|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-340 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 513.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 241 VSTVIQTEPSTSLIRRLNDEQVGDfKDYKIFVEETQVTQPIINDLIQICGREVKILFSSMSEIQGNTVCYMWLRFNIDQQ 320
Cdd:COG1135 241 LPTVLNDELPEELLARLREAAGGG-RLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDA 319
|
330 340
....*....|....*....|
gi 493203783 321 FDDTAInQYFKEKNIQFEEV 340
Cdd:COG1135 320 AIDAAL-AYLREQGVVVEVL 338
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-340 |
1.17e-158 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 447.33 E-value: 1.17e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 241 VSTVIQTEPSTSLIRRLNDEQVGDFKD-YKIFVEETQVTQPIINDLIQICGREVKILFSSMSEIQGNTVCYMWLRFNIDQ 319
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEPTTGSGPlLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|.
gi 493203783 320 QFDDTAInQYFKEKNIQFEEV 340
Cdd:PRK11153 321 GDIQAAI-AYLQEHGVKVEVL 340
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
1.41e-136 |
|
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: 387.32 E-value: 1.41e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-338 |
1.70e-115 |
|
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: 338.01 E-value: 1.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 241 VSTVIQTEPSTSLIRRLNDEQVGD-FKDYKIFVEETQVTQPIINDLIQICGREVKILFSSMSEIQGNTVCYMWLRFNIDQ 319
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPFADsVPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
|
330
....*....|....*....
gi 493203783 320 QfDDTAINQYFKEKNIQFE 338
Cdd:TIGR02314 321 Q-DTQAAIAYLQEHNVKVE 338
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-244 |
1.88e-96 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 285.73 E-value: 1.88e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImNYSDKMMRDI 80
Cdd:COG1126 1 MIEIENLHKSFGDLE----VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKK-SKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKmSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQN 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
....*
gi 493203783 240 FVSTV 244
Cdd:COG1126 235 FLSKV 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
6.27e-96 |
|
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: 293.73 E-value: 6.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFH-KKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRD 79
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQH-FNLLNSA-TVFKNVAMPL-ILSKKSKTEIKQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVAIARAL 155
Cdd:COG1123 340 LRRRVQMVFQDpYSSLNPRmTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 156 VTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
3.10e-94 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 279.62 E-value: 3.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 -KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRvIKDICNRVAVMEKGQVVE 221
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
1.50e-86 |
|
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: 260.68 E-value: 1.50e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLI-LSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-233 |
2.75e-86 |
|
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: 262.68 E-value: 2.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLE---AASNGQVIVDGHDIMNYSDKMM 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 RDIK-KDIGMIFQH-FNLLN-SATVFKNVAMPLILSKK-SKTEIKQRVTEMLEFVGLSDKK---DQFPDELSGGQKQRVA 150
Cdd:COG0444 81 RKIRgREIQMIFQDpMTSLNpVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
...
gi 493203783 231 HPK 233
Cdd:COG0444 241 NPR 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
4.38e-86 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 258.83 E-value: 4.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVE 221
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-219 |
5.23e-86 |
|
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: 258.19 E-value: 5.23e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIK 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KD-IGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKdICNRVAVMEKGQV 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
1.24e-83 |
|
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: 252.81 E-value: 1.24e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQH-FNLLN-SATVFKNVAMPLILSKK--SKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARAL 155
Cdd:cd03257 81 RKEIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 156 VTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-241 |
2.45e-80 |
|
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: 245.10 E-value: 2.45e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDI 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQH-FNLLNSA-TVFKNVAMPLILSKKskTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVT 157
Cdd:COG1124 78 RRRVQMVFQDpYASLHPRhTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIA 237
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....
gi 493203783 238 QNFV 241
Cdd:COG1124 236 RELL 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-234 |
2.65e-80 |
|
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: 244.16 E-value: 2.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIK 81
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKT 234
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
1.16e-79 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 243.43 E-value: 1.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:COG3638 2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNV------AMPL---ILSKKSKTEiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAI 151
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVlagrlgRTSTwrsLLGLFPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 152 ARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-232 |
6.26e-77 |
|
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: 235.86 E-value: 6.26e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIK 81
Cdd:cd03261 1 IELRGLTKSFGGR--TV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLI-LSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
4.82e-74 |
|
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: 237.49 E-value: 4.82e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKkkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL---EAASNGQVIVDGHDIMNYSDKMM 77
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 RdikKDIGMIFQHF-NLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV 156
Cdd:COG1123 82 G---RRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
6.24e-74 |
|
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: 227.41 E-value: 6.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImNYSDKMMRDIK 81
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKK-SKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKVKGmSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-229 |
2.10e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 227.67 E-value: 2.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysdkmmRDI 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV--------TGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHemrvikDI------CNRVAVMEKGqvveTGTVKEVF 229
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH------DVdeavflADRVVVLSAR----PGRIVEEI 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-228 |
2.67e-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: 226.68 E-value: 2.67e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIK 81
Cdd:cd03256 1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNV------AMPL---ILSKKSKTEiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgrlgRRSTwrsLFGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-234 |
1.41e-72 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.83 E-value: 1.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhdimnysdkmmRDI 80
Cdd:COG3842 5 ALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG-----------RDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 ------KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:COG3842 70 tglppeKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHemrvikD------ICNRVAVMEKGQVVETGTVKEV 228
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTH------DqeealaLADRIAVMNDGRIEQVGTPEEI 223
|
....*.
