVRQ 239
|
..
gi 489187600 241 FV 242
Cdd:COG1127 240 FL 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-239 |
2.30e-92 |
|
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: 278.09 E-value: 2.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEP---SGGRILVEGEDVTALDAEGL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 78 RRFR-QRVGMIFQhfNLLSS----KTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSD---HARKYPAQLSGGQKQR 149
Cdd:COG0444 81 RKIRgREIQMIFQ--DPMTSlnpvMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 150 VGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250
....*....|
gi 489187600 230 FLHPQHPTTR 239
Cdd:COG0444 239 FENPRHPYTR 248
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-223 |
1.76e-91 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 272.30 E-value: 1.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 R-QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQ 223
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
3.79e-87 |
|
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: 262.05 E-value: 3.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRF 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRR---RKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFnlLSS----KTVADNIAMPLRLAGgfsRAEVDARVSELLARVGL-SDHARKYPAQLSGGQKQRVGIARA 155
Cdd:COG1124 78 RRRVQMVFQDP--YASlhprHTVDRILAEPLRIHG---LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQH 235
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*..
gi 489187600 236 PTTRRFV 242
Cdd:COG1124 233 PYTRELL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-224 |
3.10e-84 |
|
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: 253.97 E-value: 3.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQhfNLLSS----KTVADNIAMPLRLAGGFSRAE-VDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGIAR 154
Cdd:cd03257 81 RKEIQMVFQ--DPMSSlnprMTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPeEVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-220 |
3.75e-84 |
|
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: 253.22 E-value: 3.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAlDAEGLRRFR 81
Cdd:cd03262 1 IEIKNLHKSF--GDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-222 |
4.30e-84 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 253.44 E-value: 4.30e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:COG2884 1 MIRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAgGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINReLKLTIVLITHEMDVIRRVCDQVAVMDGGAIVE 222
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
26-239 |
4.95e-83 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 254.66 E-value: 4.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQhfNLLSS----KTVAD 101
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ--DPYASlnprMTVGD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 102 NIAMPLRLAGGFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASV 180
Cdd:COG4608 117 IIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQV 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 181 LQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:COG4608 197 LNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHPYTQ 255
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
2.31e-82 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 249.97 E-value: 2.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvAGReiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:COG3638 2 MLELRNLSKRYP-GGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAM-------PLR-LAGGFSRAEVDaRVSELLARVGLSDHARKYPAQLSGGQKQRVGI 152
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVLAgrlgrtsTWRsLLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 153 ARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-220 |
2.43e-81 |
|
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: 246.25 E-value: 2.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 -QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQVAVMDGGAI 220
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-230 |
8.52e-81 |
|
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: 245.32 E-value: 8.52e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFR 81
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQH-FNLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFgPENL--GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-241 |
2.51e-80 |
|
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: 244.33 E-value: 2.51e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvaGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFR 81
Cdd:cd03261 1 IELRGLTKSFG--GRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHpQHPTTRRF 241
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS-DDPLVRQF 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-268 |
2.24e-79 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 245.78 E-value: 2.24e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRf 80
Cdd:COG3842 5 ALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 rqRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG3842 78 --NVGMVFQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR 240
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVAD 234
|
250 260 270
....*....|....*....|....*....|...
gi 489187600 241 FV-----FEAERVDedeRHDDFAHVPGLILRLT 268
Cdd:COG3842 235 FIgeanlLPGTVLG---DEGGGVRTGGRTLEVP 264
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-239 |
2.44e-79 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 242.69 E-value: 2.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrrf 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 rqRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG1116 81 --DRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMD--VirRVCDQVAVMDG--GAIVEQGDVAdvFLHPQHP 236
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeaV--FLADRVVVLSArpGRIVEEIDVD--LPRPRDR 233
|
...
gi 489187600 237 TTR 239
Cdd:COG1116 234 ELR 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-226 |
1.57e-75 |
|
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: 231.59 E-value: 1.57e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrrfr 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03293 74 -DRGYVFQQDALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDG--GAIVEQGDV 226
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-224 |
7.92e-75 |
|
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: 229.33 E-value: 7.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrfR 81
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGGfSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-242 |
6.61e-74 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 233.07 E-value: 6.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQ-RVGMIFQHFNLLSSKTVADNIA 104
Cdd:COG4175 48 FDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 105 MPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDP------QTta 178
Cdd:COG4175 128 FGLEIQG-VPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirremQD-- 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 179 svlQLLaEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:COG4175 205 ---ELL-ELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFV 264
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-229 |
1.59e-73 |
|
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: 227.07 E-value: 1.59e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFR 81
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAM-------PLR-LAGGFSRAEVdARVSELLARVGLSDHARKYPAQLSGGQKQRVGIA 153
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSgrlgrrsTWRsLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 154 RALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
3.42e-73 |
|
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: 226.41 E-value: 3.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:TIGR02315 1 MLEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPlRLA---------GGFSRAEVdARVSELLARVGLSDHARKYPAQLSGGQKQRVG 151
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLHG-RLGykptwrsllGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 152 IARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-242 |
2.88e-71 |
|
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: 222.52 E-value: 2.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFR-QRVGMIFQHFNLLSSK 97
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTT 177
Cdd:cd03294 118 TVLENVAFGLEVQG-VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 178 ASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:cd03294 197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-240 |
2.99e-71 |
|
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: 230.34 E-value: 2.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 16 REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEePSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQH-FNLL 94
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 95 SSK-TVADNIAMPLRLAG-GFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSA 171
Cdd:COG4172 376 SPRmTVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 172 LDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR 240
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRA 524
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-242 |
5.82e-71 |
|
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: 220.64 E-value: 5.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvAGReiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:cd03295 1 IEFENVTKRYG-GGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDH--ARKYPAQLSGGQKQRVGIARALACR 159
Cdd:cd03295 76 -KIGYVIQQIGLFPHMTVEENIALVPKLLK-WPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
...
gi 489187600 240 RFV 242
Cdd:cd03295 234 EFV 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-240 |
4.31e-70 |
|
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: 227.26 E-value: 4.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKS----TLLRLINRLEEPSGGRILVEGEDVTALDAEG 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 LRRFR-QRVGMIFQH----FNLLssKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARK---YPAQLSGGQKQ 148
Cdd:COG4172 86 LRRIRgNRIAMIFQEpmtsLNPL--HTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 149 RVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250
....*....|..
gi 489187600 229 VFLHPQHPTTRR 240
Cdd:COG4172 244 LFAAPQHPYTRK 255
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-241 |
7.09e-70 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 217.65 E-value: 7.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAlDAEGLRRF 80
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAM-PLRLAGGfSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGA-SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQ 233
|
..
gi 489187600 240 RF 241
Cdd:PRK09493 234 EF 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-241 |
8.07e-70 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 218.13 E-value: 8.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvaGrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVT---------- 70
Cdd:COG4598 8 ALEVRDLHKSF---G-DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 71 ALDAEGLRRFRQRVGMIFQHFNLLSSKTVADN-IAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQR 149
Cdd:COG4598 84 PADRRQLQRIRTRLGMVFQSFNLWSHMTVLENvIEAPVHVLG-RPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 150 VGIARALACRPSILLCDEATSALDPQTTASVL---QLLAEINRelklTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDV 226
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLkvmRDLAEEGR----TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238
|
250
....*....|....*
gi 489187600 227 ADVFLHPQHPTTRRF 241
Cdd:COG4598 239 AEVFGNPKSERLRQF 253
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-232 |
1.02e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 217.24 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaldAEGLRRFR 81
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVA--------DVFLH 232
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDelkarlleDVFLE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
1.16e-69 |
|
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: 216.18 E-value: 1.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 3 EFHDVhkTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFRQ 82
Cdd:cd03225 1 ELKNL--SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 83 RVGMIFQHFNL-LSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03225 76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
5.76e-69 |
|
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: 224.01 E-value: 5.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSG---GRILVEGEDVTALDAEGL 77
Cdd:COG1123 4 LLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 78 RRfrqRVGMIFQHF-NLLSSKTVADNIAMPLRLaGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARAL 156
Cdd:COG1123 82 GR---RIGMVFQDPmTQLNPVTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
7.69e-69 |
|
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: 214.99 E-value: 7.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 R-QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgfsRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAG---RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQVAVMDGGAIVE 222
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-242 |
1.14e-68 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 215.29 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRL--EEPSG---GRILVEGEDVTA--LDAEGLRRfrqRVGMIFQHFN 92
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYDpdVDVVELRR---RVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 93 LLSsKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGL----SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEA 168
Cdd:COG1117 103 PFP-KSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 169 TSALDPQTTASVLQLLaeinRELK--LTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:COG1117 182 TSALDPISTAKIEELI----LELKkdYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-258 |
3.84e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 214.24 E-value: 3.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV-TALDAeglrrf 80
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPP------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQR-VGMIFQHFNLLSSKTVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:COG1118 73 RERrVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVA 231
|
250 260
....*....|....*....|....
gi 489187600 240 RF-----VFEAERVDEDERHDDFA 258
Cdd:COG1118 232 RFlgcvnVLRGRVIGGQLEADGLT 255
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
2.22e-66 |
|
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: 206.65 E-value: 2.22e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEgLRRFR 81
Cdd:cd03229 1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPlrlaggfsraevdarvsellarvglsdharkypaqLSGGQKQRVGIARALACRPS 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-226 |
3.49e-66 |
|
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: 207.80 E-value: 3.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEE-----PSGGRILVEGEDVTALDAEG 76
Cdd:cd03260 1 IELRDLNVYYG----DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 LRrFRQRVGMIFQHFNLLSsKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSD--HARKYPAQLSGGQKQRVGIAR 154
Cdd:cd03260 77 LE-LRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDV 226
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-234 |
1.70e-65 |
|
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: 207.69 E-value: 1.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGR-EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQhF--NLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDH-ARKYPAQLSGGQKQRVGIARAL 156
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFgPKNL--GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-242 |
4.92e-65 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 205.75 E-value: 4.92e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEgeDVTaLDA-------EGL-RRFRQRVGMIFQHFNLLSSK 97
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DIT-IDTarslsqqKGLiRQLRQHVGFVFQNFNLFPHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTT 177
Cdd:PRK11264 101 TVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 178 ASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:PRK11264 181 GEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-242 |
8.78e-65 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 208.39 E-value: 8.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRf 80
Cdd:COG3839 3 SLELENVSKSYG----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 rqRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHE----MdvirRVCDQVAVMDGGAIVEQGDVADVFLHPQHp 236
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPAN- 227
|
....*.
gi 489187600 237 ttrRFV 242
Cdd:COG3839 228 ---LFV 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-230 |
1.20e-64 |
|
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: 205.36 E-value: 1.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaLDAEGLRRFR 81
Cdd:TIGR04520 1 IEVENVSFSY--PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQH-FNLLSSKTVADNIAMplrlaG----GFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARAL 156
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAF-----GlenlGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMD-VIRrvCDQVAVMDGGAIVEQGDVADVF 230
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIF 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-241 |
3.06e-64 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 203.32 E-value: 3.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAgreiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV---TALDAEGLR 78
Cdd:COG4161 3 IQLKNINCFYGSH----QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 79 RFRQRVGMIFQHFNLLSSKTVADN-IAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALA 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLG-LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 158 CRPSILLCDEATSALDPQTTASVlqllAEINRELK---LTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDvADVFLHPQ 234
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQV----VEIIRELSqtgITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ 232
|
....*..
gi 489187600 235 hptTRRF 241
Cdd:COG4161 233 ---TEAF 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-242 |
1.79e-62 |
|
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: 198.61 E-value: 1.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGREIpALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrrFR 81
Cdd:cd03300 1 IELENVSKFY---GGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP-----HK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHpttrRF 241
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPAN----RF 226
|
.
gi 489187600 242 V 242
Cdd:cd03300 227 V 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-241 |
3.36e-62 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 198.31 E-value: 3.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV---TALDAEGLRRFRQRVGMIFQHFNLLSS 96
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADN-IAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQ 175
Cdd:PRK11124 97 LTVQQNlIEAPCRVLG-LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 176 TTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDvADVFLHPQhptTRRF 241
Cdd:PRK11124 176 ITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQ---TEAF 236
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
1.00e-60 |
|
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: 194.88 E-value: 1.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVhkTYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglRRF 80
Cdd:COG1120 1 MLEAENL--SVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR---REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAM---PLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALA 157
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 158 CRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-254 |
1.02e-59 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 194.41 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 6 DVHKTYRV------AGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRR 79
Cdd:PRK11308 10 DLKKHYPVkrglfkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMIFQhfNLLSS----KTVADNIAMPLRLAGGFSRAEVDARVSELLARVGL-SDHARKYPAQLSGGQKQRVGIAR 154
Cdd:PRK11308 90 LRQKIQIVFQ--NPYGSlnprKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
250 260
....*....|....*....|
gi 489187600 235 HPTTRRFVFEAERVDEDERH 254
Cdd:PRK11308 248 HPYTQALLSATPRLNPDDRR 267
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-220 |
2.05e-59 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 190.03 E-value: 2.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHktYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrRFR 81
Cdd:COG4619 1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSsKTVADNIAMPLRLAGgfsRAEVDARVSELLARVGLSDHARKYPA-QLSGGQKQRVGIARALACRP 160
Cdd:COG4619 74 RQVAYVPQEPALWG-GTVRDNLPFPFQLRE---RKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
26-234 |
2.09e-59 |
|
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: 191.41 E-value: 2.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRFRQRVGMIFQHFNLLSSKTVADN--I 103
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH--RIARLGIARTFQNPRLFPELTVLENvlV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 104 AMPLRLAGGF------------SRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSA 171
Cdd:COG0411 103 AAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAG 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 172 LDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:COG0411 183 LNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-241 |
2.62e-59 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 190.35 E-value: 2.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrfrQR-VGMIFQHFNLLSSKTVADNIA 104
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA------ERpVSMLFQENNLFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 105 MPLRLAGGFSRAEVdARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLL 184
Cdd:COG3840 94 LGLRPGLKLTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 185 AEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRF 241
Cdd:COG3840 173 DELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-242 |
2.67e-59 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 191.34 E-value: 2.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 6 DVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAL----------DAE 75
Cdd:PRK10619 10 DLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 76 GLRRFRQRVGMIFQHFNLLSSKTVADNI-AMPLRLAGgFSRAEVDARVSELLARVGLSDHAR-KYPAQLSGGQKQRVGIA 153
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLG-LSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 154 RALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHP 233
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
....*....
gi 489187600 234 QHPTTRRFV 242
Cdd:PRK10619 244 QSPRLQQFL 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-209 |
1.96e-58 |
|
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: 187.62 E-value: 1.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFR 81
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGGfSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGV-PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVI----RRVC 209
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVdttrHRVI 207
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-242 |
4.51e-58 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 188.12 E-value: 4.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAG-----REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaeg 76
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 lRRFR-QRVGMIFQHFN--LLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGI 152
Cdd:COG4167 82 -YKYRcKHIRMIFQDPNtsLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 153 ARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLH 232
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|
gi 489187600 233 PQHPTTRRFV 242
Cdd:COG4167 241 PQHEVTKRLI 250
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-244 |
8.09e-58 |
|
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: 186.78 E-value: 8.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGReIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrrfR 81
Cdd:cd03296 3 IEVRNVSKRF---GD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV------Q 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QR-VGMIFQHFNLLSSKTVADNIAMPLRLAGGFSR---AEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALA 157
Cdd:cd03296 73 ERnVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 158 CRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPt 237
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP- 231
|
....*..