gi 493203783 229 FSHPKT 234
Cdd:COG3842 224 YERPAT 229
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-233 |
1.53e-70 |
|
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: 220.79 E-value: 1.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKkqT---IDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMR 78
Cdd:TIGR04521 1 IKLKNVSYIYQPG--TpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DIKKDIGMIFQhF--NLLNSATVFKNVAM-PLILsKKSKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARA 154
Cdd:TIGR04521 79 DLRKKVGLVFQ-FpeHQLFEETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-228 |
2.07e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 219.16 E-value: 2.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmmRDIK 81
Cdd:COG1131 1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-233 |
4.20e-70 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 221.53 E-value: 4.20e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 11 FHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKKDIGMIFQH 90
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 91 -FNLLNS-ATVFKNVAMPLILSK-KSKTEIKQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:COG4608 104 pYASLNPrMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 167 ATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
2.96e-69 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 215.46 E-value: 2.96e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKkqtiDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNysdkmMRDIK 81
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-244 |
6.22e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 220.36 E-value: 6.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSF-HKKKQTIDALK-------------------DVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNG 60
Cdd:COG4175 3 KIEVRNLYKIFgKRPERALKLLDqgkskdeilektgqtvgvnDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 61 QVIVDGHDIMNYSDKMMRDI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPD 139
Cdd:COG4175 83 EVLIDGEDITKLSKKELRELrRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 140 ELSGGQKQRVAIARALVTNPKILLCDEATSALDPAttasI--------LTLLKNVNQtfgiTIMMITHE----MRvikdI 207
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDPL----IrremqdelLELQAKLKK----TIVFITHDldeaLR----L 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 493203783 208 CNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVSTV 244
Cdd:COG4175 231 GDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-246 |
7.00e-69 |
|
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: 216.36 E-value: 7.00e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 11 FHKKKQTIdALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI-KKDIGMIFQ 89
Cdd:cd03294 31 LKKTGQTV-GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 90 HFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 170 ALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPkttiAQNFVSTVIQ 246
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP----ANDYVREFFR 262
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-231 |
8.45e-69 |
|
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: 215.24 E-value: 8.45e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKS--------KTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
1.06e-67 |
|
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: 212.10 E-value: 1.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdiK 81
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFV 241
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
6.48e-67 |
|
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: 209.25 E-value: 6.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 3 EFRQVSKSFHKKKQTidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIKK 82
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 83 DIGMIFQHFN--LLNSaTVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03225 76 KVGLVFQNPDdqFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQ 218
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-218 |
8.29e-67 |
|
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: 207.81 E-value: 8.29e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMmRDIK 81
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL-PPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLilskkskteikqrvtemlefvglsdkkdqfpdelSGGQKQRVAIARALVTNPKI 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQ 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-232 |
5.19e-66 |
|
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: 207.32 E-value: 5.19e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhdimnysdKMMRDIK 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHemrvikDI------CNRVAVMEKGQvvetGTVKEVFSHP 232
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTH------DIdeavflADRVVVLSARP----GRIVAEVEVD 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-234 |
1.12e-65 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 216.09 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKK-------QTIDALKDVSFTVNHNDIFGVIGYSGAGKSTL----VRLVnhleaASNGQVIVDGHDIM 70
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 71 NYSDKMMRDIKKDIGMIFQH-FNLLNS-ATVFKNVAMPLIL--SKKSKTEIKQRVTEMLEFVGLS-DKKDQFPDELSGGQ 145
Cdd:COG4172 351 GLSRRALRPLRRRMQVVFQDpFGSLSPrMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 146 KQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTV 225
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
....*....
gi 493203783 226 KEVFSHPKT 234
Cdd:COG4172 511 EQVFDAPQH 519
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-244 |
2.81e-65 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 206.10 E-value: 2.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKkkqtIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImNYSDKMMRDI 80
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAM-PLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQN 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
....*
gi 493203783 240 FVSTV 244
Cdd:PRK09493 235 FLQHV 239
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-234 |
3.89e-65 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 209.23 E-value: 3.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnYSDKMMRDik 81
Cdd:COG1118 3 IEVRNISKRFGSFT----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITH---E-MRVikdiCNRVAVMEKGQVVETGTVKEVFSHPKT 234
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHdqeEaLEL----ADRVVVMNQGRIEQVGTPDEVYDRPAT 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
4.09e-65 |
|
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: 214.55 E-value: 4.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKS----TLVRLVNHLEAASNGQVIVDGHDIMNYSDKM 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 77 MRDIK-KDIGMIFQ---------HfnllnsaTVFKNVAMPLILSKK-SKTEIKQRVTEMLEFVGLSDKK---DQFPDELS 142
Cdd:COG4172 86 LRRIRgNRIAMIFQepmtslnplH-------TIGKQIAEVLRLHRGlSGAAARARALELLERVGIPDPErrlDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 143 GGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVET 222
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250
....*....|.
gi 493203783 223 GTVKEVFSHPK 233
Cdd:COG4172 239 GPTAELFAAPQ 249
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
6.81e-65 |
|
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: 204.18 E-value: 6.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhkkKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIK 81
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-245 |
1.27e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 208.00 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDi 80
Cdd:COG3839 3 SLELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV---TDLPPKD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 kKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG3839 75 -RNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHE----MRvikdICNRVAVMEKGQVVETGTVKEVFSHPKTTi 236
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDqveaMT----LADRIAVMNDGRIQQVGTPEELYDRPANL- 228
|
....*....
gi 493203783 237 aqnFVSTVI 245
Cdd:COG3839 229 ---FVAGFI 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-242 |
5.48e-64 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 202.94 E-value: 5.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHkkkqTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDI---MNYSDKMMR 78
Cdd:COG4161 3 IQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DIKKDIGMIFQHFNLLNSATVFKN-VAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTvKEVFSHPKTTIA 237
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAF 236
|
....*
gi 493203783 238 QNFVS 242
Cdd:COG4161 237 AHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-242 |
3.79e-63 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 201.01 E-value: 3.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDI---MNYSDKMMRDIKKDIGMIFQHFNLLNS 96
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 97 ATVFKN-VAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPAT 175
Cdd:PRK11124 97 LTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 176 TASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTvKEVFSHPKTTIAQNFVS 242
Cdd:PRK11124 177 TAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
1.07e-61 |
|
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: 198.04 E-value: 1.07e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKkkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNysDKMMRDIK 81
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQH-FNLLNSATVFKNVA-------MPLIlskksktEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAfglenlgVPRE-------EMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 154 ALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEM-RVIKdiCNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVL--ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-228 |
2.58e-61 |
|
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: 195.48 E-value: 2.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL-----EAASNGQVIVDGHDIMNYSDKM 76
Cdd:cd03260 1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 77 MRdIKKDIGMIFQHFNLLNsATVFKNVAMPL-ILSKKSKTEIKQRVTEMLEFVGLSD--KKDQFPDELSGGQKQRVAIAR 153
Cdd:cd03260 77 LE-LRRRVGMVFQKPNPFP-GSIYDNVAYGLrLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 154 ALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfgITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
12-246 |
3.33e-61 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 196.17 E-value: 3.33e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 12 HKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDI---------MNYSD-KMMRDIK 81
Cdd:COG4598 15 HKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgeLVPADrRQLQRIR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNV-AMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG4598 95 TRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNF 240
Cdd:COG4598 175 VMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQF 253
|
....*.