gi 489187600 238 trrFVFE 244
Cdd:cd03296 232 ---FVYS 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
9.32e-56 |
|
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: 192.74 E-value: 9.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVhkTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR-- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHfNLLSSKTVADNIAMplrlaggfSRAEV-DARVSELLARVGLSDHARKYP-----------AQLSGGQKQR 149
Cdd:COG2274 550 -QIGVVLQD-VFLFSGTIRENITL--------GDPDAtDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 150 VGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRelKLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDG 691
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-239 |
3.35e-55 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 182.98 E-value: 3.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQhfNLLSS----KTVAD 101
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQ--DPLASlnprMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 102 NIAMPLRL-AGGFSRAEVDARVSELLARVGL-SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTAS 179
Cdd:PRK15079 120 IIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 180 VLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:PRK15079 200 VVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
26-244 |
3.70e-55 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 183.75 E-value: 3.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrRFRQrVGMIFQHFNLLSSKTVADNIAM 105
Cdd:PRK10851 23 LDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA----RDRK-VGFVFQHYALFRHMTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGGFSR---AEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQ 182
Cdd:PRK10851 98 GLTVLPRRERpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRR 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 183 LLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPqhptTRRFVFE 244
Cdd:PRK10851 178 WLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP----ATRFVLE 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-234 |
1.60e-54 |
|
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: 178.01 E-value: 1.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRFRQRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH--EIARLGIGRTFQIPRLFPELTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGG---------FSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:cd03219 99 AAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 177 TASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:cd03219 179 TEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-229 |
2.08e-54 |
|
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: 178.13 E-value: 2.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaldAEGLRRF 80
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRaEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDE-ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-207 |
4.07e-54 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 176.60 E-value: 4.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrVAGREipALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:PRK10908 1 MIRFEHVSKAY-LGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGGfSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGA-SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINReLKLTIVLITHEMDVIRR 207
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISR 202
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-239 |
5.23e-54 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 177.96 E-value: 5.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 5 HDVHKTYRVAG--REIPALQPTR---LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRR 79
Cdd:PRK10419 7 SGLSHHYAHGGlsGKHQHQTVLNnvsLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMIFQH----FNllSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSD-HARKYPAQLSGGQKQRVGIAR 154
Cdd:PRK10419 87 FRRDIQMVFQDsisaVN--PRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVfLHPQ 234
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDK-LTFS 243
|
....*
gi 489187600 235 HPTTR 239
Cdd:PRK10419 244 SPAGR 248
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
2.63e-53 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.28 E-value: 2.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvaGReiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaldaeglRRF 80
Cdd:COG1121 6 AIELENLTVSYG--GR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSK--TVADNIAMPLRLAGGFSR---AEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARA 155
Cdd:COG1121 74 RRRIGYVPQRAEVDWDFpiTVRDVVLMGRYGRRGLFRrpsRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGaIVEQGDVADVF 230
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVL 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-242 |
1.48e-52 |
|
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: 173.29 E-value: 1.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrfRQRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLA 185
Cdd:cd03299 95 GLKKRK-VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 186 EINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:cd03299 174 KIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
3.14e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 181.13 E-value: 3.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:COG1132 340 IEFENVSFSY---PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLSSkTVADNIAmplrlaggFSRAEV-DARVSELLARVGLSDHARKYP-----------AQLSGGQKQR 149
Cdd:COG1132 415 -QIGVVPQDTFLFSG-TIRENIR--------YGRPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 150 VGIARALACRPSILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGR----TTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-224 |
5.98e-52 |
|
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: 170.90 E-value: 5.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrfR 81
Cdd:cd03301 1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-232 |
5.11e-51 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 170.58 E-value: 5.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 8 HKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGedvTALDAEGLRRFRQRVGMI 87
Cdd:PRK13635 10 HISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 88 FQH-FNLLSSKTVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCD 166
Cdd:PRK13635 87 FQNpDNQFVGATVQDDVAFGLE-NIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 167 EATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVADVFLH 232
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
6.02e-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: 166.79 E-value: 6.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFR 81
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSkTVADNIamplrlaggfsraevdarvsellarvglsdharkypaqLSGGQKQRVGIARALACRPS 161
Cdd:cd03228 76 KNIAYVPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRvCDQVAVMDGG 218
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
6.93e-51 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 169.66 E-value: 6.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrf 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 rqRvGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG4525 78 --R-GVVFQKDALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMD 203
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-170 |
9.66e-51 |
|
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: 165.51 E-value: 9.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFRQRVGMIFQHFNLLSSKTVA 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 101 DNIAMPLRLAgGFSRAEVDARVSELLARVGLSD----HARKYPAQLSGGQKQRVGIARALACRPSILLCDEATS 170
Cdd:pfam00005 78 ENLRLGLLLK-GLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-218 |
1.17e-50 |
|
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: 166.03 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaldaEGLRRFR 81
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIamplrlaggfsraevdarvsellarvglsdharkypaQLSGGQKQRVGIARALACRPS 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNG 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-230 |
2.93e-50 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 168.69 E-value: 2.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEgLRRFRQRVGMIFQHFNL-LS 95
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLVFQYPEYqLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 96 SKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLS--DHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSAL 172
Cdd:PRK13637 98 EETIEKDIAFgPINL--GLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 173 DPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.17e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 166.79 E-value: 1.17e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvAGREipALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaLDAEGLRRF 80
Cdd:PRK13639 1 ILETRDLKYSYP-DGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHF-NLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALAC 158
Cdd:PRK13639 77 RKTVGIVFQNPdDQLFAPTVEEDVAFgPLNL--GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
1.28e-48 |
|
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: 171.09 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:COG4988 337 IELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLSSkTVADNIAMPLRLAGgfsraevDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:COG4988 412 -QIAWVPQNPYLFAG-TIRENLRLGRPDAS-------DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQGDVAD 228
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.46e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 164.01 E-value: 1.46e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVhkTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtalDAEGLRRF 80
Cdd:PRK13632 7 MIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQH-FNLLSSKTVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLE-NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMD-VIRrvCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-242 |
4.26e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 162.00 E-value: 4.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 9 KTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRL-----EEPSGGRILVEGEDVTALDAEGLRRfrqR 83
Cdd:PRK14247 7 RDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRR---R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 84 VGMIFQHFNLLSSKTVADNIAMPL---RLAGgfSRAEVDARVSELLARVGLSDHARKY---PA-QLSGGQKQRVGIARAL 156
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLklnRLVK--SKKELQERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHP 236
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*.
gi 489187600 237 TTRRFV 242
Cdd:PRK14247 240 LTEKYV 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-272 |
4.27e-48 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 165.89 E-value: 4.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrfr 81
Cdd:PRK09452 15 VELRGISKSF--DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QR-VGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:PRK09452 85 NRhVNTVFQSYALFPHMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR 240
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAR 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 489187600 241 F-----VFEA---ERVDED-----------ERHDDFAHVPGLILRLTFRGE 272
Cdd:PRK09452 244 FigeinIFDAtviERLDEQrvranvegrecNIYVNFAVEPGQKLHVLLRPE 294
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-230 |
1.35e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 161.79 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVA--GREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTalDAEGLR 78
Cdd:PRK13633 4 MIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 79 RFRQRVGMIFQH-FNLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARAL 156
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFgPENL--GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEGTPKEIF 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-224 |
1.37e-47 |
|
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: 159.67 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvAGReipALQPTRLNIQAGqIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaldaEGLRRFR 81
Cdd:cd03264 1 LQLENLTKRYG-KKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMpLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDY-IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELgeDR----IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-282 |
3.19e-47 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 168.50 E-value: 3.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 16 REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQ--HFNL 93
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQdpYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 94 LSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGL-SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSAL 172
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 173 DPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFVFEAERVDEDE 252
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVADPSR 574
|
250 260 270
....*....|....*....|....*....|....*..
gi 489187600 253 RH-------DDfahVPGLILRltfRGEATYAPLLGTV 282
Cdd:PRK10261 575 QRpqrvllsDD---LPSNIHL---RGEEVAAVSLQCV 605
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-241 |
4.93e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 160.57 E-value: 4.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRV----AGReipALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTA-LDAEG 76
Cdd:PRK13634 3 ITFQKVEHRYQYktpfERR---ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 LRRFRQRVGMIFQhF--NLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGI 152
Cdd:PRK13634 80 LKPLRKKVGIVFQ-FpeHQLFEETVEKDICFgPMNF--GVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 153 ARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLH 232
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
250
....*....|....*..
gi 489187600 233 PQH--------PTTRRF 241
Cdd:PRK13634 237 PDEleaigldlPETVKF 253
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
1.65e-46 |
|
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: 165.71 E-value: 1.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGReiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:COG4987 334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRR-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLSSkTVADNiampLRLAggfsRAEV-DARVSELLARVGLSDHARKYP-----------AQLSGGQKQR 149
Cdd:COG4987 410 -RIAVVPQRPHLFDT-TLREN----LRLA----RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 150 VGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVAD 228
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-254 |
1.73e-46 |
|
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: 161.04 E-value: 1.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 25 RLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaLDAEgLRRF----RQRVGMIFQHFNLLSSKTVA 100
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSA-RGIFlpphRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 DNIAMPLRLAGGFSRAEVDARVSELLarvGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASV 180
Cdd:COG4148 96 GNLLYGRKRAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 181 LQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ-HPTTRRF----VFEAERVDEDERH 254
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDlLPLAGGEeagsVLEATVAAHDPDY 251
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-224 |
1.94e-46 |
|
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: 156.90 E-value: 1.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaldAEGLRRFR 81
Cdd:cd03263 1 LQIRNLTKTYK--KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKG-LPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRelKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-242 |
3.60e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 157.31 E-value: 3.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSG-----GRILVEGEDVTALDAEGLRrFRQRVGMIFQHFNLLSSKTVA 100
Cdd:PRK14267 25 LKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNPFPHLTIY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 DNIAMPLRLAGGF-SRAEVDARVSELLARVGLSDHARK----YPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQ 175
Cdd:PRK14267 104 DNVAIGVKLNGLVkSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 176 TTASVLQLLAEINRElkLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:PRK14267 184 GTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-241 |
4.24e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 161.35 E-value: 4.24e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAL-DAEGLRRFRQRVGMIFQHFNLLSSKTVADNIA 104
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 105 MPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLL 184
Cdd:PRK10070 129 FGMELAG-INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 185 AEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRF 241
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-220 |
7.10e-46 |
|
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: 155.00 E-value: 7.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 3 EFHDVhkTYRVAGReiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaldaeglRRFRQ 82
Cdd:cd03235 1 EVEDL--TVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 83 RVGMIFQHFNLLSSK--TVADNIAMPLRLAGGFSR---AEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALA 157
Cdd:cd03235 69 RIGYVPQRRSIDRDFpiSVRDVVLMGLYGHKGLFRrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 158 CRPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-220 |
4.56e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 155.27 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaEGLRRF 80
Cdd:PRK13650 4 IIEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQH-FNLLSSKTVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIrRVCDQVAVMDGGAI 220
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
6.59e-45 |
|
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: 150.86 E-value: 6.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 3 EFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfrq 82
Cdd:cd00267 1 EIENLSFRYG----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 83 RVGMIFQhfnllssktvadniamplrlaggfsraevdarvsellarvglsdharkypaqLSGGQKQRVGIARALACRPSI 162
Cdd:cd00267 74 RIGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 163 LLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-224 |
8.88e-45 |
|
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: 151.05 E-value: 8.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 10 TYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALdaeglrrfrqrvgmifq 89
Cdd:cd03214 6 SVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 90 hfnllSSKTVADNIAMplrlaggfsraevdarVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEAT 169
Cdd:cd03214 67 -----SPKELARKIAY----------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 170 SALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-230 |
1.44e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 153.80 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEP---SGGRILVEGedvTALDAEGLR 78
Cdd:PRK13640 6 VEFKHVSFTYP--DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG---ITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 79 RFRQRVGMIFQH-FNLLSSKTVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALA 157
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 158 CRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIrRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-224 |
2.92e-44 |
|
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: 151.37 E-value: 2.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAlDAEGLRRfrqRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:cd03265 21 FRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRR---RIGIVFQDLSVDDELTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLA 185
Cdd:cd03265 97 HARLYG-VPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 489187600 186 EINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03265 176 KLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-217 |
4.26e-44 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 151.12 E-value: 4.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 5 HDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQR- 83
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 84 VGMIFQHFNLLSSKTVADNIAMPLrLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSIL 163
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489187600 164 LCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-274 |
5.67e-44 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 154.99 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 18 IPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrrFRQRVGMIFQHFNLLSSK 97
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-----YQRPINMMFQSYALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTT 177
Cdd:PRK11607 107 TVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 178 ASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFlhpQHPTTRrfvFEAERVDE------- 250
Cdd:PRK11607 186 DRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTR---YSAEFIGSvnvfegv 259
|
250 260
....*....|....*....|....*..
gi 489187600 251 -DERHDD--FAHVPGLILRLTFRGEAT 274
Cdd:PRK11607 260 lKERQEDglVIDSPGLVHPLKVDADAS 286
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-235 |
1.10e-43 |
|
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: 149.92 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaEGLRRFrqrvgMIFQHFNLLSSKTVA 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE---PGPDRM-----VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 DNIAMPL-RLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTAS 179
Cdd:TIGR01184 73 ENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 180 VLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV-FLHPQH 235
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-229 |
1.13e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 156.72 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvAGreIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV---TALDAEgl 77
Cdd:COG1129 4 LLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 78 rrfRQRVGMIFQHFNLLSSKTVADNIAM--PLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARA 155
Cdd:COG1129 78 ---AAGIAIIHQELNLVPNLSVAENIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLaeinRELK---LTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRII----RRLKaqgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-224 |
1.27e-43 |
|
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: 149.18 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrfRQRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 P----LRLaggfsRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVL 181
Cdd:cd03298 94 GlspgLKL-----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489187600 182 QLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
26-233 |
1.27e-43 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 153.34 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaeglRRFRQR-VGMIFQHFNLLSSKTVADNIA 104
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRdICMVFQSYALFPHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 105 MPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLL 184
Cdd:PRK11432 101 YGLKMLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489187600 185 AEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHP 233
Cdd:PRK11432 180 RELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-225 |
1.58e-43 |
|
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: 150.00 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTY--RvagREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRR 79
Cdd:cd03249 1 IEFKNVSFRYpsR---PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMIFQHFNLLSSkTVADNIAMplrlaGGFSRAEVDARVSELLARV---------GLSDHARKYPAQLSGGQKQRV 150
Cdd:cd03249 75 LRSQIGLVSQEPVLFDG-TIAENIRY-----GKPDATDEEVEEAAKKANIhdfimslpdGYDTLVGERGSQLSGGQKQRI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLL--AEINRelklTIVLITHEMDVIRRvCDQVAVMDGGAIVEQGD 225
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALdrAMKGR----TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-242 |
1.76e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 150.58 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEE------PSGGRILVEGEDVTALDAEGLRRfrqRVGMIFQHFNLL 94
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRK---EVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 95 SSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGL----SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATS 170
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 171 ALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-242 |
5.13e-43 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 149.55 E-value: 5.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAG-----REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDae 75
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 76 glRRFR-QRVGMIFQ--HFNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGL-SDHARKYPAQLSGGQKQRVG 151
Cdd:PRK15112 82 --YSYRsQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 152 IARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFL 231
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|.
gi 489187600 232 HPQHPTTRRFV 242
Cdd:PRK15112 240 SPLHELTKRLI 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
5.55e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 150.00 E-value: 5.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrVAGREipALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaLDAEGLRRF 80
Cdd:PRK13636 5 ILKVEELNYNY-SDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQH-FNLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSdHARKYPAQ-LSGGQKQRVGIARALA 157
Cdd:PRK13636 81 RESVGMVFQDpDNQLFSASVYQDVSFgAVNL--KLPEDEVRKRVDNALKRTGIE-HLKDKPTHcLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 158 CRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-219 |
9.93e-43 |
|
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: 147.58 E-value: 9.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYR---VAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGED-----VTAL 72
Cdd:COG4778 4 LLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 73 DAEGLRRFRQRVGMIFQHFNLLSSKTVADNIAMPLrLAGGFSRAEVDARVSELLARVGLSDH-ARKYPAQLSGGQKQRVG 151
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPL-LERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 152 IARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGA 219
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-262 |
2.16e-42 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 149.49 E-value: 2.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKS-TLLRLINRLeePSGGRI----LVEGEDVTALDAE 75
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIggsaTFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 76 GLRRFR-QRVGMIFQH--FNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDhARK----YPAQLSGGQKQ 148
Cdd:PRK09473 90 ELNKLRaEQISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPE-ARKrmkmYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 149 RVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARD 248
|
250 260 270
....*....|....*....|....*....|....
gi 489187600 229 VFLHPQHPTTRRFVFEAERVDEDERHddFAHVPG 262
Cdd:PRK09473 249 VFYQPSHPYSIGLLNAVPRLDAEGES--LLTIPG 280
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-224 |
2.26e-42 |
|
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: 146.20 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVhkTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:cd03245 3 IEFRNV--SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLSSkTVADNIAMPLRLAGgfsraevDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:cd03245 79 -NIGYVPQDVTLFYG-TLRDNITLGAPLAD-------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIrRVCDQVAVMDGGAIVEQG 224
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-230 |
2.91e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 147.97 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvAGR--EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDA-EGLR 78
Cdd:PRK13649 3 INLQNVSYTYQ-AGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 79 RFRQRVGMIFQhF--NLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDHAR-KYPAQLSGGQKQRVGIAR 154
Cdd:PRK13649 82 QIRKKVGLVFQ-FpeSQLFEETVLKDVAFgPQNF--GVSQEEAEALAREKLALVGISESLFeKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEINrELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-224 |
3.02e-42 |
|
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: 146.48 E-value: 3.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHfNLLSSKTVADNIA-----MPLRlaggfsraevdaRVSELLARVGLSDHARKYP-----------AQLSGG 145
Cdd:cd03252 77 -QVGVVLQE-NVLFNRSIRDNIAladpgMSME------------RVIEAAKLAGAHDFISELPegydtivgeqgAGLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 146 QKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEMDVIRRVcDQVAVMDGGAIVEQ 223
Cdd:cd03252 143 QRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGR----TVIIIAHRLSTVKNA-DRIIVMEKGRIVEQ 217
|
.
gi 489187600 224 G 224
Cdd:cd03252 218 G 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-224 |
4.93e-42 |
|
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: 145.13 E-value: 4.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGedVTALDAE---GLRRFRQRVGMIFQHFNLLSSKTVADNIAMPL 107
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG--TVLFDSRkkiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 108 RlagGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEI 187
Cdd:cd03297 101 K---RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 489187600 188 NRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03297 178 KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
1.14e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 146.05 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRF 80
Cdd:PRK13648 7 IIVFKNVSFQYQ--SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN---FEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQH-FNLLSSKTVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLE-NHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQGDVADVFLHPQHPTT 238
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-224 |
2.14e-41 |
|
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: 143.91 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:cd03254 3 IEFENVNFSYD---EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHfNLLSSKTVADNIAMplrlagGFSRAEvDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:cd03254 78 -MIGVVLQD-TFLFSGTIMENIRL------GRPNAT-DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVlITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSII-IAHRLSTIKNA-DKILVLDDGKIIEEG 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-240 |
2.61e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 151.01 E-value: 2.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 11 YRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKS-TLLRLINRLEEPS----GGRILVEGEDVTALDAEGLRRFR-QRV 84
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRgNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 85 GMIFQH--FNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARK---YPAQLSGGQKQRVGIARALACR 159
Cdd:PRK15134 95 AMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
.
gi 489187600 240 R 240
Cdd:PRK15134 255 K 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
26-229 |
3.10e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 150.18 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVT------ALDAeglrrfrqRVGMIFQHFNLLSSKTV 99
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIAL--------GIGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 ADNIA--MPLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTT 177
Cdd:COG3845 98 AENIVlgLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 178 ASVLQLLaeinRELK---LTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG3845 178 DELFEIL----RRLAaegKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-239 |
5.17e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 150.24 E-value: 5.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKST----LLRLINrleepSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQHFN--L 93
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNssL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 94 LSSKTVADNIAMPLRL-AGGFSRAEVDARVSELLARVGLSDHAR-KYPAQLSGGQKQRVGIARALACRPSILLCDEATSA 171
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 172 LDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-224 |
8.27e-41 |
|
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: 142.12 E-value: 8.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGlrrf 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAgGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-333 |
1.90e-40 |
|
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: 144.87 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEdvTALDAEG---LRRFRQRVGMIFQHFNLLSSKTVADN 102
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR--TLFDSRKgifLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 103 IAMPLRLAGGFSRAEVDARVSELLarvGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQ 182
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 183 LLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRR----FVFEAeRVDEDERHDDFA 258
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLARedqgSLIEG-VVAEHDQHYGLT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 259 HV--PGLILRLTFRGEATYAPLLGTV-------ARQTGVDYSI---LSGRIDRIKDTPYGQLTLAL-VGGD-LEAAMSQL 324
Cdd:TIGR02142 252 ALrlGGGHLWVPENLGPTGARLRLRVpardvslALQKPEATSIrniLPARVVEIEDSDIGRVGVVLeSGGKtLWARITRW 331
|
....*....
gi 489187600 325 NAADVHVEV 333
Cdd:TIGR02142 332 ARDELGIAP 340
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-229 |
3.75e-40 |
|
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: 140.65 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRFRQRVGMIFQHFNLLSS 96
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH--ERARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAMPLRLAGGFSRAEVDARVSELLARvgLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489187600 177 TASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:cd03224 168 VEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-229 |
5.43e-40 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 140.60 E-value: 5.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRV------------------AGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRI 62
Cdd:COG1134 4 MIEVENVSKSYRLyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 63 LVEGEdVTALDAeglrrfrqrVGMIFqHFNLlsskTVADNIamplRLAG---GFSRAEVDARVSELLARVGLSDHA---- 135
Cdd:COG1134 84 EVNGR-VSALLE---------LGAGF-HPEL----TGRENI----YLNGrllGLSRKEIDEKFDEIVEFAELGDFIdqpv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 136 RKYpaqlSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVM 215
Cdd:COG1134 145 KTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|....
gi 489187600 216 DGGAIVEQGDVADV 229
Cdd:COG1134 220 EKGRLVMDGDPEEV 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-288 |
8.57e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 141.78 E-value: 8.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaeglrrf 80
Cdd:COG4152 1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVG-----------MifqhfnllsskTVADNIAMPLRLAgGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQR 149
Cdd:COG4152 70 RRRIGylpeerglypkM-----------KVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 150 VGIARALACRPSILLCDEATSALDPQTTasvlQLLAEINRELKL---TIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDV 226
Cdd:COG4152 138 VQLIAALLHDPELLILDEPFSGLDPVNV----ELLKDVIRELAAkgtTVIFSSHQMELVEELCDRIVIINKGRKVLSGSV 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 227 ADVflhpqhptTRRFVFEAERVDEDERHDDFAHVPGLI--------LRLTFRGEATYAPLLGTVARQTGV 288
Cdd:COG4152 214 DEI--------RRQFGRNTLRLEADGDAGWLRALPGVTvveedgdgAELKLEDGADAQELLRALLARGPV 275
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-224 |
9.71e-40 |
|
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: 138.95 E-value: 9.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaeglrrfR 81
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAgGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-228 |
1.46e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 139.33 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagreipaLQPTR--LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglr 78
Cdd:PRK10771 1 MLKLTDITWLYH--------HLPMRfdLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 79 rfRQRVGMIFQHFNLLSSKTVADNIAM---P-LRLAggfsrAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIAR 154
Cdd:PRK10771 70 --RRPVSMLFQENNLFSHLTVAQNIGLglnPgLKLN-----AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
1.47e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 140.64 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGReipALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaEGLRRFR 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---ENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQH-FNLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFgPVNM--GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDV 226
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-217 |
2.91e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 138.37 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 R-QRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRaEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSR-QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
19-203 |
5.84e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 138.29 E-value: 5.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGlrrfrqrvGMIFQHFNLLSSKT 98
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTA 178
Cdd:PRK11248 87 VQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180
....*....|....*....|....*
gi 489187600 179 SVLQLLAEINRELKLTIVLITHEMD 203
Cdd:PRK11248 166 QMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-229 |
7.92e-39 |
|
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: 137.42 E-value: 7.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvaGrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRF 80
Cdd:COG0410 3 MLEVENLHAGY---G-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH--RIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRAEVD-ARVSELLARvgLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADlERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-220 |
8.10e-39 |
|
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: 135.42 E-value: 8.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 10 TYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFRQRVGMIFQ 89
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 90 HFNLLSSkTVADNIamplrlaggfsraevdarvsellarvglsdharkypaqLSGGQKQRVGIARALACRPSILLCDEAT 169
Cdd:cd03246 84 DDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489187600 170 SALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRvCDQVAVMDGGAI 220
Cdd:cd03246 125 SHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-204 |
1.28e-38 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 144.87 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 R-QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK10535 84 RrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAG-LERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489187600 160 PSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDV 204
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQV 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-242 |
1.49e-38 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 137.52 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKS-TLLRLINRLeePSG-----GRILVEGEDVTALDAEGlrrfrQRVGMIFQH----FNLLs 95
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKSlTCAAALGIL--PAGvrqtaGRVLLDGKPVAPCALRG-----RKIATIMQNprsaFNPL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 96 sKTVADNIAMPLRLAGgfsRAEVDARVSELLARVGLSDHAR---KYPAQLSGGQKQRVGIARALACRPSILLCDEATSAL 172
Cdd:PRK10418 96 -HTMHTHARETCLALG---KPADDATLTAALEAVGLENAARvlkLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 173 DPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-242 |
1.62e-38 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 137.21 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRL-----EEPSGGRILVEGEDVTALDAEGLRrFRQRVGMIFQHFNLL 94
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVD-LRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 95 SSkTVADNIAMPLRLAGGFSRAEVDARVSELLARVGL----SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATS 170
Cdd:PRK14239 99 PM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 171 ALDPQTTASVLQLLAEINRelKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
1.75e-38 |
|
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: 136.59 E-value: 1.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:cd03253 1 IEFENVTFAY-DPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQH---FNllssKTVADNIAMplrlaGGFSRAEVD----ARVSELLARV-GLSDharKYPAQ-------LSGGQ 146
Cdd:cd03253 76 -AIGVVPQDtvlFN----DTIGYNIRY-----GRPDATDEEvieaAKAAQIHDKImRFPD---GYDTIvgerglkLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 147 KQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGR----TTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-233 |
1.92e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 137.63 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaEGLRRF 80
Cdd:PRK13652 3 LIETRDLCYSYS---GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFN-LLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALAC 158
Cdd:PRK13652 77 RKFVGLVFQNPDdQIFSPTVEQDIAFgPINL--GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHP 233
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-226 |
2.13e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 137.12 E-value: 2.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 6 DVHKTYrvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVegedvtalDAEGLRRFRQRVG 85
Cdd:PRK11247 17 AVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA--------GTAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 86 MIFQHFNLLSSKTVADNIAMPLRlaGGFSRAEVDArvselLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLC 165
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLK--GQWRDAALQA-----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 166 DEATSALDPQTTASVLQLLAEINRELKLTIVLITHEmdvirrVCDQVAVMDGGAIVEQGDV 226
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD------VSEAVAMADRVLLIEEGKI 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
2.38e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 136.83 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHktYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:PRK13548 2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RqrvGMIFQHFNLLSSKTVADNIAMPlRLAGGFSRAEVDARVSELLARVGLSDHA-RKYPaQLSGGQKQRVGIARALA-- 157
Cdd:PRK13548 78 R---AVLPQHSSLSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLAHLAgRDYP-QLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 158 ----CRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-255 |
3.19e-38 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 143.46 E-value: 3.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 15 GREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGE----------DVTALDAEGLRRFR-QR 83
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 84 VGMIFQH--FNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHA---RKYPAQLSGGQKQRVGIARALAC 158
Cdd:PRK10261 106 MAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTT 238
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYT 265
|
250
....*....|....*..
gi 489187600 239 RRFVFEAERVDEDERHD 255
Cdd:PRK10261 266 RALLAAVPQLGAMKGLD 282
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
5.18e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 136.01 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHktYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF 80
Cdd:COG4559 1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 R----QRVGMIFqHFnllsskTVADNIAMPlRLAGGFSRAEVDARVSELLARVGLSDHA-RKYPaQLSGGQKQRVGIARA 155
Cdd:COG4559 77 RavlpQHSSLAF-PF------TVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAHLAgRSYQ-TLSGGEQQRVQLARV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 156 LA-------CRPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
..
gi 489187600 229 VF 230
Cdd:COG4559 227 VL 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-230 |
6.53e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 136.45 E-value: 6.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAG-REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEG-LRR 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMIFQhfnLLSSKTVADNIAMPLRLAG---GFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGIARA 155
Cdd:PRK13646 83 VRKRIGMVFQ---FPESQLFEDTVEREIIFGPknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-221 |
1.51e-37 |
|
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: 133.15 E-value: 1.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 5 HDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaeglRRFRQRV 84
Cdd:cd03226 3 ENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 85 GMIFQHFNL-LSSKTVADNIAMPLRLAGgfsraEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSIL 163
Cdd:cd03226 74 GYVMQDVDYqLFTDSVREELLLGLKELD-----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 164 LCDEATSALDPQTtasvLQLLAEINRELKL---TIVLITHEMDVIRRVCDQVAVMDGGAIV 221
Cdd:cd03226 149 IFDEPTSGLDYKN----MERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-224 |
2.13e-37 |
|
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: 141.11 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:COG5265 358 VRFENVSFGYD-PERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQH---FNllssKTVADNIAMPlRLagGFSRAEVD--ARVSELLARV-GLSDharKYPAQ-------LSGGQKQ 148
Cdd:COG5265 433 -AIGIVPQDtvlFN----DTIAYNIAYG-RP--DASEEEVEaaARAAQIHDFIeSLPD---GYDTRvgerglkLSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 149 RVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVlITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLV-IAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-201 |
2.69e-37 |
|
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: 132.60 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvaGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrF 80
Cdd:COG4133 2 MLEAENLSCRRG--ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----Y 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGgfsRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:COG4133 74 RRRLAYLGHADGLKPELTVRENLRFWAALYG---LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEiNRELKLTIVLITHE 201
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-247 |
3.70e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 134.57 E-value: 3.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGR-EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTA-LDAEGLRR 79
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMIFQhF--NLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLSDH-ARKYPAQLSGGQKQRVGIARA 155
Cdd:PRK13641 83 LRKKVSLVFQ-FpeAQLFENTVLKDVEFgPKNF--GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ- 234
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEw 238
|
250 260
....*....|....*....|
gi 489187600 235 -------HPTTRRFVFEAER 247
Cdd:PRK13641 239 lkkhyldEPATSRFASKLEK 258
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-228 |
5.15e-37 |
|
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: 132.74 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVhkTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:cd03251 1 VEFKNV--TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHfNLLSSKTVADNIAMPLRLAGgfsraevDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:cd03251 77 -QIGLVSQD-VFLFNDTVAENIAYGRPGAT-------REEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVAD 228
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLmkNR----TTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEE 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-239 |
5.75e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 135.25 E-value: 5.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKS----TLLRLINRLEEPSGGRILVEGEDVTALDAeglRRFRQRVG----MIFQH--FNLLSSK 97
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISE---KERRNLVGaevaMIFQDpmTSLNPCY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARK---YPAQLSGGQKQRVGIARALACRPSILLCDEATSALDP 174
Cdd:PRK11022 107 TVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 175 QTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:PRK11022 187 TIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-243 |
1.82e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 132.08 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSG-----GRILVEGEDVTALDAEgLRRFRQRVGMIFQHFNLLS 95
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVN-LNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 96 sKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHAR----KYPAQLSGGQKQRVGIARALACRPSILLCDEATSA 171
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKhkihKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 172 LDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDG-----GAIVEQGDVADVFLHPQHPTTRRFVF 243
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREYVL 257
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-229 |
2.41e-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: 2.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGRE-IPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILV----EGEDVTALDAE 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 76 GLRRFRQRVGMIFQHFNLLSSKTVADNI--AMPLRLAGGFSRAevdaRVSELLARVGLSD-HAR----KYPAQLSGGQKQ 148
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLteAIGLELPDELARM----KAVITLKMVGFDEeKAEeildKYPDELSEGERH 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 149 RVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEE 514
|
.
gi 489187600 229 V 229
Cdd:TIGR03269 515 I 515
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-242 |
2.54e-36 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 131.83 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEE--PSG---GRILVEGEDVTA--LDAEGLRRfrqRVGMIFQHFN 92
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYApdVDPVEVRR---RIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 93 LLSsKTVADNIAMPLRLAGgfSRAEVDARVSELLARVGL----SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEA 168
Cdd:PRK14243 102 PFP-KSIYDNIAYGARING--YKGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 169 TSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRVCDQVAVMDG---------GAIVEQGDVADVFLHPQHPTTR 239
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNVeltegggryGYLVEFDRTEKIFNSPQQQATR 256
|
...