gi 493203783 241 VSTVIQ 246
Cdd:COG4598 254 LSSSLK 259
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
4.03e-61 |
|
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: 196.03 E-value: 4.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFhkkkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDI 80
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI---TGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 -KKDIGMIFQHFNLLNSATVFKNVAM---------------PLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGG 144
Cdd:COG0411 77 aRLGIARTFQNPRLFPELTVLENVLVaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGT 224
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....*....
gi 493203783 225 VKEVFSHPK 233
Cdd:COG0411 237 PAEVRADPR 245
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-233 |
5.80e-61 |
|
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: 194.96 E-value: 5.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSF--HKkkqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRD 79
Cdd:cd03219 1 LEVRGLTKRFggLV------ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI---TGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 I-KKDIGMIFQHFNLLNSATVFKNVAMPLILSK----------KSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQR 148
Cdd:cd03219 72 IaRLGIGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 149 VAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
....*
gi 493203783 229 FSHPK 233
Cdd:cd03219 231 RNNPR 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-224 |
2.98e-60 |
|
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: 193.03 E-value: 2.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYS-DKMMRD 79
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQHFNLLNSATVFKNVAMPLILskKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGT 224
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-246 |
4.66e-60 |
|
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: 192.90 E-value: 4.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdik 81
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKK--DQFPDELSGGQKQRVAIARALVTNP 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPkttiAQN 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP----AND 230
|
....*..
gi 493203783 240 FVSTVIQ 246
Cdd:cd03295 231 FVAEFVG 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-245 |
5.28e-58 |
|
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: 187.54 E-value: 5.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNysdkmMRDIKKDIGMIFQHFNLLNSATVF 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-----LPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL 180
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 181 TLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVSTVI 245
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-244 |
9.29e-58 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 189.92 E-value: 9.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 11 FHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKKDIGMIFQH 90
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 91 -FNLLN-SATVFKNVAMPLIL--SKKSKTEIKQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARALVTNPKILLCD 165
Cdd:PRK15079 107 pLASLNpRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 166 EATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVSTV 244
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
1.21e-57 |
|
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: 186.39 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDik 81
Cdd:cd03296 3 IEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPL----ILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIA 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 493203783 238 QNFV 241
Cdd:cd03296 234 YSFL 237
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
1.55e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 186.45 E-value: 1.55e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysdkmmRDI 80
Cdd:COG1121 6 AIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNS--ATVFKNVAMPLI----LSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVEtGTVKEVFSHP 232
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPE 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
1.04e-56 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 184.57 E-value: 1.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKkkQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIV-----DGHDIMNYSDK 75
Cdd:PRK11264 3 AIEVKNLVKKFHG--QTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 76 MMRDIKKDIGMIFQHFNLLNSATVFKNVAM-PLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKT 234
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
|
....*...
gi 493203783 235 TIAQNFVS 242
Cdd:PRK11264 238 PRTRQFLE 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
6.11e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 181.88 E-value: 6.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHkkkqtiDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdi 80
Cdd:COG3840 1 MLRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAmpLILS---KKSKTEiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIG--LGLRpglKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-220 |
6.39e-56 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 181.61 E-value: 6.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-241 |
6.90e-55 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 180.42 E-value: 6.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHK-----KKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImNYSDKM 76
Cdd:COG4167 5 LEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 77 MRdiKKDIGMIFQHFNL-LN-SATVFKNVAMPLIL-SKKSKTEIKQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVAIA 152
Cdd:COG4167 84 YR--CKHIRMIFQDPNTsLNpRLNIGQILEEPLRLnTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
....*....
gi 493203783 233 KTTIAQNFV 241
Cdd:COG4167 242 QHEVTKRLI 250
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-251 |
1.71e-54 |
|
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: 178.70 E-value: 1.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDkmmRDI 80
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR---REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAM---PLI--LSKKSKTEiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARAL 155
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 156 VTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPktT 235
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPE--L 230
|
250
....*....|....*..
gi 493203783 236 IAQNF-VSTVIQTEPST 251
Cdd:COG1120 231 LEEVYgVEARVIEDPVT 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-244 |
1.40e-52 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 177.72 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFhkkkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysdKMMRDI 80
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNF 240
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
....