gi 489187600 240 RFV 242
Cdd:PRK14243 257 DYV 259
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-224 |
3.19e-36 |
|
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: 130.31 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGReiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALdaeGLRRFR 81
Cdd:cd03244 3 IEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSkTVADNIAmPLrlaGGFSraevDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:cd03244 78 SRISIIPQDPVLFSG-TIRSNLD-PF---GEYS----DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLlaeINRELK-LTIVLITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKT---IREAFKdCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-224 |
3.61e-36 |
|
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: 129.64 E-value: 3.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALdAEGLRRfr 81
Cdd:cd03268 1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qrVGMIFQHFNLLSSKTVADNIAMPLRLAGGfsraeVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03268 74 --IGALIEAPGFYPNLTARENLRLLARLLGI-----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGI-TVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-224 |
5.92e-36 |
|
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: 136.77 E-value: 5.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFR 81
Cdd:TIGR02203 331 VEFRNVTFRYP--GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSkTVADNIAMplrlagGFSRAEVDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:TIGR02203 406 RQVALVSQDVVLFND-TIANNIAY------GRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElKLTIVlITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQG-RTTLV-IAHRLSTIEKA-DRIVVMDDGRIVERG 549
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-230 |
6.37e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 130.98 E-value: 6.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfrqRVGMIFQH-FNLLS 95
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR---KIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 96 SKTVADNIAMPLRlAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQ 175
Cdd:PRK13642 96 GATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 176 TTASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13642 175 GRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-233 |
1.21e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 130.49 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAgreIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDvtALDAEGLRRF 80
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNL-LSSKTVADNIAM-PLRLAggFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALAC 158
Cdd:PRK13644 76 RKLVGIVFQNPETqFVGRTVEEDLAFgPENLC--LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIrRVCDQVAVMDGGAIVEQGDVADVFLHP 233
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
26-239 |
1.32e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 131.57 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPS----GGRILVEGEDVTALDAEGLRRF-RQRVGMIFQHFN--LLSSKT 98
Cdd:COG4170 28 LTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKIiGREIAMIFQEPSscLDPSAK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNI--AMPLRLAGG------FSRAEvdaRVSELLARVGLSDHA---RKYPAQLSGGQKQRVGIARALACRPSILLCDE 167
Cdd:COG4170 108 IGDQLieAIPSWTFKGkwwqrfKWRKK---RAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQPRLLIADE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 168 ATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:COG4170 185 PTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTK 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
10-229 |
2.33e-35 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 129.14 E-value: 2.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 10 TYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglRRFRQRVGMIFQ 89
Cdd:PRK10575 18 SFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 90 HFNLLSSKTVADNIAM---PLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCD 166
Cdd:PRK10575 93 QLPAAEGMTVRELVAIgryPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 167 EATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:PRK10575 173 EPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-224 |
3.05e-35 |
|
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: 135.47 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGReiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLSSkTVADNIAmplrlagGFSRAEVDaRVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:TIGR03797 528 -QLGVVLQNGRLMSG-SIFENIA-------GGAPLTLD-EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRL 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAeinrELKLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-224 |
2.74e-34 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 132.92 E-value: 2.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGR-EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRf 80
Cdd:TIGR00958 479 IEFQDVSFSY--PNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR- 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 rqRVGMIFQHfNLLSSKTVADNIAMPLRLAggfSRAEVDARVSELLARVGLSDHARKYP-------AQLSGGQKQRVGIA 153
Cdd:TIGR00958 556 --QVALVGQE-PVLFSGSVRENIAYGLTDT---PDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 154 RALACRPSILLCDEATSALDpqttASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-230 |
5.88e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.39 E-value: 5.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYR----VAGReipALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEG 76
Cdd:PRK13643 1 MIKFEKVNYTYQpnspFASR---ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 -LRRFRQRVGMIFQH-FNLLSSKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGI 152
Cdd:PRK13643 78 eIKPVRKKVGVVFQFpESQLFEETVLKDVAFgPQNF--GIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 153 ARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-230 |
6.04e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 126.28 E-value: 6.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTA--LDAEGLRRFRQRVGMIFQ--HFN 92
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 93 LLSsKTVADNIAM-PLRLagGFSRAEVDARVSELLARVGL-SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATS 170
Cdd:PRK13645 103 LFQ-ETIEKDIAFgPVNL--GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 171 ALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
6.90e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.20 E-value: 6.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVA-GREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRR 79
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY--KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRqRVGMIFQhfNLL----SSKTVADNIAMPLR------LAGGFSRAEVDaRVSELLARV--GLSDHARKYPAQLSGGQK 147
Cdd:COG1101 79 AK-YIGRVFQ--DPMmgtaPSMTIEENLALAYRrgkrrgLRRGLTKKRRE-LFRELLATLglGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 148 QRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEM-DVIrRVCDQVAVMDGGAIV 221
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeQAL-DYGNRLIMMHEGRII 228
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
7.61e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 130.72 E-value: 7.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRR-- 79
Cdd:PRK11160 339 LTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQai 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 --FRQRVgMIFqhfnllsSKTVADNIAMPLRLAGgfsraevDARVSELLARVGLSDHARKYPA----------QLSGGQK 147
Cdd:PRK11160 417 svVSQRV-HLF-------SATLRDNLLLAAPNAS-------DEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 148 QRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElKlTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGD 225
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN-K-TVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-221 |
1.11e-33 |
|
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: 121.77 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVagreIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAL---DAEglr 78
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsprDAR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 79 rfRQRVGMIFQhfnllssktvadniamplrlaggfsraevdarvsellarvglsdharkypaqLSGGQKQRVGIARALAC 158
Cdd:cd03216 74 --RAGIAMVYQ----------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIV 221
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-242 |
2.25e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 124.44 E-value: 2.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 7 VHKTYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEP-SG----GRILVEGEDVtaLDAEGLRRFR 81
Cdd:PRK14271 25 VNLTLGFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvSGyrysGDVLLGGRSI--FNYRDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSsKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARK----YPAQLSGGQKQRVGIARALA 157
Cdd:PRK14271 101 RRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDrlsdSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 158 CRPSILLCDEATSALDPQTTASVLQLLAEINRelKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPT 237
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAE 257
|
....*
gi 489187600 238 TRRFV 242
Cdd:PRK14271 258 TARYV 262
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-220 |
3.47e-33 |
|
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: 122.58 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:cd03248 12 VKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHfNLLSSKTVADNIAMPL------RLAGGFSRAEVDARVSELlaRVGLSDHARKYPAQLSGGQKQRVGIARA 155
Cdd:cd03248 89 -KVSLVGQE-PVLFARSLQDNIAYGLqscsfeCVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLAEINRelKLTIVLITHEMDVIRRVcDQVAVMDGGAI 220
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-228 |
3.70e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 128.98 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDvtaLDAEGLRRFR 81
Cdd:PRK11176 342 IEFRNVTFTY--PGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSkTVADNIAMPLRlaGGFSRAEVD-----ARVSELLARV--GLSDHARKYPAQLSGGQKQRVGIAR 154
Cdd:PRK11176 417 NQVALVSQNVHLFND-TIANNIAYART--EQYSREQIEeaarmAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 155 ALACRPSILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVAD 228
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEKA-DEILVVEDGEIVERGTHAE 564
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
26-242 |
7.21e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.95 E-value: 7.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:PRK11831 28 LTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLA 185
Cdd:PRK11831 108 PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIS 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 186 EINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDvADVFLHPQHPTTRRFV 242
Cdd:PRK11831 188 ELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS-AQALQANPDPRVRQFL 243
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
10-230 |
9.12e-33 |
|
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: 127.56 E-value: 9.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 10 TYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFrqrVGMIFQ 89
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH---IGYLPQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 90 HFNLLSSkTVADNIAmplRLAGGFSRAEVDA----RVSELLAR--------VGLSDHArkypaqLSGGQKQRVGIARALA 157
Cdd:COG4618 414 DVELFDG-TIAENIA---RFGDADPEKVVAAaklaGVHEMILRlpdgydtrIGEGGAR------LSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 158 CRPSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIrRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-224 |
1.82e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 127.00 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVhkTYRVAGREiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:PRK13657 335 VEFDDV--SFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRR-- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHfNLLSSKTVADNI------AMPLRLAGGFSRAEVdarvSELLAR--VGLSDHARKYPAQLSGGQKQRVGIA 153
Cdd:PRK13657 410 -NIAVVFQD-AGLFNRSIEDNIrvgrpdATDEEMRAAAERAQA----HDFIERkpDGYDTVVGERGRQLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 154 RALACRPSILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELmkGR----TTFIIAHRLSTVRNA-DRILVFDNGRVVESG 551
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
2.04e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 120.96 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRf 80
Cdd:COG4604 1 MIEIKNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 rqRVGMIFQHFNLLSSKTVADNIamplrlagGFSR---------AEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVG 151
Cdd:COG4604 76 --RLAILRQENHINSRLTVRELV--------AFGRfpyskgrltAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 152 IARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-233 |
2.17e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 122.65 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVE----GEDVTALDAEG---------LRRFRQR 83
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITnpyskkiknFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 84 VGMIFQ--HFNLLSSKTVADNIAMPLRLagGFSRAEVDARVSELLARVGL-SDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:PRK13631 118 VSMVFQfpEYQLFKDTIEKDIMFGPVAL--GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHP 233
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
20-224 |
3.11e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 120.89 E-value: 3.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRL---EEPSGGRILVEGEDVTALD--AEGLRRFRQRVGMIFQHFNLL 94
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlARDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 95 SSKTVADNIAMPLRLAGGFSRA-------EVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDE 167
Cdd:PRK09984 99 NRLSVLENVLIGALGSTPFWRTcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 168 ATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-230 |
3.72e-32 |
|
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: 120.19 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVhkTYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEP-SGGRILVEGEDvtaLDAEGLRR 79
Cdd:COG1119 3 LLELRNV--TVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGER---RGGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMI--FQHFNLLSSKTVADNIamplrLAGGFS--------RAEVDARVSELLARVGLSDHARKYPAQLSGGQKQR 149
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVLDVV-----LSGFFDsiglyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 150 VGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
.
gi 489187600 230 F 230
Cdd:COG1119 231 L 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-212 |
6.01e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 119.05 E-value: 6.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHktYRVAGREIpaLQPTRLNIQAGQiFGLI-GHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrR 79
Cdd:PRK10247 7 LLQLQNVG--YLAGDAKI--LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 FRQRVGMIFQHFNLLSsKTVADNIAMPLRLAGgfSRAEVDARVSELlARVGLSDHARKYP-AQLSGGQKQRVGIARALAC 158
Cdd:PRK10247 79 YRQQVSYCAQTPTLFG-DTVYDNLIFPWQIRN--QQPDPAIFLDDL-ERFALPDTILTKNiAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQV 212
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-215 |
6.95e-32 |
|
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: 124.71 E-value: 6.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGreiPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfr 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qRVGMIFQHFNLLsSKTVADNIAMPLRLAGgfsraevDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRV 150
Cdd:TIGR02857 397 -QIAWVPQHPFLF-AGTIAENIRLARPDAS-------DAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEI--NRelklTIVLITHEmDVIRRVCDQVAVM 215
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGR----TVLLVTHR-LALAALADRIVVL 529
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-234 |
1.41e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.59 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvaGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRf 80
Cdd:COG1137 3 TLEAENLVKSYG--KRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP---MHK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGM--------IFQhfNLlsskTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSdHARKYPA-QLSGGQKQRVG 151
Cdd:COG1137 75 RARLGIgylpqeasIFR--KL----TVEDNILAVLELRK-LSKKEREERLEELLEEFGIT-HLRKSKAySLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 152 IARALACRPSILLCDEATSALDPQTTASVLQLLaeinRELK-LTI-VLIT-HEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDPIAVADIQKII----RHLKeRGIgVLITdHNVRETLGICDRAYIISEGKVLAEGTPEE 222
|
....*.
gi 489187600 229 VFLHPQ 234
Cdd:COG1137 223 ILNNPL 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-224 |
5.97e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLrrfrQRVGMI--FQHFNLLSSKTVADN- 102
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI----ARMGVVrtFQHVRLFREMTVIENl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 103 -IAMPLR-----LAG-----GFSRAEVDA--RVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEAT 169
Cdd:PRK11300 102 lVAQHQQlktglFSGllktpAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 170 SALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-224 |
6.39e-31 |
|
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: 116.48 E-value: 6.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRV------------------AGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRIL 63
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 64 VEGEDVTALDaeglrrfrqrVGMIFQhfnllSSKTVADNIAMPLRLAgGFSRAEVDARVSELLARVGLSDHA----RKYp 139
Cdd:cd03220 81 VRGRVSSLLG----------LGGGFN-----PELTGRENIYLNGRLL-GLSRKEIDEKIDEIIEFSELGDFIdlpvKTY- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 140 aqlSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGA 219
Cdd:cd03220 144 ---SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGK 219
|
....*
gi 489187600 220 IVEQG 224
Cdd:cd03220 220 IRFDG 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-242 |
7.77e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 119.75 E-value: 7.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTalDAEGLRRfrqRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAER---GVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGGfSRAEVDARV---SELLARVGLSDhaRKyPAQLSGGQKQRVGIARALACRPSILLCDEATSALDpqtTASVLQ 182
Cdd:PRK11000 99 GLKLAGA-KKEEINQRVnqvAEVLQLAHLLD--RK-PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD---AALRVQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 183 LLAEINR---ELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHpttrRFV 242
Cdd:PRK11000 172 MRIEISRlhkRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPAN----RFV 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-242 |
1.31e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 118.79 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvAGReIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrrf 80
Cdd:PRK11650 3 GLKLQAVRKSY--DGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQR-VGMIFQHFNLLSSKTVADNIAMPLRLAgGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACR 159
Cdd:PRK11650 74 ADRdIAMVFQNYALYPHMSVRENMAYGLKIR-GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 160 PSILLCDEATSALDPQTTAsvlQLLAEI---NRELKLTIVLITHemdvirrvcDQV---------AVMDGGAIvEQ-GDV 226
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRV---QMRLEIqrlHRRLKTTSLYVTH---------DQVeamtladrvVVMNGGVA-EQiGTP 219
|
250
....*....|....*.
gi 489187600 227 ADVFlhpQHPTTrRFV 242
Cdd:PRK11650 220 VEVY---EKPAS-TFV 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
1.44e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 117.49 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTY-RVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRI------------LVEGED 68
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 69 VTALDAEGLRRF---------RQRVGMIFQ--HFNLLSSKTVADNIAMPLRLagGFSRAEVDARVSELLARVGLS-DHAR 136
Cdd:PRK13651 83 VLEKLVIQKTRFkkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSM--GVSKEEAKKRAAKYIELVGLDeSYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 137 KYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMD 216
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|...
gi 489187600 217 GGAIVEQGDVADV 229
Cdd:PRK13651 240 DGKIIKDGDTYDI 252
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
26-229 |
1.63e-30 |
|
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: 115.31 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRFRQRVG------MIFQHFnllsskTV 99
Cdd:TIGR03410 21 LEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH--ERARAGIAyvpqgrEIFPRL------TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 ADNIAMPLRLAGGFSRaEVDARVSEL-------LARVGlsdharkypAQLSGGQKQRVGIARALACRPSILLCDEATSAL 172
Cdd:TIGR03410 93 EENLLTGLAALPRRSR-KIPDEIYELfpvlkemLGRRG---------GDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 173 DPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:TIGR03410 163 QPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-224 |
2.45e-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: 115.12 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRV----AG-------------REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILV 64
Cdd:cd03267 1 IEVSNLSKSYRVyskePGligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 65 EGEdvtaLDAEGLRRFRQRVGMIF-QHFNLLSSKTVADNIAMpLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLS 143
Cdd:cd03267 81 AGL----VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYL-LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 144 GGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQ 223
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
.
gi 489187600 224 G 224
Cdd:cd03267 236 G 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
3.28e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 116.44 E-value: 3.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVtaldAEGLRRFR 81
Cdd:PRK13537 8 IDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNiampLRLAG---GFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALAC 158
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVREN----LLVFGryfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
26-240 |
5.79e-30 |
|
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: 114.18 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGlrrfRQRVGMIF--QHFNLLSSKTVADNI 103
Cdd:cd03218 21 LSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLGIGYlpQEASIFRKLTVEENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 104 AMPLRLAGgFSRAEVDARVSELLARVGLSdHARKYPA-QLSGGQKQRVGIARALACRPSILLCDEATSALDPQTtasvLQ 182
Cdd:cd03218 97 LAVLEIRG-LSKKEREEKLEELLEEFHIT-HLRKSKAsSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA----VQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 183 LLAEINRELKLT-I-VLIT-HEMDVIRRVCDQVAVMDGGAIVEQGDVADVFlhpQHPTTRR 240
Cdd:cd03218 171 DIQKIIKILKDRgIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIA---ANELVRK 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-292 |
1.35e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 115.18 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRVAGR-----------------EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRIL 63
Cdd:COG4586 1 IIEVENLSKTYRVYEKepglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 64 VEGEDVTALDaeglRRFRQRVGMIF-QHFNLLSSKTVADNiampLRLAG---GFSRAEVDARVSELLARVGLSDHARKyP 139
Cdd:COG4586 81 VLGYVPFKRR----KEFARRIGVVFgQRSQLWWDLPAIDS----FRLLKaiyRIPDAEYKKRLDELVELLDLGELLDT-P 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 140 A-QLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:COG4586 152 VrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 219 AIVEQGDVADvfLHPQHPTTRRFVFEAERVDEDERHDDFAHV---PGLILRLTFRGEATYAPLLGTVARQTGV-DYSI 292
Cdd:COG4586 232 RIIYDGSLEE--LKERFGPYKTIVLELAEPVPPLELPRGGEVierEGNRVRLEVDPRESLAEVLARLLARYPVrDLTI 307
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-224 |
3.18e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 114.54 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaeGLRRFR 81
Cdd:PRK13536 42 IDLAGVSKSYG----DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRaEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTR-EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-231 |
4.35e-29 |
|
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: 116.83 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLE--EPSGGRIL-----------VE-----GE-------------- 67
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyVErpskvGEpcpvcggtlepeev 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 68 DVTALDAEGLRRFRQRVGMIFQH-FNLLSSKTVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQ 146
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIG-YEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 147 KQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGD- 225
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTp 253
|
....*...
gi 489187600 226 --VADVFL 231
Cdd:TIGR03269 254 deVVAVFM 261
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-224 |
9.15e-29 |
|
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: 109.32 E-value: 9.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrFR 81
Cdd:cd03247 1 LSINNVSFSY--PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSkTVADNIAmplrlaggfsraevdarvsellarvglsdharkypAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03247 75 SLISVLNQRPYLFDT-TLRNNLG-----------------------------------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 162 ILLCDEATSALDPQTTASVLQLLAEINRElkLTIVLITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-224 |
1.04e-28 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 110.44 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLI-NRLEEPS--GGRILVEGEDVTAldaeglRRFRQRVGMIFQHFNLLSSK 97
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPRKP------DQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNI--AMPLRLAGGFSRAEVDARV-SELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDP 174
Cdd:cd03234 97 TVRETLtyTAILRLPRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489187600 175 QTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-234 |
2.24e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 112.66 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 33 IFGLighSGAGKSTLLRLINRLEEPSGGRI------LVEGEDVTALDAEglrrfRQRVGMIFQHFNLLSSKTVADNIAMP 106
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIvlngrvLFDAEKGICLPPE-----KRRIGYVFQDARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 107 LRlagGFSRAEVDaRVSELLarvGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAE 186
Cdd:PRK11144 101 MA---KSMVAQFD-KIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489187600 187 INRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-229 |
4.08e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 114.11 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRFRQRVGMIFQHFNLLSSKTV 99
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAAQLGIGIIYQELSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 ADNI---AMPLRLAGGFS---RAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALd 173
Cdd:PRK09700 98 LENLyigRHLTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL- 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 174 pqTTASVLQLLAEINRELK--LTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:PRK09700 177 --TNKEVDYLFLIMNQLRKegTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
31-242 |
1.20e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.47 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALD----AEGLRRFRQRVGMIFQHFN----LLSSKTVADN 102
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalSEAERRRLLRTEWGFVHQHprdgLRMQVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 103 IAMPLRLAGGFSRAEVDARVSELLARVGLsDHAR--KYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASV 180
Cdd:PRK11701 112 IGERLMAVGARHYGDIRATAGDWLERVEI-DAARidDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 181 LQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:PRK11701 191 LDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHPYTQLLV 252
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-230 |
1.73e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 108.56 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEdvtALD--AEGLRRFRQRVGMIFQHFNLLSS 96
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDysKRGLLALRQQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVAD-NIAMPLRLAGgFSRAEVDARVSELLARVGlSDHARKYPAQ-LSGGQKQRVGIARALACRPSILLCDEATSALDP 174
Cdd:PRK13638 92 YTDIDsDIAFSLRNLG-VPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 175 ----QTTASVLQLLAEINRelkltIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK13638 170 agrtQMIAIIRRIVAQGNH-----VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
26-230 |
2.11e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.79 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglRRFRQRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:PRK11231 23 LSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQHHLTPEGITVRELVAY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 ---P-LRLAGGFSRAEvDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVL 181
Cdd:PRK11231 100 grsPwLSLWGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELM 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489187600 182 QLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:PRK11231 179 RLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-239 |
8.94e-27 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 107.97 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEP----SGGRILVEGEDVTALDAEGLRRF-RQRVGMIFQHFN--LLSSKT 98
Cdd:PRK15093 28 MTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLvGHNVSMIFQEPQscLDPSER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNI--AMPLRLAGGFSRAEVD---ARVSELLARVGLSDHA---RKYPAQLSGGQKQRVGIARALACRPSILLCDEATS 170
Cdd:PRK15093 108 VGRQLmqNIPGWTYKGRWWQRFGwrkRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPRLLIADEPTN 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 171 ALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQHPTTR 239
Cdd:PRK15093 188 AMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQ 256
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-246 |
5.61e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.85 E-value: 5.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfrqRVGMIFQHFNLLSS 96
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR---RVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAM---PLRlaGGFSRAEVDAR--VSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSA 171
Cdd:PRK09536 92 FDVRQVVEMgrtPHR--SRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 172 LDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLhpqhPTTRRFVFEAE 246
Cdd:PRK09536 170 LDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLT----ADTLRAAFDAR 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-228 |
1.41e-25 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 106.63 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaEGLRRFRQR-VGMIFQHFNLLSSKT 98
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF---NGPKSSQEAgIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMPLRLAGGFSR-------AEVDArvseLLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSA 171
Cdd:PRK10762 96 IAENIFLGREFVNRFGRidwkkmyAEADK----LLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 172 LDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVM-DGGAIVEQgDVAD 228
Cdd:PRK10762 172 LTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFrDGQFIAER-EVAD 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-224 |
1.62e-25 |
|
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: 101.33 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFRQRVGMIFQHFNLLSSkT 98
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNiampLRLAGGFSRAEVDA--RVSEllarVGLSdharkypaqLSGGQKQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:cd03369 98 IRSN----LDPFDEYSDEEIYGalRVSE----GGLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489187600 177 TAsvlqLLAEINREL--KLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQG 224
Cdd:cd03369 161 DA----LIQKTIREEftNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-226 |
1.67e-25 |
|
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: 101.71 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaldaeglRRFR 81
Cdd:TIGR03740 1 LETKNLSKRFG----KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSKTVADNIAMPLRLAGgfsraEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPS 161
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVHTTLLG-----LPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 162 ILLCDEATSALDPQTtasvLQLLAEINRELK---LTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDV 226
Cdd:TIGR03740 145 LLILDEPTNGLDPIG----IQELRELIRSFPeqgITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
1.88e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 4 FHDVHKTYrvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILV--------------EGEDV 69
Cdd:COG0488 1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrigylpqeppLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 70 TALDA--EGLRRFRQrvgmIFQHFNLLSSKTvADNIAMPLRLA---------GGFsraEVDARVSELLARVGLS--DHAR 136
Cdd:COG0488 77 TVLDTvlDGDAELRA----LEAELEELEAKL-AEPDEDLERLAelqeefealGGW---EAEARAEEILSGLGFPeeDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 137 KYpAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTAsvlqLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMD 216
Cdd:COG0488 149 PV-SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE----WLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD 223
|
....
gi 489187600 217 GGAI 220
Cdd:COG0488 224 RGKL 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-228 |
2.45e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.47 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLR-LINRLeePSGGRILVEGEDVTALDaegLRRFRQRVGMIFQHFNLLSSk 97
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELD---PESWRKHLSWVGQNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNIAMplrlagGFSRAEvDARVSELLARVGLSDHARKYP-----------AQLSGGQKQRVGIARALACRPSILLCD 166
Cdd:PRK11174 438 TLRDNVLL------GNPDAS-DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 167 EATSALDPQTTASVLQLLAEINRelKLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQGDVAD 228
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-220 |
3.04e-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: 99.81 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRFRQRVGMI---FQHFNLLSS 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR--DAIRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAMPlrlaggfsraevdarvsellarvglsdharkypAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:cd03215 93 LSVAENIALS---------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489187600 177 TASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:cd03215 140 KAEIYRLIRELADAGK-AVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-224 |
5.71e-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: 99.55 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLR-LINRLEEPS-GGRILVEGEDVTaldaegLRRFRQRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGvSGEVLINGRPLD------KRSFRKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGgfsraevdarvsellarvglsdharkypaqLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLL- 184
Cdd:cd03213 106 AAKLRG------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLr 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489187600 185 --AEINRelklTIVLITHE-MDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03213 156 rlADTGR----TIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-229 |
9.10e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.22 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 3 EFHDVHKTYrvagreiP---ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV---TALDAeg 76
Cdd:PRK11288 6 SFDGIGKTF-------PgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 lrrFRQRVGMIFQHFNLLSSKTVADNI---AMPLRLaGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIA 153
Cdd:PRK11288 77 ---LAAGVAIIYQELHLVPEMTVAENLylgQLPHKG-GIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 154 RALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLtIVLITHEMDVIRRVCDQVAVM-DGGAIVEQGDVADV 229
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFkDGRYVATFDDMAQV 228
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-218 |
1.04e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 104.82 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGlrrfRQRVGMIFQHFNLLSSKTVADNIAM 105
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT----RRRVGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLaggF--SRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQL 183
Cdd:NF033858 363 HARL---FhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190
....*....|....*....|....*....|....*
gi 489187600 184 LAEINRELKLTIVLITHEMDVIRRvCDQVAVMDGG 218
Cdd:NF033858 440 LIELSREDGVTIFISTHFMNEAER-CDRISLMHAG 473
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-224 |
1.12e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfrqRVGMIFQHFNLLSSKTVADNIA- 104
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQNATTPGDITVQELVAr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 105 -----MPLrlaggFSR--AEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTT 177
Cdd:PRK10253 105 gryphQPL-----FTRwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489187600 178 ASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-200 |
1.46e-24 |
|
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: 103.98 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfrqRVGMIFQHFNLLSSkT 98
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR---RVSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNiampLRLAggfsRAEV-DARVSELLARVGLSDHARKYP-----------AQLSGGQKQRVGIARALACRPSILLCD 166
Cdd:TIGR02868 425 VREN----LRLA----RPDAtDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....
gi 489187600 167 EATSALDPQTTASVLQLLAEINRElkLTIVLITH 200
Cdd:TIGR02868 497 EPTEHLDAETADELLEDLLAALSG--RTVVLITH 528
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-228 |
3.71e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRIlVEGEDVtaldaeglrrf 80
Cdd:COG0488 315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 rqRVGMIFQHFNLL-SSKTVADNIAmplRLAGGFSRAEvdarVSELLARVGLS-DHARKYPAQLSGGQKQRVGIARALAC 158
Cdd:COG0488 379 --KIGYFDQHQEELdPDKTVLDELR---DGAPGGTEQE----VRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 159 RPSILLCDEATSALDPQTtasvLQLLAEINRELKLTIVLITHEMDVIRRVCDQV-AVMDGGAIVEQGDVAD 228
Cdd:COG0488 450 PPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRYFLDRVATRIlEFEDGGVREYPGGYDD 516
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-224 |
5.69e-24 |
|
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: 103.17 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 9 KTYRVAGReiPALQptRLNIQ--AGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV-TALDAeglrrFRQRVG 85
Cdd:TIGR01257 936 KIFEPSGR--PAVD--RLNITfyENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA-----VRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 86 MIFQHFNLLSSKTVADNIAMPLRLAGGfSRAEVDARVSELLARVGLSdHARKYPAQ-LSGGQKQRVGIARALACRPSILL 164
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGR-SWEEAQLEMEAMLEDTGLH-HKRNEEAQdLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 165 CDEATSALDPQTTASVLQLLaeINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
13-230 |
6.48e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 98.37 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 13 VAGReipaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLeEPSGGRILVEGEDVTALDAEGLRRFRqrvGMIFQHfn 92
Cdd:COG4138 8 VAGR----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR---AYLSQQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 93 llsSKTVAdniAMP------LRLAGGFSRAEVDARVSELLARVGLSDharKYP---AQLSGGQKQRVGIARAL-----AC 158
Cdd:COG4138 78 ---QSPPF---AMPvfqylaLHQPAGASSEAVEQLLAQLAEALGLED---KLSrplTQLSGGEWQRVRLAAVLlqvwpTI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 159 RPS--ILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVF 230
Cdd:COG4138 149 NPEgqLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-224 |
7.50e-24 |
|
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: 102.51 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFR 81
Cdd:TIGR01193 474 IVINDVSYSY---GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRV--------GMIFQhfNLL---SSKTVADNIAMPLRLAggfsraEVDARVSELLARVG--LSDHArkypAQLSGGQKQ 148
Cdd:TIGR01193 551 NYLpqepyifsGSILE--NLLlgaKENVSQDEIWAACEIA------EIKDDIENMPLGYQteLSEEG----SSISGGQKQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 149 RVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElklTIVLITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-205 |
1.25e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 96.95 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEE--PSGGRILVEGEDVTaldaeglrrfrqrvgmifqhfnllSSKTVADNI 103
Cdd:COG2401 51 LEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG------------------------REASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 104 AmplrlaggfSRAEVDARVsELLARVGLSDHA--RKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVL 181
Cdd:COG2401 107 G---------RKGDFKDAV-ELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180
....*....|....*....|....
gi 489187600 182 QLLAEINRELKLTIVLITHEMDVI 205
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYDVI 200
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-229 |
1.04e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 16 REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRF--------RQRVGMI 87
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 88 fqhfnllSSKTVADNIAM------PLRLAGGFSRAEVDARVSELLAR-----VGLSDHARkypaQLSGGQKQRVGIARAL 156
Cdd:COG3845 349 -------PDMSVAENLILgryrrpPFSRGGFLDRKAIRAFAEELIEEfdvrtPGPDTPAR----SLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-233 |
1.24e-22 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.63 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 9 KTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFRQRVGMIF 88
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 89 QHfNLLSSKTVADNIAM--PLRLAGGFSRAEVDARVSELLARV--GLSDHARKYPAQLSGGQKQRVGIARALACRPSILL 164
Cdd:PRK10789 396 QT-PFLFSDTVANNIALgrPDATQQEIEHVARLASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 165 CDEATSALDPQTTASVLQLLAEINRelKLTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVADVFLHP 233
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEA-SEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-222 |
3.03e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 97.89 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagreiPALQPT----RLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALdaeGL 77
Cdd:PLN03130 1238 IKFEDVVLRYR------PELPPVlhglSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GL 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 78 RRFRQRVGMIFQHfNLLSSKTVADNIamplrlaGGFSRAEvDARVSELLARVGLSDHARKYPAQL-----------SGGQ 146
Cdd:PLN03130 1309 MDLRKVLGIIPQA-PVLFSGTVRFNL-------DPFNEHN-DADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQ 1379
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 147 KQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEinrELK-LTIVLITHEMDVIRRvCDQVAVMDGGAIVE 222
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE---EFKsCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-220 |
5.02e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 18 IPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEePSG---GRILVEGEDVTA---LDAEglrrfRQRVGMIFQHF 91
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQAsniRDTE-----RAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 92 NLLSSKTVADNIAM---PLRlAGGFSRAEVDARVSELLARVGLS-DHARKYpAQLSGGQKQRVGIARALACRPSILLCDE 167
Cdd:PRK13549 92 ALVKELSVLENIFLgneITP-GGIMDYDAMYLRAQKLLAQLKLDiNPATPV-GNLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 168 ATSALdpqtTASVLQLLAEINRELK---LTIVLITHEMDVIRRVCDQVAVM-DGGAI 220
Cdd:PRK13549 170 PTASL----TESETAVLLDIIRDLKahgIACIYISHKLNEVKAISDTICVIrDGRHI 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
5.16e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 96.71 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRrfr 81
Cdd:PRK10790 341 IDIDNVSFAYR---DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSkTVADNIAMplrlaggfSRAEVDARVSELLARVGLSDHARKYPA-----------QLSGGQKQRV 150
Cdd:PRK10790 415 QGVAMVQQDPVVLAD-TFLANVTL--------GRDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEInRElKLTIVLITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-RE-HTTLVVIAHRLSTIVEA-DTILVLHRGQAVEQG 556
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
1.64e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagrEIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTalDAEGLRRF 80
Cdd:PRK11614 5 MLSFDKVSAHYG----KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMplrlaGGF--SRAEVD---ARVSELLARVGLSDHARKypAQLSGGQKQRVGIARA 155
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAM-----GGFfaERDQFQeriKWVYELFPRLHERRIQRA--GTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIV 221
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-234 |
2.88e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.72 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 9 KTYRvaGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglRRFRQRVGMIF 88
Cdd:PRK10895 11 KAYK--GRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH--ARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 89 QHFNLLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSdHARKYPAQ-LSGGQKQRVGIARALACRPSILLCDE 167
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQsLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 168 ATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHPQ 234
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-221 |
3.04e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.93 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaldaegLRRFRQRV--GMIF-----QHFNLLSSKT 98
Cdd:COG1129 273 FSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDAIraGIAYvpedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMP----LRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQ-LSGGQKQRVGIARALACRPSILLCDEATSALD 173
Cdd:COG1129 347 IRENITLAsldrLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489187600 174 PQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIV 221
Cdd:COG1129 427 VGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-222 |
4.84e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 94.27 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYRvagreiPALQPT----RLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEG 76
Cdd:PLN03232 1234 SIKFEDVHLRYR------PGLPPVlhglSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 LRrfrqRVGMIFQHFNLLSSKTVADNIamplrlaGGFSRAEvDARVSELLARVGLSDHARKYPAQL-----------SGG 145
Cdd:PLN03232 1308 LR----RVLSIIPQSPVLFSGTVRFNI-------DPFSEHN-DADLWEALERAHIKDVIDRNPFGLdaevseggenfSVG 1375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 146 QKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEinrELK-LTIVLITHEMDVIRRvCDQVAVMDGGAIVE 222
Cdd:PLN03232 1376 QRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE---EFKsCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-226 |
9.17e-21 |
|
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: 88.35 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 10 TYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLE--EPSGGRILVEGEDVTALDAEglRRFRQRVGMI 87
Cdd:cd03217 7 HVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE--ERARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 88 FQHfnllssktvadniamPLRLAGgfsraevdARVSELLARVGLSdharkypaqLSGGQKQRVGIARALACRPSILLCDE 167
Cdd:cd03217 83 FQY---------------PPEIPG--------VKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 168 ATSALDpqttASVLQLLAE-IN--RELKLTIVLITHEMDVIRRV-CDQVAVMDGGAIVEQGDV 226
Cdd:cd03217 131 PDSGLD----IDALRLVAEvINklREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-224 |
1.01e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.80 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLR-LINRLEEPS--GGRILVEGEDVTAldaeglRRFRQRVGMIFQHFNLLSSKTVADNI- 103
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVkgSGSVLLNGMPIDA------KEMRAISAYVQQDDLFIPTLTVREHLm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 104 --AMpLRLAGGFSRAEVDARVSELLARVGLSDHARK---YPAQ---LSGGQKQRVGIARALACRPSILLCDEATSALDPQ 175
Cdd:TIGR00955 122 fqAH-LRMPRRVTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489187600 176 TTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLG 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-228 |
1.18e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.42 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvAGreIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGlrrf 80
Cdd:PRK15439 11 LLCARSISKQY--SG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVG--MIFQHFNLLSSKTVADNIAmpLRLAGgfsRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALAC 158
Cdd:PRK15439 83 AHQLGiyLVPQEPLLFPNLSVKENIL--FGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
262-334 |
1.93e-20 |
|
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: 83.71 E-value: 1.93e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 262 GLILRLTFRGEATYAPLLGTVARQTGVDYSILSGRIDRIKDTPYGQLTLALVG--GDLEAAMSQLNAADVHVEVL 334
Cdd:smart00930 2 GRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGdeEDIEAALAYLREQGVEVEVL 76
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-218 |
3.17e-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: 91.04 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 18 IPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEePSG---GRILVEGEDvtaLDAEGLRRF-RQRVGMIFQHFNL 93
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSP---LKASNIRDTeRAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 94 LSSKTVADNIAM--PLRLAGG-FSRAEVDARVSELLARVGLSDHARKYP-AQLSGGQKQRVGIARALACRPSILLCDEAT 169
Cdd:TIGR02633 90 VPELSVAENIFLgnEITLPGGrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489187600 170 SALdpqtTASVLQLLAEINRELK---LTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:TIGR02633 170 SSL----TEKETEILLDIIRDLKahgVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-228 |
9.42e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.85 E-value: 9.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLInrleepSG--------GRILVEGEdvtaldaegLRRFR-----QRVGM 86
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVL------SGvyphgsyeGEILFDGE---------VCRFKdirdsEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 87 --IFQHFNLLSSKTVADNIAmpL---RLAGGF-SRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:NF040905 81 viIHQELALIPYLSIAENIF--LgneRAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVAD 228
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
3.22e-19 |
|
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: 82.50 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRIlvegedvtaldaeglrrfr 81
Cdd:cd03221 1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 qrvgmifqhfnllsskTVADNIamplrlaggfsraevdarvsellaRVGlsdharkYPAQLSGGQKQRVGIARALACRPS 161
Cdd:cd03221 58 ----------------TWGSTV------------------------KIG-------YFEQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 162 ILLCDEATSALDPQTtasvLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:cd03221 91 LLLLDEPTNHLDLES----IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-200 |
4.55e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.94 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILV-EGEDVTALDaeglrrfrQRVGMIfqhfnllsSKTV 99
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP--------QRPYLP--------LGTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 ADNIAMPlRLAGGFSraevDARVSELLARVGLSDHARKY------PAQLSGGQKQRVGIARALACRPSILLCDEATSALD 173
Cdd:COG4178 443 REALLYP-ATAEAFS----DAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180
....*....|....*....|....*..