gi 493203783 241 VSTV 244
Cdd:PRK11607 250 IGSV 253
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-228 |
1.41e-52 |
|
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: 184.27 E-value: 1.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:COG2274 474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHfNLLNSATVFKNVAMplilskkSKTEI-KQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRV 149
Cdd:COG2274 549 RQIGVVLQD-VFLFSGTIRENITL-------GDPDAtDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 150 AIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEV 228
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEEL 696
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
1.57e-52 |
|
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: 173.51 E-value: 1.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdI 80
Cdd:COG4555 1 MIEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-230 |
2.09e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 174.53 E-value: 2.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDI 80
Cdd:PRK13650 4 IIEVKNLTFKYKED-QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL---TEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKdICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-242 |
2.60e-52 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 173.30 E-value: 2.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL-----EAASNGQVIVDGHDImnYSDKM-MRDIKKDIGMIFQHFNL 93
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDI--YDPDVdVVELRRRVGMVFQKPNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 94 LnSATVFKNVAMPL-ILSKKSKTEIKQRVTEMLEFVGL----SDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:COG1117 104 F-PKSIYDNVAYGLrLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 169 SALDPATTASILTLLKNVNQTFgiTIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVS 242
Cdd:COG1117 183 SALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
6.95e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 173.31 E-value: 6.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMmRDIKKDIGMIFQH--FNLLNSa 97
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKL-SDIRKKVGLVFQYpeYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 98 TVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLS--DKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPAT 175
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493203783 176 TASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVF 229
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-223 |
8.05e-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: 170.51 E-value: 8.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdiK 81
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-217 |
8.13e-52 |
|
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: 170.79 E-value: 8.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysdkmmRDIKKDIGMIFQHFNLLNS--A 97
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSIDRDfpI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 98 TVFKNVAMPLI----LSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDP 173
Cdd:cd03235 86 SVRDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493203783 174 ATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKG 217
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
8.71e-52 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 169.12 E-value: 8.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysDKMMRDIK 81
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVamplilskkskteikqrvtemlefvglsdkkdqfpdELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-233 |
9.87e-52 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 174.00 E-value: 9.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 6 QVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKKDIG 85
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 86 MIFQH-FNLLN-SATVFKNVAMPL-ILSKKSKTEIKQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK11308 96 IVFQNpYGSLNpRKKVGQILEEPLlINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
1.57e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 174.75 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdiK 81
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFV 241
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-241 |
4.81e-51 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 170.64 E-value: 4.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 10 SFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKKDIGMIFQ 89
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 90 H-FNLLNS-ATVFKNVAMPLI-LSKKSKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVTNPKILLCD 165
Cdd:PRK10419 97 DsISAVNPrKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 166 EATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV--FSHPKTTIAQNFV 241
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltFSSPAGRVLQNAV 254
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-242 |
4.95e-51 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 170.15 E-value: 4.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 11 FHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSD----------KMMRDI 80
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNV-AMPLILSKKSKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQ 238
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....
gi 493203783 239 NFVS 242
Cdd:PRK10619 250 QFLK 253
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-227 |
8.20e-51 |
|
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: 168.32 E-value: 8.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 13 KKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMnysdKMMRDIKKDIGMIFQHFN 92
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 93 LLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 173 PATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKE 227
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-219 |
8.46e-51 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 168.84 E-value: 8.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 5 RQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIK-KD 83
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 84 IGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILL 163
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 164 CDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDIcNRVAVMEKGQV 219
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-244 |
1.69e-49 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 169.11 E-value: 1.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDik 81
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLIL----SKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIA 237
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFV 233
|
....*..
gi 493203783 238 QNFVSTV 244
Cdd:PRK10851 234 LEFMGEV 240
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-227 |
1.97e-49 |
|
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: 164.60 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMnysdKMMRDIK 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKE 227
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
2.06e-49 |
|
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: 162.94 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIk 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdIGMIFQHFNLLNsATVFKNVamplilskkskteikqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKI 161
Cdd:cd03228 78 --IAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQ 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
3.30e-49 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 173.04 E-value: 3.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysdkmmRDIK 81
Cdd:COG1132 340 IEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--------RDLT 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KD-----IGMIFQHFNLLnSATVFKNVAmpliLSKKSKTEikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQ 145
Cdd:COG1132 409 LEslrrqIGVVPQDTFLF-SGTIRENIR----YGRPDATD--EEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 146 KQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGT 224
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
4.33e-49 |
|
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: 161.28 E-value: 4.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIKKDIGMIFQHFNLLNSATVF 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 101 KNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPD----ELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-231 |
4.83e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 165.57 E-value: 4.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 10 SFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhdiMNYSDKMMRDIKKDIGMIFQ 89
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 90 H-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:PRK13635 89 NpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 169 SALDPATTASILTLLKNVNQTFGITIMMITHemrvikDI-----CNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLSITH------DLdeaaqADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
2.20e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 161.52 E-value: 2.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKKSKTEikQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG4619 74 RQVAYVPQEPALW-GGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-240 |
2.39e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 166.05 E-value: 2.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhKKKQTIDalkDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdiK 81
Cdd:PRK11432 7 VVLKNITKRF-GSNTVID---NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-----Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNF 240
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-244 |
1.73e-47 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 165.21 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIK-KDIGMIFQHFNLLNSAT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 99 VFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAS 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 179 ILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVSTV 244
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
4.87e-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: 158.13 E-value: 4.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNhNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMnysdKMMRDIK 81
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTfgITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-242 |
5.15e-47 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 159.69 E-value: 5.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhkkkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL-----EAASNGQVIVDGHDIMnysdKM 76
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF----KM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 77 -MRDIKKDIGMIFQHFNLLNSATVFKNVAMPLILSK--KSKTEIKQRVTEMLEFVGLSDK-KDQF---PDELSGGQKQRV 149
Cdd:PRK14247 76 dVIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEvKDRLdapAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 150 AIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfgITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVF 229
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
250
....*....|...
gi 493203783 230 SHPKTTIAQNFVS 242
Cdd:PRK14247 234 TNPRHELTEKYVT 246
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-267 |
5.84e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 160.24 E-value: 5.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImNYSDKMMRDI 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHF-NLLNSATVFKNVAM-PLILsKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK13639 77 RKTVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQ 238
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRKA 234
|
250 260
....*....|....*....|....*....
gi 493203783 239 NFVSTVIqtepsTSLIRRLNDEQVGDFKD 267
Cdd:PRK13639 235 NLRLPRV-----AHLIEILNKEDNLPIKM 258
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-230 |
8.47e-47 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 159.87 E-value: 8.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTID--ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDkmMR 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DIKKDIGMIFQH-FNLLNSATVFKNVAM-PLILSKKSKtEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFgPENLGIPPE-EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-223 |
1.54e-46 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 156.06 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 3 EFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIKK 82
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 83 DIGMIFQhfnllnsatvfknvamplilskkskteikqrvteMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKIL 162
Cdd:cd03214 74 KIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 163 LCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
4.95e-46 |
|
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: 153.94 E-value: 4.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 3 EFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIKK 82
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 83 DIGMIFQhfnllnsatvfknvamplilskkskteikqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKIL 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 163 LCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQ 218
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-223 |
1.55e-45 |
|
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: 154.38 E-value: 1.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 23 DVSFTVNHNDIfGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKM-MRDIKKDIGMIFQHFNLLNSATVFK 101
Cdd:cd03297 16 KIDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 102 NVAmpLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILT 181
Cdd:cd03297 95 NLA--FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493203783 182 LLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-233 |
5.35e-45 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 161.03 E-value: 5.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKK----KQTID---ALKDVSFTVNHNDIFGVIGYSGAGKST----LVRLVNhleaaSNGQVIVDGHDI 69
Cdd:PRK15134 275 LLDVEQLQVAFPIRkgilKRTVDhnvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 70 MNYSDKMMRDIKKDIGMIFQHFN-LLN-SATVFKNVAMPLILSKK--SKTEIKQRVTEMLEFVGLS-DKKDQFPDELSGG 144
Cdd:PRK15134 350 HNLNRRQLLPVRHRIQVVFQDPNsSLNpRLNVLQIIEEGLRVHQPtlSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGT 224
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
....*....