gi 489187600 174 PQTTASVLQLLAEinRELKLTIVLITH 200
Cdd:COG4178 518 EENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-222 |
6.45e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.33 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYrvaGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaldAEGLRRFR 81
Cdd:PRK10522 323 LELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSsktvadniamplRLAGGFSRAEVDARVSELLARVGLSD-----HARKYPAQLSGGQKQRVGIARAL 156
Cdd:PRK10522 397 KLFSAVFTDFHLFD------------QLLGPEGKPANPALVEKWLERLKMAHkleleDGRISNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEmDVIRRVCDQVAVMDGGAIVE 222
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQLSE 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-186 |
7.40e-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: 83.18 E-value: 7.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALdaeglRRFRQRVGMIFQHFNLLSS 96
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-----RDEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 K-TVADNIAMPLRLAGGFSRAevdarVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQ 175
Cdd:TIGR01189 87 ElSALENLHFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170
....*....|.
gi 489187600 176 TTASVLQLLAE 186
Cdd:TIGR01189 162 GVALLAGLLRA 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
28-186 |
1.86e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.23 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFrqrVGmifqHFNLL-SSKTVADNIAMP 106
Cdd:PRK13539 25 LAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY---LG----HRNAMkPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 107 LRLAGGFsraevDARVSELLARVGLSDHA-RKYpAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLA 185
Cdd:PRK13539 98 AAFLGGE-----ELDIAAALEAVGLAPLAhLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171
|
.
gi 489187600 186 E 186
Cdd:PRK13539 172 A 172
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-237 |
2.57e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 86.24 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAgREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEgeDVTALDAEGLRRFR 81
Cdd:PTZ00265 383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHfNLLSSKTVADNIAMPL--------------------------------RLAGGFS--------------R 115
Cdd:PTZ00265 460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscraKCAGDLNdmsnttdsneliemR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 116 AEV----DARVSELLARVGLSDHARKYP-----------AQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASV 180
Cdd:PTZ00265 539 KNYqtikDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 181 LQLLAEIN-RELKLTIVlITHEMDVIrRVCDQVAVMDGGaivEQGDVADVFLHPQHPT 237
Cdd:PTZ00265 619 QKTINNLKgNENRITII-IAHRLSTI-RYANTIFVLSNR---ERGSTVDVDIIGEDPT 671
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-229 |
2.77e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLInrleepSGGRILVEGEdVTALDAE-GLRRFRQRVG-----MIfQHF--NLLSSK 97
Cdd:NF033858 22 LDIPAGCMVGLIGPDGVGKSSLLSLI------AGARKIQQGR-VEVLGGDmADARHRRAVCpriayMP-QGLgkNLYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNIAMPLRLAGgFSRAEVDARVSELLARVGLSDHARKyPA-QLSGGQKQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:NF033858 94 SVFENLDFFGRLFG-QDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489187600 177 TASVLQLLAEINREL-KLTIVLITHEMDVIRRvCDQVAVMDGGAIVEQGDVADV 229
Cdd:NF033858 172 RRQFWELIDRIRAERpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAEL 224
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
264-333 |
5.79e-18 |
|
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: 77.11 E-value: 5.79e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 264 ILRLTFRGEATYAPLLGTVARQTGVDYSILSGRIDRIKDTPYGQLTLALVG--GDLEAAMSQLNAADVHVEV 333
Cdd:pfam09383 2 LVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGdpEQIEAALAYLREQGVEVEV 73
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
12-249 |
8.02e-18 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 81.80 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 12 RVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLR-LINRLEEPSG-------GRILVEGEDVTALDAEGLRRFRQR 83
Cdd:PRK13547 8 HVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 84 VGMIFQHFNLLSSKTVADNIAMP-LRLAGGFSRAEVDArVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALA----- 157
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLGRYPhARRAGALTHRDGEI-AWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 158 ----CRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVfLHP 233
Cdd:PRK13547 167 hdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV-LTP 245
|
250
....*....|....*.
gi 489187600 234 QHpTTRRFVFEAERVD 249
Cdd:PRK13547 246 AH-IARCYGFAVRLVD 260
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-234 |
8.36e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 84.45 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvagREIP-ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALdaeGLRRF 80
Cdd:PTZ00243 1309 LVFEGVQMRYR---EGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLREL 1382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHfNLLSSKTVADNI-----AMP------LRLAGGFSR--AE---VDARVSEllarvGLSDHarkypaqlSG 144
Cdd:PTZ00243 1383 RRQFSMIPQD-PVLFDGTVRQNVdpfleASSaevwaaLELVGLRERvaSEsegIDSRVLE-----GGSNY--------SV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 145 GQKQRVGIARALACRPS-ILLCDEATS----ALDPQTTASVLQLLAeinrelKLTIVLITHEMDVIRRvCDQVAVMDGGA 219
Cdd:PTZ00243 1449 GQRQLMCMARALLKKGSgFILMDEATAnidpALDRQIQATVMSAFS------AYTVITIAHRLHTVAQ-YDKIIVMDHGA 1521
|
250
....*....|....*
gi 489187600 220 IVEQGDVADVFLHPQ 234
Cdd:PTZ00243 1522 VAEMGSPRELVMNRQ 1536
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-230 |
1.49e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQHFNLLssktV 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVL----V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 ADNIAMPLRLAGGFSR---AEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489187600 177 TASVLQLLAEINRELKlTIVLITHEMDVIRRVCDqVAVMDGGAIVEQGDVADVF 230
Cdd:PRK15056 178 EARIISLLRELRDEGK-TMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTF 229
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-223 |
1.15e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.54 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 18 IPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDA-EGLrrfRQRVGMIFQHFNLLSS 96
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkEAL---ENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAM---PLRlaGGFsraeVDAR-----VSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEA 168
Cdd:PRK10982 88 RSVMDNMWLgryPTK--GMF----VDQDkmyrdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 169 TSALdpqTTASVLQLLAEIN--RELKLTIVLITHEMDVIRRVCDQVAVM-DGGAIVEQ 223
Cdd:PRK10982 162 TSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILrDGQWIATQ 216
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-219 |
1.20e-16 |
|
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: 81.21 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTYrvAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTAldaeGLRRF 80
Cdd:TIGR01257 1937 ILRLNELTKVY--SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 81 RQRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRaEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRP 160
Cdd:TIGR01257 2011 HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAE-EIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGA 219
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-232 |
2.12e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 77.93 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGE-DVTALDAeGLRrfRQRVGMifqhfnllsskt 98
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISA-GLS--GQLTGI------------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 vaDNIAMPLrLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTA 178
Cdd:PRK13546 104 --ENIEFKM-LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489187600 179 SVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLH 232
Cdd:PRK13546 181 KCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
1.14e-15 |
|
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: 74.43 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTY-RVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLR-LINRLEePSGGRILVEGedvtaldaeglrr 79
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPG------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 frqRVGMIFQHFNLLSSkTVADNIAmplrlaggFSRAEVDARVSELLARVGLSDHARKYPAQ-----------LSGGQKQ 148
Cdd:cd03250 67 ---SIAYVSQEPWIQNG-TIRENIL--------FGKPFDEERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 149 RVGIARALACRPSILLCDEATSALDPQTTASVLQLLaeINRELKL--TIVLITHEMDVIRRvCDQVAVMDGG 218
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLLNnkTRILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
26-212 |
1.21e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILvegedvtaldaeglRRFRQRVGMIFQHFNLlsSKTVADNIAM 105
Cdd:PRK09544 25 LELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRIGYVPQKLYL--DTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRLAGGFSRAEVdarvSELLARVGlSDHARKYPAQ-LSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLL 184
Cdd:PRK09544 89 FLRLRPGTKKEDI----LPALKRVQ-AGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
170 180
....*....|....*....|....*...
gi 489187600 185 AEINRELKLTIVLITHEMDVIRRVCDQV 212
Cdd:PRK09544 164 DQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-221 |
5.20e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 75.76 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV--------------TALD--AEGLrrfrQ 82
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIvarlqqdpprnvegTVYDfvAEGI----E 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 83 RVGMIFQHFNLLSSKTVAD----NIAMPLRL------AGGFsraEVDARVSELLARVGLSDHARKypAQLSGGQKQRVGI 152
Cdd:PRK11147 93 EQAEYLKRYHDISHLVETDpsekNLNELAKLqeqldhHNLW---QLENRINEVLAQLGLDPDAAL--SSLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 153 ARALACRPSILLCDEATSALDPQTtasvLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIV 221
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-232 |
6.52e-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: 73.40 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaegLRRFRQRVGMIFQ--------- 89
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQdpilfsgsi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 90 HFNLLSSKTVADNiamplRLAGGFSRAEVDARVSELLArvGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEAT 169
Cdd:cd03288 112 RFNLDPECKCTDD-----RLWEALEIAQLKNMVKSLPG--GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 170 SALDpQTTASVLQ---LLAEINRelklTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVADVFLH 232
Cdd:cd03288 185 ASID-MATENILQkvvMTAFADR----TVVTIAHRVSTILDA-DLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-220 |
7.74e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAeglrRFRQRVGMIF-----QHFNLLSSKTVA 100
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST----AQRLARGLVYlpedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 DNI-AMPLRLAGGFSRAEVDARVSELLAR-VGLS-DHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTT 177
Cdd:PRK15439 360 WNVcALTHNRRGFWIKPARENAVLERYRRaLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSAR 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489187600 178 ASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:PRK15439 440 NDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-229 |
1.43e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLeEPSGGRILVEGEDVTALDAEGLRRFRqrvGMIFQHFNLLssktva 100
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPP------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 dnIAMP------LRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARA-LACRPSI------LLCDE 167
Cdd:PRK03695 82 --FAMPvfqyltLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 168 ATSALDPQTTASVLQLLAEINReLKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-229 |
1.44e-14 |
|
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: 74.98 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRvAGREIpALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALdaeGLRRFR 81
Cdd:TIGR00957 1285 VEFRNYCLRYR-EDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLR 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 82 QRVGMIFQHFNLLSSktvadNIAMPLRLAGGFSRAEV---------DARVSELLArvGLSDHARKYPAQLSGGQKQRVGI 152
Cdd:TIGR00957 1360 FKITIIPQDPVLFSG-----SLRMNLDPFSQYSDEEVwwalelahlKTFVSALPD--KLDHECAEGGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 153 ARALACRPSILLCDEATSALDPQTTaSVLQllAEINRELK-LTIVLITHEMDVIRRVCdQVAVMDGGAIVEQGDVADV 229
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETD-NLIQ--STIRTQFEdCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-185 |
3.28e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.21 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGedvTALDAEglRRFRQRVGMIFQHFNLLSSK-TVADNIA 104
Cdd:cd03231 21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQ--RDSIARGLLYLGHAPGIKTTlSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 105 MplrlaggFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLL 184
Cdd:cd03231 96 F-------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
.
gi 489187600 185 A 185
Cdd:cd03231 169 A 169
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-200 |
4.35e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 69.10 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRI-LVEGEDVTaldaeglrrfrqrvgMIFQH--FNLLSsk 97
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLL---------------FLPQRpyLPLGT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 tvadniampLRlaggfsraevdarvsELLArvglsdharkYP--AQLSGGQKQRVGIARALACRPSILLCDEATSALDPQ 175
Cdd:cd03223 80 ---------LR---------------EQLI----------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....*
gi 489187600 176 TTASVLQLLaeinRELKLTIVLITH 200
Cdd:cd03223 126 SEDRLYQLL----KELGITVISVGH 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-186 |
6.41e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 26 LNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEglrrFRQrvgmifqhfNLL---------SS 96
Cdd:PRK13538 22 FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQ---------DLLylghqpgikTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAMPLRLAGGFSraevDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:PRK13538 89 LTALENLRFYQRLHGPGD----DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170
....*....|
gi 489187600 177 TASVLQLLAE 186
Cdd:PRK13538 165 VARLEALLAQ 174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
113-229 |
1.01e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.92 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 113 FSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRElK 192
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-G 194
|
90 100 110
....*....|....*....|....*....|....*..
gi 489187600 193 LTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-253 |
1.77e-13 |
|
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: 71.48 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 11 YRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEpSGGRILVEGedvTALDAEGLRRFRQRVGMIFQH 90
Cdd:TIGR01271 1227 YTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG---VSWNSVTLQTWRKAFGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 91 FNLLSSktvadNIAMPLRLAGGFSRAEVdARVSEllaRVGLSDHARKYPAQ-----------LSGGQKQRVGIARALACR 159
Cdd:TIGR01271 1301 VFIFSG-----TFRKNLDPYEQWSDEEI-WKVAE---EVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 160 PSILLCDEATSALDPQTtasvLQLlaeINRELK-----LTIVLITHEMDVIRRvCDQVAVMDGGAiVEQGDV-------A 227
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVT----LQI---IRKTLKqsfsnCTVILSEHRVEALLE-CQQFLVIEGSS-VKQYDSiqkllneT 1442
|
250 260
....*....|....*....|....*.
gi 489187600 228 DVFLHPQHPTTRRFVFEAERVDEDER 253
Cdd:TIGR01271 1443 SLFKQAMSAADRLKLFPLHRRNSSKR 1468
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
138-242 |
2.10e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 138 YPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRvCDQVAVMDG 217
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
|
90 100
....*....|....*....|....*....
gi 489187600 218 ----GAIVEQGDVADVFLHPQHPTTRRFV 242
Cdd:PTZ00265 1434 pdrtGSFVQAHGTHEELLSVQDGVYKKYV 1462
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-226 |
2.17e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.90 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 1 MIEFHDVHKTyrVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLInrLEEPS----GGRILVEGEDVTALDAEG 76
Cdd:CHL00131 7 ILEIKNLHAS--VNENEI--LKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AGHPAykilEGDILFKGESILDLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 lrrfRQRVGmIFQHFNLLSSKTVADNIAMpLRLAGGFSR-----AEVDA-----RVSELLARVGLSDH--ARKYPAQLSG 144
Cdd:CHL00131 81 ----RAHLG-IFLAFQYPIEIPGVSNADF-LRLAYNSKRkfqglPELDPlefleIINEKLKLVGMDPSflSRNVNEGFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 145 GQKQRVGIARALACRPSILLCDEATSALDP---QTTASVLQLLAEINRelklTIVLITHE---MDVIrrVCDQVAVMDGG 218
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITHYqrlLDYI--KPDYVHVMQNG 228
|
....*...
gi 489187600 219 AIVEQGDV 226
Cdd:CHL00131 229 KIIKTGDA 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
28-241 |
2.79e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.91 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLRLINrlEEPSGGRILVEGedVTALD----AEGLRRFRQRVGMIFQ---HFNLLsskTVA 100
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVEG--VITYDgitpEEIKKHYRGDVVYNAEtdvHFPHL---TVG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 DNIAMPLRLAG------GFSRAEVDARVSELLARV-GLSdHARK------YPAQLSGGQKQRVGIARALACRPSILLCDE 167
Cdd:TIGR00956 157 ETLDFAARCKTpqnrpdGVSREEYAKHIADVYMATyGLS-HTRNtkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 168 ATSALDPQTTASVLQLLAEINRELKLT-IVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV--------FLHPQHPTT 238
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAkqyfekmgFKCPDRQTT 315
|
...