gi 493203783 225 VKEVFSHPK 233
Cdd:PRK15134 510 CERVFAAPQ 518
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
7.17e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 154.52 E-value: 7.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDI 80
Cdd:PRK13648 7 IIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-228 |
3.14e-44 |
|
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: 151.43 E-value: 3.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 18 IDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNY-SDKMMRdikKDIGMIFQHFNLLNS 96
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERAR---AGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 97 ATVFKNVAMPLILSKKSKteIKQRVTEMLE-FVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPAT 175
Cdd:cd03224 90 LTVEENLLLGAYARRRAK--RKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493203783 176 TASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:cd03224 168 VEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
3.22e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 152.71 E-value: 3.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmmrdi 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 kKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG4525 76 -ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITH 199
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
9.33e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 151.88 E-value: 9.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSksfHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDI 80
Cdd:PRK13652 3 LIETRDLC---YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFN-LLNSATVFKNVAM-PLILSKKSKTeIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK13652 77 RKFVGLVFQNPDdQIFSPTVEQDIAFgPINLGLDEET-VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-223 |
1.04e-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: 149.57 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 23 DVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDiMNYSDKMMRDIKkdigMIFQHFNLLNSATVFKN 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD-VTAAPPADRPVS----MLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 103 VAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTL 182
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493203783 183 LKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
1.58e-43 |
|
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: 149.28 E-value: 1.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:cd03245 3 IEFRNVS--FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKKskteikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNITLGAPLADD------ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVnqTFGITIMMITHEMRVIkDICNRVAVMEKGQVVETG 223
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-232 |
1.41e-42 |
|
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: 151.02 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 23 DVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnYSDKMMRDI---KKDIGMIFQHFNLLNSATV 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLpphRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNV--AMPLILSKKSKTEIkQRVTEMLefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:COG4148 95 RGNLlyGRKRAPRAERRISF-DEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 178 SILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:COG4148 171 EILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
11-260 |
1.51e-42 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 155.78 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 11 FHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKKDIGMIFQ- 89
Cdd:PRK10261 330 LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQd 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 90 -HFNLLNSATVFKNVAMPLILSKKSKTEIKQ-RVTEMLEFVGLSDKKD-QFPDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:PRK10261 410 pYASLDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 167 ATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVSTVIQ 246
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPV 569
|
250
....*....|....*.
gi 493203783 247 TEPSTSLIRR--LNDE 260
Cdd:PRK10261 570 ADPSRQRPQRvlLSDD 585
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-230 |
1.66e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 148.84 E-value: 1.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImNYSDKMMRDIKKDIGMIFQH-FNLLNSAT 98
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 99 VFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAS 178
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493203783 179 ILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-230 |
2.61e-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: 146.86 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdik 81
Cdd:cd03252 1 ITFEHVR--FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHfNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIARALV 156
Cdd:cd03252 76 RQVGVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFIsELPEGYDTIVGEqgagLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFS 230
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-232 |
2.64e-42 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 149.49 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKS-TLVRLVNHLeaASNGQV----IVDGHDIMNYSDKMMRDIK-KDIGMIFQH-FN 92
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIggsaTFNGREILNLPEKELNKLRaEQISMIFQDpMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 93 LLNS-ATVFKNVAMPLILSKK-SKTEIKQRVTEMLEFVGLSDKKDQ---FPDELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:PRK09473 109 SLNPyMRVGEQLMEVLMLHKGmSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 168 TSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.19e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.44 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDI 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEM-RVIKdiCNRVAVMEKGQVVETGTVKEVF 229
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAIL--ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
3.37e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 148.24 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQ-TIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSD-KMMRD 79
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQhF--NLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK13634 83 LRKKVGIVFQ-FpeHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-233 |
5.62e-42 |
|
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: 145.69 E-value: 5.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYS-DKMMrdikkdigmIFQHFNLLNSATV 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNVAMPL--ILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 178 SILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV-FSHPK 233
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-231 |
2.33e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 145.66 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYS-DKMMRDIKKDIGMIFQhF--NLLNS 96
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKKVGLVFQ-FpeSQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 97 ATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPAT 175
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 176 TASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-242 |
3.42e-41 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 144.53 E-value: 3.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL-----EAASNGQVIVDGHDImnYSDK 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI--YSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 76 M-MRDIKKDIGMIFQHFNLLnSATVFKNVAMPL-ILSKKSKTEIKQRVTEMLEFVGLSDK-KDQFPDE---LSGGQKQRV 149
Cdd:PRK14239 79 TdTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLrLKGIKDKQVLDEAVEKSLKGASIWDEvKDRLHDSalgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 150 AIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFgiTIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVF 229
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
250
....*....|...
gi 493203783 230 SHPKTTIAQNFVS 242
Cdd:PRK14239 236 MNPKHKETEDYIS 248
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-240 |
3.77e-41 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 144.55 E-value: 3.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKK-----KQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDiMNYSDK 75
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP-LHFGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 76 MMRdiKKDIGMIFQH-FNLLN-SATVFKNVAMPLILSKK-SKTEIKQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAI 151
Cdd:PRK15112 83 SYR--SQRIRMIFQDpSTSLNpRQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 152 ARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|....