gi 489187600 239 RRF 241
Cdd:TIGR00956 316 ADF 318
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-213 |
3.37e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.35 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 5 HDVHKTYRvAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSggrilvEGEdvtALDAEGLRrfrqrV 84
Cdd:TIGR03719 8 NRVSKVVP-PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDF------NGE---ARPQPGIK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 85 GMIFQHFNLLSSKTVADNIAMPLR-LAGGFSR--------AEVDARVSELLARVG-LSD------------------HAR 136
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVAeIKDALDRfneisakyAEPDADFDKLAAEQAeLQEiidaadawdldsqleiamDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 137 KYP------AQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLaeinRELKLTIVLITHEmdviRRVCD 210
Cdd:TIGR03719 151 RCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD----RYFLD 222
|
...
gi 489187600 211 QVA 213
Cdd:TIGR03719 223 NVA 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-224 |
5.16e-13 |
|
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: 66.90 E-value: 5.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 16 REIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLI-NRLEEPSG--GRILVEGEDVtaldAEGLRRFRQRVGMIFQ--- 89
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNGIPY----KEFAEKYPGEIIYVSEedv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 90 HFNLLsskTVADNIAMPLRLAGG-FSRAevdarvsellarvglsdharkypaqLSGGQKQRVGIARALACRPSILLCDEA 168
Cdd:cd03233 94 HFPTL---TVRETLDFALRCKGNeFVRG-------------------------ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 169 TSALDPQTTASVLQLLAEINRELKLT-IVLITHEMDVIRRVCDQVAVMDGGAIVEQG 224
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-222 |
3.28e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 13 VAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVT---ALDA----EGLRRFRQRVG 85
Cdd:PRK09700 271 VTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsPLDAvkkgMAYITESRRDN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 86 MIFQHFnllsskTVADNIAMP--LRLAG-GFSRAEVDARVSELLARVGLSDHARKYPA------QLSGGQKQRVGIARAL 156
Cdd:PRK09700 351 GFFPNF------SIAQNMAISrsLKDGGyKGAMGLFHEVDEQRTAENQRELLALKCHSvnqnitELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 157 ACRPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVE 222
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-227 |
3.87e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 12 RVAGREIPAL-QPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaldaegLRRFRQ--RVGMIF 88
Cdd:PRK11288 259 RLDGLKGPGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDaiRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 89 -----QHFNLLSSKTVADNIAMPLRlaGGFSRAE--VDARVSELLARVGLSDHARKYPA------QLSGGQKQRVGIARA 155
Cdd:PRK11288 333 cpedrKAEGIIPVHSVADNINISAR--RHHLRAGclINNRWEAENADRFIRSLNIKTPSreqlimNLSGGNQQKAILGRW 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 156 LACRPSILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVeqGDVA 227
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELA 479
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-217 |
5.60e-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: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 27 NIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVgmifqhFNLLSSKT-------- 98
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTV------RDLLSSITkdfythpy 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMPLRLAGgfsraEVDARVSEllarvglsdharkypaqLSGGQKQRVGIARALACRPSILLCDEATSALDPQT-- 176
Cdd:cd03237 95 FKTEIAKPLQIEQ-----ILDREVPE-----------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrl 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489187600 177 -TASVLQLLAEINrelKLTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:cd03237 153 mASKVIRRFAENN---EKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-220 |
1.35e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEG--------------EDVTALDAeglrrfrqrvgMIFQHFNLLSS 96
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPnerlgklrqdqfafEEFTVLDT-----------VIMGHTELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNI-AMP-------LRLA---GGFsrAEVD-----ARVSELLARVGLSDHARKYP-AQLSGGQKQRVGIARALACR 159
Cdd:PRK15064 96 KQERDRIyALPemseedgMKVAdleVKF--AEMDgytaeARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 160 PSILLCDEATSALDPQTtasvLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:PRK15064 174 PDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
31-201 |
2.50e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLR-LINRLEEPS-GGRILVEGEDVTaldaeglRRFRQRVGMIFQHFNLLSSKTVADNIAMP-- 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNRKPT-------KQILKRTGFVTQDDILYPHLTVRETLVFCsl 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 107 LRLAGGFSRAE----VDARVSEL-LARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVL 181
Cdd:PLN03211 167 LRLPKSLTKQEkilvAESVISELgLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180
....*....|....*....|
gi 489187600 182 QLLAEINRELKlTIVLITHE 201
Cdd:PLN03211 247 LTLGSLAQKGK-TIVTSMHQ 265
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-255 |
2.52e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.53 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDAEGLRRfrQRVGMifqhfnllssktv 99
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNG--QLTGI------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 aDNIAMPlRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTAS 179
Cdd:PRK13545 104 -ENIELK-GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 180 VLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADVFLHpqhptTRRFVFEAERVDEDERHD 255
Cdd:PRK13545 182 CLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFLKKYNQMSVEERKD 251
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-217 |
2.97e-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: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 15 GREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLL-RLINRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVGMIFQHFNL 93
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 94 LSSkTVADNIAMPLRLAGGFSRAEVDArvSELLARVGLSDHARKYPA-----QLSGGQKQRVGIARALACRPSILLCDEA 168
Cdd:cd03290 91 LNA-TVEENITFGSPFNKQRYKAVTDA--CSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489187600 169 TSALDPQTTASVLQL-LAEINRELKLTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:cd03290 168 FSALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-229 |
3.23e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 3.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLInrleepSGGRILVEGE------DVTALDAEGLRrfrQRVGMIFQHFN-- 92
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARAL------AGELPLLSGErqsqfsHITRLSFEQLQ---KLVSDEWQRNNtd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 93 LLS------SKTVADNIAMplrlaggfsraEVD--ARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILL 164
Cdd:PRK10938 90 MLSpgeddtGRTTAEIIQD-----------EVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 165 CDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAIVEQGDVADV 229
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-222 |
3.62e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDV---TALDAeglrrfrqrvgmIFQHFNLLS 95
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhNANEA------------INHGFALVT 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 96 SKTvadniamplRLAGGFSRAEVD-----ARVSELLARVGLSDHAR--------------KYPAQ------LSGGQKQRV 150
Cdd:PRK10982 330 EER---------RSTGIYAYLDIGfnsliSNIRNYKNKVGLLDNSRmksdtqwvidsmrvKTPGHrtqigsLSGGNQQKV 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 151 GIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKlTIVLITHEMDVIRRVCDQVAVMDGG---AIVE 222
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGlvaGIVD 474
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-220 |
6.52e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALD-AEGLR-------RFRQRVGMIFQhfnlLSsktVADN 102
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLAngivyisEDRKRDGLVLG----MS---VKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 103 iaMPLRLAGGFSRAEVDARVSEllARVGLSDHAR----KYPAQ------LSGGQKQRVGIARALACRPSILLCDEATSAL 172
Cdd:PRK10762 351 --MSLTALRYFSRAGGSLKHAD--EQQAVSDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489187600 173 DPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-212 |
8.50e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 8.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGE-------------DVTALD--AEGLRRFRQrvgmIFQHFN 92
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalPQPALEyvIDGDREYRQ----LEAQLH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 93 LLSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLSDHARKYPAQ-LSGGQKQRVGIARALACRPSILLCDEATSA 171
Cdd:PRK10636 100 DANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNH 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489187600 172 LDpqttasvLQLLAEINRELKL---TIVLITHEMDVIRRVCDQV 212
Cdd:PRK10636 180 LD-------LDAVIWLEKWLKSyqgTLILISHDRDFLDPIVDKI 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-222 |
1.51e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 27 NIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVeGEDVtaldaeglrrfrqRVGMIFQ-HFNLLSSKTVADNIAM 105
Cdd:TIGR03719 344 KLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KLAYVDQsRDALDPNKTVWEEISG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 106 PLRL--AGGFsraEVDARvsellARVGL-----SDHaRKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTta 178
Cdd:TIGR03719 410 GLDIikLGKR---EIPSR-----AYVGRfnfkgSDQ-QKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET-- 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489187600 179 svLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGGAIVE 222
Cdd:TIGR03719 479 --LRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVE 520
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-201 |
4.17e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTaldaEGLRRFRQRVGMIFQHFNLLSSKT 98
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMPLRLAGGfsraevDARVSELLARVGLsDHARKYP-AQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTT 177
Cdd:PRK13540 91 LRENCLYDIHFSPG------AVGITELCRLFSL-EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|....
gi 489187600 178 ASVLQLLAEiNRELKLTIVLITHE 201
Cdd:PRK13540 164 LTIITKIQE-HRAKGGAVLLTSHQ 186
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-175 |
5.28e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaeglrrfRQRVGMIFQHFNLLSS 96
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVA-DNIAMPLRLAGGFSRAevdaRVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQ 175
Cdd:PRK13543 96 DLSTlENLHFLCGLHGRRAKQ----MPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-220 |
5.59e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 59.10 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTYRVAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTL----LRLINrleepSGGRILVEGedvTALDAEGL 77
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDG---VSWNSVPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 78 RRFRQRVGMIFQHFNLLSSktvadNIAMPLRLAGGFSRAEVdARVSEllaRVGLSDHARKYPAQL-----------SGGQ 146
Cdd:cd03289 73 QKWRKAFGVIPQKVFIFSG-----TFRKNLDPYGKWSDEEI-WKVAE---EVGLKSVIEQFPGQLdfvlvdggcvlSHGH 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 147 KQRVGIARALACRPSILLCDEATSALDPQTTASvlqllaeINRELK-----LTIVLITHEMDVIRRvCDQVAVMDGGAI 220
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDPITYQV-------IRKTLKqafadCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-213 |
5.88e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 35 GLIGHSGAGKSTLLRLINRLEEPSggrilvEGEdvtALDAEGLRrfrqrVGMIFQHFNLLSSKTVADNIAMPLR-LAGGF 113
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEF------EGE---ARPAPGIK-----VGYLPQEPQLDPEKTVRENVEEGVAeVKAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 114 SR--------AEVDARVSELLARVG----LSDHA----------------RKYP-----AQLSGGQKQRVGIARALACRP 160
Cdd:PRK11819 103 DRfneiyaayAEPDADFDALAAEQGelqeIIDAAdawdldsqleiamdalRCPPwdakvTKLSGGERRRVALCRLLLEKP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLaeinRELKLTIVLITHEmdviRRVCDQVA 213
Cdd:PRK11819 183 DMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD----RYFLDNVA 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-184 |
6.15e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLrliNRLEEP------SGGRILVEGEdvtALDAEglrrFRQRVGMIFQHFNLLSSKTVADNI- 103
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLL---NVLAERvttgviTGGDRLVNGR---PLDSS----FQRSIGYVQQQDLHLPTSTVRESLr 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 104 -AMPLRLAGGFSRAEVDARVSELLARVGLSDHARKY---PAQ-LSGGQKQRVGIARALACRPSILL-CDEATSALDPQTT 177
Cdd:TIGR00956 859 fSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
....*..
gi 489187600 178 ASVLQLL 184
Cdd:TIGR00956 939 WSICKLM 945
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-173 |
6.76e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 6.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 13 VAGREIpaLQPTRLNIQAGQIFGLIGHSGAGKSTLLR-----LINRLeePSGGRIL-----VEGEDVTAL------DAEG 76
Cdd:PLN03073 187 VGGRDL--IVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI--PKNCQILhveqeVVGDDTTALqcvlntDIER 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 77 LRRFRQRVGMIFQHFNL----------LSSKTVADNIAMPLRLAGGFSRAEV------DARVSELLArvGLS---DHARK 137
Cdd:PLN03073 263 TQLLEEEAQLVAQQRELefetetgkgkGANKDGVDKDAVSQRLEEIYKRLELidaytaEARAASILA--GLSftpEMQVK 340
|
170 180 190
....*....|....*....|....*....|....*.
gi 489187600 138 YPAQLSGGQKQRVGIARALACRPSILLCDEATSALD 173
Cdd:PLN03073 341 ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-207 |
7.69e-10 |
|
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: 56.61 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLRLI-NRLEEPSGGRILVEGEDVTALDAEGLRRFRQRVGmifqhfnllssktvadniamplrl 109
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 110 aggfsraevdarvsellarvglsdharkyPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQL-----L 184
Cdd:smart00382 58 -----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180
....*....|....*....|...
gi 489187600 185 AEINRELKLTIVLITHEMDVIRR 207
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP 131
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-217 |
1.05e-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: 59.41 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 29 QAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEG--EDVtaldaegLRRFRqrvGM-IFQHFNLLSSKTV------ 99
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswDEV-------LKRFR---GTeLQDYFKKLANGEIkvahkp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 --ADNIAMplrlaggfsraEVDARVSELLARV---GLSDHAR----------KYPAQLSGGQKQRVGIARALACRPSILL 164
Cdd:COG1245 167 qyVDLIPK-----------VFKGTVRELLEKVderGKLDELAeklglenildRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 165 CDEATSALDPQ---TTASVLQLLAEINRelklTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:COG1245 236 FDEPSSYLDIYqrlNVARLIRELAEEGK----YVLVVEHDLAILDYLADYVHILYG 287
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-230 |
1.09e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLInrLEEpsggriLVEGEDvTALDAEGLRRFRQRVGMIFqhfnllsSKT 98
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGE------LSHAET-SSVVIRGSVAYVPQVSWIF-------NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMPLRLAGGFSRAEVDARVSE----LLARVGLSDHARKyPAQLSGGQKQRVGIARALACRPSILLCDEATSALDP 174
Cdd:PLN03232 695 VRENILFGSDFESERYWRAIDVTALQhdldLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 175 QTTASVLQllAEINRELK-LTIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVADVF 230
Cdd:PLN03232 774 HVAHQVFD--SCMKDELKgKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
28-184 |
1.60e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.48 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLRLINRLEEPS--GGRILVEGEDVTAldaeglrRFRQRVGMIFQhfnllssktvadniam 105
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK-------NFQRSTGYVEQ---------------- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489187600 106 plrlaggfsraeVDARVSELLARVGLSDHArkYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLL 184
Cdd:cd03232 87 ------------QDVHSPNLTVREALRFSA--LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-225 |
5.47e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 9 KTYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTL-LRLINRLE-EPSGGRILVEGEDVTALDAEglRRFRQRVGM 86
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDyEVTGGTVEFKGKDLLELSPE--DRAGEGIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 87 IFQHfnllssktvadniamPLRLAGG----FSRAEVDA----RVSELLARVGLSD------HARKYPAQL---------S 143
Cdd:PRK09580 83 AFQY---------------PVEIPGVsnqfFLQTALNAvrsyRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 144 GGQKQRVGIARALACRPSILLCDEATSALDpqttASVLQLLAE-IN--RELKLTIVLITHE---MDVIRRvcDQVAVMDG 217
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLD----IDALKIVADgVNslRDGKRSFIIVTHYqriLDYIKP--DYVHVLYQ 221
|
....*...
gi 489187600 218 GAIVEQGD 225
Cdd:PRK09580 222 GRIVKSGD 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
10-224 |
5.83e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 10 TYRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLrlinrleepsgGRILVEGEDVtaldaEGLRRFRQRVGMIFQ 89
Cdd:TIGR00957 643 TFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLL-----------SALLAEMDKV-----EGHVHMKGSVAYVPQ 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 90 HfNLLSSKTVADNIAMPLRLAGGFSRAEVDArvSELLARV-----GLSDHARKYPAQLSGGQKQRVGIARALACRPSILL 164
Cdd:TIGR00957 707 Q-AWIQNDSLRENILFGKALNEKYYQQVLEA--CALLPDLeilpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYL 783
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 165 CDEATSALDPQTTASVLQLLAEINRELK-LTIVLITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:TIGR00957 784 FDDPLSAVDAHVGKHIFEHVIGPEGVLKnKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-176 |
5.90e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFHDVHKTY--RVAgreIPALQptrLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVeGEDVtaldaeglrr 79
Cdd:PRK11819 325 IEAENLSKSFgdRLL---IDDLS---FSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV---------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 80 frqRVGMIFQ-HFNLLSSKTV-------ADNIAMplrlaGGF---SRAEVdarvsellARVGL--SDHaRKYPAQLSGGQ 146
Cdd:PRK11819 388 ---KLAYVDQsRDALDPNKTVweeisggLDIIKV-----GNReipSRAYV--------GRFNFkgGDQ-QKKVGVLSGGE 450
|
170 180 190
....*....|....*....|....*....|
gi 489187600 147 KQRVGIARALACRPSILLCDEATSALDPQT 176
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-228 |
6.56e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEgedvtaldaeglrrfrQRVGMIFQHFNLLSSkTVA 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----------------RSIAYVPQQAWIMNA-TVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 DNIAM-----PLRLAggfsraevDA-RVSELLARV-----GLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEAT 169
Cdd:PTZ00243 739 GNILFfdeedAARLA--------DAvRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 170 SALDpqttASVLQLLAEinrELKL------TIVLITHEMDVIRRVcDQVAVMDGGAIVEQGDVAD 228
Cdd:PTZ00243 811 SALD----AHVGERVVE---ECFLgalagkTRVLATHQVHVVPRA-DYVVALGDGRVEFSGSSAD 867
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-228 |
8.39e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 21 LQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVegedvtaldAEGLRrfrqrVGMIFQH-FNLLSsktv 99
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIK-----LGYFAQHqLEFLR---- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 ADNiaMPLRLAGGFSRAEVDARVSELLARVGLS-DHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDpqttA 178
Cdd:PRK10636 390 ADE--SPLQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----L 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489187600 179 SVLQLLAEINRELKLTIVLITHEMDVIRRVCDQV-AVMDGGAIVEQGDVAD 228
Cdd:PRK10636 464 DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLyLVHDGKVEPFDGDLED 514
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-219 |
2.94e-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: 54.09 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGedvtaldaeglrrfrqRVGMIFQhFNLLSSKT 98
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------------RISFSSQ-FSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMplrlagGFSRAEVdaRVSELLARVGLSDHARKYPAQ-----------LSGGQKQRVGIARALACRPSILLCDE 167
Cdd:cd03291 114 IKENIIF------GVSYDEY--RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 168 ATSALDPQTT-----ASVLQLLAEINRelkltiVLITHEMDVIRRVcDQVAVMDGGA 219
Cdd:cd03291 186 PFGYLDVFTEkeifeSCVCKLMANKTR------ILVTSKMEHLKKA-DKILILHEGS 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-224 |
4.46e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLR-LINRLEEPSGGRILVEGEDVtaldaeglrrFRQRVGMIFqhfnlls 95
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVA----------YVPQVSWIF------- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 96 SKTVADNIAMPLRLAGgfSRAEVDARVSEL---LARVGLSDHAR--KYPAQLSGGQKQRVGIARALACRPSILLCDEATS 170
Cdd:PLN03130 692 NATVRDNILFGSPFDP--ERYERAIDVTALqhdLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 171 ALDPQTTASVLQLLaeINRELK-LTIVLITHEMDVIRRVcDQVAVMDGGAIVEQG 224
Cdd:PLN03130 770 ALDAHVGRQVFDKC--IKDELRgKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
142-224 |
7.94e-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: 51.55 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 142 LSGGQKQRVGIARALACRP--SILLCDEATSALDPQTTasvLQLLAEINR--ELKLTIVLITHEMDVIRRvCDQVAVM-- 215
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDI---NQLLEVIKGliDLGNTVILIEHNLDVLSS-ADWIIDFgp 163
|
90
....*....|...