gi 493203783 232 P-----KTTIAQNF 240
Cdd:PRK15112 241 PlheltKRLIAGHF 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-246 |
4.35e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 151.55 E-value: 4.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKS-TLVRLVNHLEAAS-------------NGQVIvdg 66
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGglvqcdkmllrrrSRQVI--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 67 hDIMNYSDKMMRDIK-KDIGMIFQH-FNLLNSA-TVFKNVAMPLILSKK-SKTEIKQRVTEMLEFVGLSDKK---DQFPD 139
Cdd:PRK10261 89 -ELSEQSAAQMRHVRgADMAMIFQEpMTSLNPVfTVGEQIAESIRLHQGaSREEAMVEAKRMLDQVRIPEAQtilSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 140 ELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260
....*....|....*....|....*..
gi 493203783 220 VETGTVKEVFSHPKTTIAQNFVSTVIQ 246
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVPQ 274
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-227 |
1.59e-40 |
|
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: 141.98 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdik 81
Cdd:cd03253 1 IEFENVTFAYDPGRPV---LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNsATVFKNVAMplilSKKSKTEikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:cd03253 75 RAIGVVPQDTVLFN-DTIGYNIRY----GRPDATD--EEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKE 227
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-245 |
1.79e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 142.67 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL-----EAASNGQVIVDGHDImnYSDKMMR-DIKKDIGMIFQHFNLL 94
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 95 NSATVFKNVAMPLILSK--KSKTEIKQRVTEMLEFVGLSDK-KDQ---FPDELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEvKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 169 SALDPATTASILTLLKNVNQTFgiTIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVSTVI 245
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
9.12e-40 |
|
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: 139.43 E-value: 9.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMnysdKMMRDI 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
1.43e-39 |
|
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: 146.83 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLD---PASWR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNsATVFKNVAmpliLSKKSKTEikQRVTEMLEFVGLSDKKDQFPD-------E----LSGGQKQRVA 150
Cdd:COG4988 411 RQIAWVPQNPYLFA-GTIRENLR----LGRPDASD--EELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFS 230
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLA 560
|
.
gi 493203783 231 H 231
Cdd:COG4988 561 K 561
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-287 |
1.78e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 141.01 E-value: 1.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDI 80
Cdd:COG4152 1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 -----------KKDIGMIFQHFNLLnsatvfKNVamplilskkSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRV 149
Cdd:COG4152 74 gylpeerglypKMKVGEQLVYLARL------KGL---------SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 150 AIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVf 229
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 230 shpKTTIAQNFVstVIQTEPSTSLIRRLNDEQVGDFKD--YKIFVEETQVTQPIINDLIQ 287
Cdd:COG4152 217 ---RRQFGRNTL--RLEADGDAGWLRALPGVTVVEEDGdgAELKLEDGADAQELLRALLA 271
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-227 |
2.03e-39 |
|
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: 146.45 E-value: 2.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIk 81
Cdd:COG4987 334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdIGMIFQHFNLLNsATVFKNvampLILSKKSKTEikQRVTEMLEFVGLSDKKDQFPD-------E----LSGGQKQRVA 150
Cdd:COG4987 411 --IAVVPQRPHLFD-TTLREN----LRLARPDATD--EELWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIkDICNRVAVMEKGQVVETGTVKE 227
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEE 555
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
3.19e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 144.78 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGH--DIMNYSDKmmr 78
Cdd:COG3845 5 ALELRGITKRFGGVV----ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 dIKKDIGMIFQHFNLLNSATVFKNVAM---PLILSKKSKTEIKQRVTEMLEFVGLS-DkkdqfPD----ELSGGQKQRVA 150
Cdd:COG3845 78 -IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvD-----PDakveDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKN-VNQtfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRlAAE--GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
4.71e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.39 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDG--HDIMNYSDkmmr 78
Cdd:COG1129 4 LLEMRGISKSFGGVK----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DIKKDIGMIFQHFNLLNSATVFKNVAMPLILSKK---SKTEIKQRVTEMLEFVGLS-DkkdqfPD----ELSGGQKQRVA 150
Cdd:COG1129 76 AQAAGIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDiD-----PDtpvgDLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-227 |
7.15e-39 |
|
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: 137.67 E-value: 7.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIdALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:cd03249 1 IEFKNVSFRYPSRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNsATVFKNVAmpliLSKKSKT--EIKQ--RVTEMLEFV-GLSDKKD----QFPDELSGGQKQRVAIA 152
Cdd:cd03249 77 SQIGLVSQEPVLFD-GTIAENIR----YGKPDATdeEVEEaaKKANIHDFImSLPDGYDtlvgERGSQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKE 227
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
7.92e-39 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 136.96 E-value: 7.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdik 81
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdIGMIFQHFNLLNSATVFKNvampLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03268 74 --IGALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-233 |
9.76e-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: 9.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 18 IDALKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAASnGQVIVDGHDIMNYS-DKMMRdikKDIGM------IFQ 89
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLLPPRS-GSIRFDGEDITGLPpHRIAR---LGIGYvpegrrIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 90 HFnllnsaTVFKNVAMPLILsKKSKTEIKQRVTEMLE-FVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:COG0410 92 SL------TVEENLLLGAYA-RRDRAEVRADLERVYElFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 169 SALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-221 |
1.03e-38 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 137.22 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 K-KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDiCNRVAVMEKGQVVE 221
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
1.31e-38 |
|
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: 136.98 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSaTVFKNVAmpliLSKKSKTEikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIA----YGRPGATR--EEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 151 IARALVTNPKILLCDEATSALDPAT----TASILTLLKNVnqtfgiTIMMITHEMRVIKDIcNRVAVMEKGQVVETGT 224
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESerlvQAALERLMKNR------TTFVIAHRLSTIENA-DRIVVLEDGKIVERGT 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-261 |
1.52e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.39 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL---EAASNGQVIVDGhdiMNYSDKMMR 78
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDG---ITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DIKKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRViKDICNRVAVMEKGQVVETGTVKEVFshPKTTIA 237
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIF--SKVEML 237
|
250 260 270
....*....|....*....|....*....|..