gi 489187600 216 ----DGGAIVEQG 224
Cdd:cd03238 164 gsgkSGGKVVFSG 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-201 |
9.21e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 27 NIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEgedvTALDAEGLRRFRQrvgmifqhfNLLSSKTVADNiamp 106
Cdd:PRK11147 341 QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQHRA---------ELDPEKTVMDN---- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 107 lrLAGGFSRAEVDARVSELLARvgLSD------HARKYPAQLSGGQKQRVGIARaLACRPSILLC-DEATSALDPQTtas 179
Cdd:PRK11147 404 --LAEGKQEVMVNGRPRHVLGY--LQDflfhpkRAMTPVKALSGGERNRLLLAR-LFLKPSNLLIlDEPTNDLDVET--- 475
|
170 180
....*....|....*....|..
gi 489187600 180 vLQLLAEINRELKLTIVLITHE 201
Cdd:PRK11147 476 -LELLEELLDSYQGTVLLVSHD 496
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-218 |
1.65e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 19 PALQPTRLNIQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRIlvegedvtaldaeglrRFRQRVGMIFQhFNLLSSKT 98
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISFSPQ-TSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 99 VADNIAMplrlagGFSRAEVdaRVSELLARVGLSDHARKYPAQ-----------LSGGQKQRVGIARALACRPSILLCDE 167
Cdd:TIGR01271 503 IKDNIIF------GLSYDEY--RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489187600 168 ATSALDPQTTASVLQ-----LLAEINRelkltiVLITHEMDVIRRVcDQVAVMDGG 218
Cdd:TIGR01271 575 PFTHLDVVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKKA-DKILLLHEG 623
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-217 |
2.07e-07 |
|
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: 51.21 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 31 GQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDA----------EGLRRFRQRVGMIFQHFNLLSsKTVA 100
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEfrgselqnyfTKLLEGDVKVIVKPQYVDLIP-KAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 101 DNIAMPLrlaggfSRAEVDARVSELLARVGLSDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASV 180
Cdd:cd03236 105 GKVGELL------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 489187600 181 LQLLAEINRELKLTIVlITHEMDVIRRVCDQVAVMDG 217
Cdd:cd03236 179 ARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCLYG 214
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-185 |
2.23e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 20 ALQPTRLNIQAGQIFGLI------------GHSGAGKSTLLRLINRLEEPSGGRILVEGEDVTALDaeglrrfRQRVGMI 87
Cdd:PRK13541 3 SLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 88 FQHFNLLSSKTVADNIAMplrlaggfsRAEVDARVSELLARV---GLSDHARKYPAQLSGGQKQRVGIARALACRPSILL 164
Cdd:PRK13541 76 GHNLGLKLEMTVFENLKF---------WSEIYNSAETLYAAIhyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
170 180
....*....|....*....|.
gi 489187600 165 CDEATSALDPQTTASVLQLLA 185
Cdd:PRK13541 147 LDEVETNLSKENRDLLNNLIV 167
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-200 |
4.07e-07 |
|
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: 51.67 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 17 EIPALQPT------RLNIQ--AGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVegedvtalDAEG-LRRFRQRVGMi 87
Cdd:TIGR00954 456 NIPLVTPNgdvlieSLSFEvpSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------PAKGkLFYVPQRPYM- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 88 fqhfnllSSKTVADNIAMPLRLAGGFSRAEVDARVSELLARVGLS---------DHARKYPAQLSGGQKQRVGIARALAC 158
Cdd:TIGR00954 527 -------TLGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489187600 159 RPSILLCDEATSALDPQTTASVLQLLaeinRELKLTIVLITH 200
Cdd:TIGR00954 600 KPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-200 |
2.06e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLRLINRlEEPSG--------GRILVEGEdvTALDaeglrrFRQRVGMIFQ--HFNLLSSK 97
Cdd:PRK10938 283 VNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfGRRRGSGE--TIWD------IKKHIGYVSSslHLDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 98 TVADNIamplrLAG-----GFSRAEVDAR---VSELLARVGLSDHARKYPAQ-LSGGQKQRVGIARALACRPSILLCDEA 168
Cdd:PRK10938 354 SVRNVI-----LSGffdsiGIYQAVSDRQqklAQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEP 428
|
170 180 190
....*....|....*....|....*....|....
gi 489187600 169 TSALDPqttasvlqllaeINREL--KLTIVLITH 200
Cdd:PRK10938 429 LQGLDP------------LNRQLvrRFVDVLISE 450
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
97-224 |
2.48e-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: 49.24 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAMPLRLAGGFSRAEVD-ARVSELLARVGLSDHARKYPA-QLSGGQKQRVGIARALACR---PSILLCDEATSA 171
Cdd:TIGR00630 783 KNIADVLDMTVEEAYEFFEAVPSiSRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTG 862
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 172 LDpqtTASVLQLLAEINRELKL--TIVLITHEMDVIrRVCDQVAVM------DGGAIVEQG 224
Cdd:TIGR00630 863 LH---FDDIKKLLEVLQRLVDKgnTVVVIEHNLDVI-KTADYIIDLgpeggdGGGTVVASG 919
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-218 |
5.51e-06 |
|
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: 47.90 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 11 YRVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLLR-LINRLEEPSGGRILVEGEDVTALDAegLRRFRQRVGMI-- 87
Cdd:TIGR02633 266 WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNP--AQAIRAGIAMVpe 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 88 -FQHFNLLSSKTVADNIAMP-LRLAGGFSR----AEVDArVSELLARVGLSDHARKYP-AQLSGGQKQRVGIARALACRP 160
Cdd:TIGR02633 344 dRKRHGIVPILGVGKNITLSvLKSFCFKMRidaaAELQI-IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489187600 161 SILLCDEATSALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGG 218
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-217 |
9.49e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLRLINRLEEPSGGRILVEG--EDVtaldaegLRRFRqrvGMIFQ-HFNLLSSKTV----- 99
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswDEV-------LKRFR---GTELQnYFKKLYNGEIkvvhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 100 ---ADNIAMplrlaggfsraEVDARVSELLARV---GLSDHARKYPA----------QLSGGQKQRVGIARALACRPSIL 163
Cdd:PRK13409 166 pqyVDLIPK-----------VFKGKVRELLKKVderGKLDEVVERLGlenildrdisELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489187600 164 LCDEATSALDPQ---TTASVLQLLAEinrelKLTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:PRK13409 235 FFDEPTSYLDIRqrlNVARLIRELAE-----GKYVLVVEHDLAVLDYLADNVHIAYG 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-220 |
3.23e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 28 IQAGQIFGLIGHSGAGKSTLLRLI-----NRLEepsgGRILVEGEDV---TALDAeglrrFRQRVGMI---FQHFNLLSS 96
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLfgaypGRWE----GEIFIDGKPVkirNPQQA-----IAQGIAMVpedRKRDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAMP-LRLAGGFSR----AEVDArVSELLARVGL-SDHARKYPAQLSGGQKQRVGIARALACRPSILLCDEATS 170
Cdd:PRK13549 356 MGVGKNITLAaLDRFTGGSRiddaAELKT-ILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489187600 171 ALDPQTTASVLQLLAEINRElKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
97-224 |
3.29e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 97 KTVADNIAMPLRLAGGFsrAEVDARVSE---LLARVGLSDHARKYPA-QLSGGQKQRVGIARALACR---PSILLCDEAT 169
Cdd:cd03271 123 KSIADVLDMTVEEALEF--FENIPKIARklqTLCDVGLGYIKLGQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPT 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 170 SALDpqtTASVLQLLAEINRELKL--TIVLITHEMDVIrRVCDQVAVM------DGGAIVEQG 224
Cdd:cd03271 201 TGLH---FHDVKKLLEVLQRLVDKgnTVVVIEHNLDVI-KCADWIIDLgpeggdGGGQVVASG 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-217 |
3.86e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.16 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFhDVHKTYRVAGREI----PALQPT----RLNIQAGQIF-----GLIGHSGAGKSTLLRLINRLEEPSGGRIlveGED 68
Cdd:COG1245 325 IEF-EVHAPRREKEEETlveyPDLTKSyggfSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEV---DED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 69 VtaldaeglrrfrqRVGMIFQHFNLLSSKTVADNIAMPLRLAGGFSRAEvdarvSELLARVGLSDHARKYPAQLSGGQKQ 148
Cdd:COG1245 401 L-------------KISYKPQYISPDYDGTVEEFLRSANTDDFGSSYYK-----TEIIKPLGLEKLLDKNVKDLSGGELQ 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489187600 149 RVGIARALACRPSILLCDEATSALDPQ---TTASVLQLLAEINrelKLTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:COG1245 463 RVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRFAENR---GKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-234 |
5.23e-05 |
|
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: 43.33 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 142 LSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAEINRELKLTIVLITHEMDVIRRVCDQVAVMDGgaiv 221
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG---- 147
|
90
....*....|...
gi 489187600 222 eQGDVADVFLHPQ 234
Cdd:cd03222 148 -EPGVYGIASQPK 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-220 |
5.72e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 36 LIGHSGAGKSTLLRLINRLEEPSGGRILvegedvtaldaeglRRFRQRVGMIFQH----FNLLSSktvadniamPLRLAG 111
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVF--------------RSAKVRMAVFSQHhvdgLDLSSN---------PLLYMM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 112 GFSRAEVDARVSELLARVGLSDHARKYPA-QLSGGQKQRVGIARALACRPSILLCDEATSALDPQTTASVLQLLAeinrE 190
Cdd:PLN03073 597 RCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV----L 672
|
170 180 190
....*....|....*....|....*....|
gi 489187600 191 LKLTIVLITHEMDVIRRVCDQVAVMDGGAI 220
Cdd:PLN03073 673 FQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2-217 |
1.09e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 2 IEFhDVHKTYRVAGREI----PALQPT----RLNIQAGQIF-----GLIGHSGAGKSTLLRLINRLEEPSGGRILVEged 68
Cdd:PRK13409 324 IEF-EERPPRDESERETlveyPDLTKKlgdfSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 69 vtaldaeglrrfrQRVGMIFQHFNLLSSKTVADNIA-MPLRLAGGFSRaevdarvSELLARVGLSDHARKYPAQLSGGQK 147
Cdd:PRK13409 400 -------------LKISYKPQYIKPDYDGTVEDLLRsITDDLGSSYYK-------SEIIKPLQLERLLDKNVKDLSGGEL 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489187600 148 QRVGIARALACRPSILLCDEATSALDPQ---TTASVLQLLAEinrELKLTIVLITHEMDVIRRVCDQVAVMDG 217
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRRIAE---EREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
124-229 |
1.44e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 124 ELLARVGLSdharkY-----PA-QLSGGQKQRVGIARALACRPS-----ILlcDEATSALDpqtTASVLQLLAEINR--E 190
Cdd:PRK00349 812 QTLVDVGLG-----YiklgqPAtTLSGGEAQRVKLAKELSKRSTgktlyIL--DEPTTGLH---FEDIRKLLEVLHRlvD 881
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489187600 191 LKLTIVLITHEMDVIrRVCDQvaVMD--------GGAIVEQG---DVADV 229
Cdd:PRK00349 882 KGNTVVVIEHNLDVI-KTADW--IIDlgpeggdgGGEIVATGtpeEVAKV 928
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
141-207 |
3.03e-04 |
|
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: 40.81 E-value: 3.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489187600 141 QLSGGQKQRVGIARALA---CRPSILLC-DEATSALDPQTTASVLQLLAEINRELKLTIVlITHEMDVIRR 207
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAEL 146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
12-224 |
4.01e-04 |
|
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: 41.09 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 12 RVAGREIPALQPTRLNIQAGQIFGLIGHSGAGKSTLlrlinrleepsggrilvegedvtALD---AEGLRRFRQRVGMIF 88
Cdd:cd03270 2 IVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSL-----------------------AFDtiyAEGQRRYVESLSAYA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 89 QHFNLLSSKTVADNI-------AMPLRLAGGFSRAEVdARVSE-------LLARVGLS-----------DH---ARKYPA 140
Cdd:cd03270 59 RQFLGQMDKPDVDSIeglspaiAIDQKTTSRNPRSTV-GTVTEiydylrlLFARVGIRerlgflvdvglGYltlSRSAPT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 141 qLSGGQKQRVGIARALACRPS--ILLCDEATSALDPQTTASVLQLLAEInRELKLTIVLITHEMDVIRRVcDQV------ 212
Cdd:cd03270 138 -LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAA-DHVidigpg 214
|
250
....*....|..
gi 489187600 213 AVMDGGAIVEQG 224
Cdd:cd03270 215 AGVHGGEIVAQG 226
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
141-187 |
7.49e-04 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 40.32 E-value: 7.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489187600 141 QLSGGQKQRVGIARALA---CRPS-ILLCDEATSALDPQTTASVLQLLAEI 187
Cdd:cd03272 158 QLSGGQKSLVALALIFAiqkCDPApFYLFDEIDAALDAQYRTAVANMIKEL 208
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
124-229 |
1.81e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 124 ELLARVGLSdharkY-----PA-QLSGGQKQRVGIARALACRPS-----ILlcDEATSAL---DpqttasVLQLLAEINR 189
Cdd:COG0178 808 QTLQDVGLG-----YiklgqPAtTLSGGEAQRVKLASELSKRSTgktlyIL--DEPTTGLhfhD------IRKLLEVLHR 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489187600 190 --ELKLTIVLITHEMDVIRrvcdqVA--VMD--------GGAIVEQG---DVADV 229
Cdd:COG0178 875 lvDKGNTVVVIEHNLDVIK-----TAdwIIDlgpeggdgGGEIVAEGtpeEVAKV 924
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
139-208 |
2.05e-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: 38.74 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489187600 139 PAQLSGGQKQ------RVGIARALACRPSILLCDEATSALDPQTTASVL-QLLAEINRELKLTIVLITHE------MDVI 205
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEERKSQKNFQLIVITHDeelvdaADHI 192
|
...
gi 489187600 206 RRV 208
Cdd:cd03240 193 YRV 195
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
6-54 |
2.93e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.53 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489187600 6 DVHKTYRVAGREIPALQPtRLniqAGQIFGLIGHSGAGKSTllrLINRL 54
Cdd:cd01854 64 PVLAVSAKTGEGLDELRE-LL---KGKTSVLVGQSGVGKST---LLNAL 105
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
6-54 |
6.37e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 37.79 E-value: 6.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489187600 6 DVHKTYRVAGREIPALQPtRLniqAGQIFGLIGHSGAGKSTllrLINRL 54
Cdd:COG1162 145 PVLAVSAKTGEGLDELRE-LL---KGKTSVLVGQSGVGKST---LINAL 186
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
6-55 |
8.13e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.49 E-value: 8.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 489187600 6 DVHKTYRVAGREIPALQPtRLniqAGQIFGLIGHSGAGKSTllrLINRLE 55
Cdd:PRK00098 143 DVLELSAKEGEGLDELKP-LL---AGKVTVLAGQSGVGKST---LLNALA 185
|
|
| |