gi 493203783 238 QN------FVSTVIQ--TEPSTSLIRRLNDEQ 261
Cdd:PRK13640 238 KEigldipFVYKLKNklKEKGISVPQEINTEE 269
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-222 |
2.51e-38 |
|
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: 134.09 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIK 81
Cdd:cd03216 1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdIGMIFQhfnllnsatvfknvamplilskkskteikqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKI 161
Cdd:cd03216 77 --IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVET 222
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-231 |
2.65e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 137.07 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRlvnHLEAASNGQVIVDGH-----DIMNYSDK 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKSAGSHiellgRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 76 MMRDIKKD---IGMIFQHFNLLNSATVFKNVAMPLILS--------KKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGG 144
Cdd:PRK09984 77 LARDIRKSranTGYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGT 224
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
250
....*....|.
gi 493203783 225 VK----EVFSH 231
Cdd:PRK09984 237 SQqfdnERFDH 247
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-232 |
3.42e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 138.50 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 17 TIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEaaSNGQVIVD-----GHDIMNYSDKMMRDI-KKDIGMIFQ 89
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITK--DNWHVTADrfrwnGIDLLKLSPRERRKIiGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 90 HFN--LLNSATVFKNV--AMPLILSK----KSKTEIKQRVTEMLEFVGLSDKKD---QFPDELSGGQKQRVAIARALVTN 158
Cdd:COG4170 97 EPSscLDPSAKIGDQLieAIPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-220 |
5.43e-38 |
|
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: 134.69 E-value: 5.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 7 VSKSFHKKkqtIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNysdkmmRDIKKDIGM 86
Cdd:cd03226 5 ISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 87 IFQHfnlLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:cd03226 76 VMQD---VDYQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493203783 167 ATSALDPATTASILTLLKNVnQTFGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:cd03226 153 PTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
1.04e-37 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 134.59 E-value: 1.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkMMRDIK 81
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP--MHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQtFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-233 |
1.06e-37 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 137.18 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 6 QVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKS----TLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI- 80
Cdd:PRK11022 8 KLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQhfNLLNSATVFKNVAMPLILSKK-----SKTEIKQRVTEMLEFVGLSD---KKDQFPDELSGGQKQRVAIA 152
Cdd:PRK11022 88 GAEVAMIFQ--DPMTSLNPCYTVGFQIMEAIKvhqggNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
.
gi 493203783 233 K 233
Cdd:PRK11022 246 R 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
1.14e-37 |
|
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: 141.09 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHK-KKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVD-GHDIMNYSDK--M 76
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPgpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 77 MRD-IKKDIGMIFQHFNLLNSATVFKNV--AMPLILSKKSKteiKQRVTEMLEFVGLSDKK-----DQFPDELSGGQKQR 148
Cdd:TIGR03269 359 GRGrAKRYIGILHQEYDLYPHRTVLDNLteAIGLELPDELA---RMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 149 VAIARALVTNPKILLCDEATSALDPAT----TASILTLLKNVNQTFGItimmITHEMRVIKDICNRVAVMEKGQVVETGT 224
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITkvdvTHSILKAREEMEQTFII----VSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 493203783 225 VKEVFS 230
Cdd:TIGR03269 512 PEEIVE 517
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
1.58e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 135.17 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRD---IKKDIGMIFQHFNLLNSA 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDaikLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 98 TVFKNVAMPLILSK-KSKTEIKQRVTEMLEFVGL----SDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PRK14246 106 SIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 173 PATTASILTLLKNVNQTfgITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFV 241
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-245 |
1.72e-37 |
|
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: 137.55 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 23 DVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI-KKDIGMIFQHFNLLNSATVFK 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 102 NVAMPLILSKKSKTEIK-QRVTEMLefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL 180
Cdd:TIGR02142 95 NLRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 181 TLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPK-TTIAQNFVSTVI 245
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlPWLAREDQGSLI 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-203 |
3.44e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 141.01 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNY-SDKMMRD 79
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRV 203
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQV 206
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
3.82e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 133.23 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkMMRDI 80
Cdd:COG1137 3 TLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--MHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGM------IFQhfNLlnsaTVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:COG1137 77 RLGIGYlpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTL---LKNvnqtFGITImMIT-HEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIirhLKE----RGIGV-LITdHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
...
gi 493203783 231 HPK 233
Cdd:COG1137 226 NPL 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-224 |
4.65e-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: 140.34 E-value: 4.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdik 81
Cdd:COG5265 358 VRFENVSFGYDPERP-I--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR--- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQH---FNllnsATVFKNVAM--PlilsKKSKTEIKQ--RVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRV 149
Cdd:COG5265 432 AAIGIVPQDtvlFN----DTIAYNIAYgrP----DASEEEVEAaaRAAQIHDFIeSLPDGYDTRVGErglkLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 150 AIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGT 224
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-249 |
5.25e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 134.36 E-value: 5.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 7 VSKSFHKKKQ-TIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKM--MRDIKKD 83
Cdd:PRK13645 12 VSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkeVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 84 IGMIFQ--HFNLLNSaTVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK13645 92 IGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKttiaqnf 240
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE------- 243
|
....*....
gi 493203783 241 VSTVIQTEP 249
Cdd:PRK13645 244 LLTKIEIDP 252
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-229 |
5.62e-37 |
|
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: 132.73 E-value: 5.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdik 81
Cdd:cd03254 3 IEFENVNFSYDEKKPV---LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIARALV 156
Cdd:cd03254 77 SMIGVVLQDTFLF-SGTIMENIRLGRPNATDEEVIEAAKEAGAHDFImKLPNGYDTVLGEnggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVF 229
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-245 |
7.11e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 135.74 E-value: 7.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQtidALKDVSFTVnHNDIFGVI-GYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRD 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ---VIKGIDLDV-ADGEFIVLvGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---NELEPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 ikKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTE---MLEFVGLSDKKdqfPDELSGGQKQRVAIARALV 156
Cdd:PRK11650 76 --RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITH---EMRVIKDicnRVAVMEKGQVVETGTVKEVFSHPK 233
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHdqvEAMTLAD---RVVVMNGGVAEQIGTPVEVYEKPA 227
|
250
....*....|..
gi 493203783 234 TTiaqnFVSTVI 245
Cdd:PRK11650 228 ST----FVASFI 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-245 |
1.05e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 134.59 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 13 KKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQV----IVDGHDIMNYSD---------KMMRD 79
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkiKNFKE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQ--HFNLLNSaTVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK13631 114 LRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP---- 232
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQhiin 271
|
250
....*....|...
gi 493203783 233 KTTIAQNFVSTVI 245
Cdd:PRK13631 272 STSIQVPRVIQVI 284
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-223 |
1.55e-36 |
|
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: 130.86 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHdimnysdKMMRDIK 81
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-------PLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVnQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-231 |
2.98e-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: 137.54 E-value: 2.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:TIGR02203 331 VEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSaTVFKNVAMplilsKKSKTEIKQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:TIGR02203 406 RQVALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFS 230
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
.
gi 493203783 231 H 231
Cdd:TIGR02203 557 R 557
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-230 |
3.84e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 130.47 E-value: 3.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 25 SFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdiKKDIGMIFQHFNLLNSATVFKNVA 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 105 MPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLK 184
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493203783 185 NVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-224 |
5.70e-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: 129.54 E-value: 5.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTidALKDVSFTVNHNDIFGVIGYSGAGKSTLV----RLVNhleaASNGQVIVDGHDImnySDKMM 77
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDGVDI---SKIGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 RDIKKDIGMIFQHfNLLNSATVFKNVAmplILSKKSKTEIKQrvteMLEFVGLSDKKDQFPDEL-----------SGGQK 146
Cdd:cd03244 74 HDLRSRISIIPQD-PVLFSGTIRSNLD---PFGEYSDEELWQ----ALERVGLKEFVESLPGGLdtvveeggenlSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 147 QRVAIARALVTNPKILLCDEATSALDPATTASILTLLKnvNQTFGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
6.02e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.98 E-value: 6.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKkkQTID---ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNysdkmM 77
Cdd:COG1101 1 MLELKNLSKTFNP--GTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 RDIK--KDIGMIFQhfN-LLNSA---TVFKNVAM--------PLI--LSKKSKTEIKQRVTEM-LefvGLSDKKDQFPDE 140
Cdd:COG1101 74 PEYKraKYIGRVFQ--DpMMGTApsmTIEENLALayrrgkrrGLRrgLTKKRRELFRELLATLgL---GLENRLDTKVGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-234 |
1.20e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 135.60 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAAS-----NGQVIVDGHDIMNYSDK 75
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 76 MMRDIKKD-IGMIFQH----FNLLNsaTVFKNVAMPLILSKKSKTEIKQrvTEM---LEFVGLSDKKDQ---FPDELSGG 144
Cdd:PRK15134 85 TLRGVRGNkIAMIFQEpmvsLNPLH--TLEKQLYEVLSLHRGMRREAAR--GEIlncLDRVGIRQAAKRltdYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGT 224
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250
....*....|...
gi 493203783 225 VKEVFS---HPKT 234
Cdd:PRK15134 241 AATLFSaptHPYT 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-219 |
1.59e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.80 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 5 RQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVdghdimnySDKMMRDIKKDI 84
Cdd:PRK11247 16 NAVSKRYGER--TV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA--------GTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 85 GMIFQHFNLLNSATVFKNVAMPLilskksKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLC 164
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 165 DEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-231 |
5.32e-35 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 127.89 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFH------------------KKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQV 62
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 63 IVDGhdimnysdkmmrdikK-----DIGMIFQhfnllNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQf 137
Cdd:COG1134 84 EVNG---------------RvsallELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 138 P-DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEK 216
Cdd:COG1134 143 PvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
250
....*....|....*
gi 493203783 217 GQVVETGTVKEVFSH 231
Cdd:COG1134 222 GRLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-266 |
6.36e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 128.79 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVS------KSFHKKkqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDI-MNYSD 74
Cdd:PRK13641 3 IKFENVDyiyspgTPMEKK-----GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 75 KMMRDIKKDIGMIFQhF--NLLNSATVFKNVAM-PLILSKkSKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVA 150
Cdd:PRK13641 78 KNLKKLRKKVSLVFQ-FpeAQLFENTVLKDVEFgPKNFGF-SEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVnQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 493203783 231 HPKtTIAQNFVStviqtEPSTSLIRRlnDEQVGDFK 266
Cdd:PRK13641 235 DKE-WLKKHYLD-----EPATSRFAS--KLEKGGFK 262
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-229 |
1.19e-34 |
|
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: 127.12 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVN-HLEAASNGQVIVDGHDIMNYSdkmMRD 79
Cdd:COG1119 3 LLELRNVTVRRGGK--TI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGERRGGED---VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMI--FQHFNLLNSATVFkNVamplILS---------KKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQR 148
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVL-DV----VLSgffdsiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 149 VAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
.
gi 493203783 229 F 229
Cdd:COG1119 231 L 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-227 |
3.60e-34 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 132.01 E-value: 3.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIK 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI---RTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNsatvfKNVAMPLILSKKSKTEIKQR----VTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIA 152
Cdd:PRK13657 409 RNIAVVFQDAGLFN-----RSIEDNIRVGRPDATDEEMRaaaeRAQAHDFIeRKPDGYDTVVGErgrqLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKE 227
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-230 |
4.50e-34 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 131.08 E-value: 4.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASN--GQVIV--------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPtsGRIIYhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 65 -DGH--------------DIMNYSDKMMRDIKKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFV 128
Cdd:TIGR03269 77 kVGEpcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 129 GLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|..
gi 493203783 209 NRVAVMEKGQVVETGTVKEVFS 230
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-219 |
5.87e-34 |
|
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: 123.10 E-value: 5.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIkkdIGMIFQHFNLLnSATVF 100
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH---VGYLPQDDELF-SGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVamplilskkskteikqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL 180
Cdd:cd03246 94 ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 493203783 181 TLLKNVnQTFGITIMMITHEMRVIKdICNRVAVMEKGQV 219
Cdd:cd03246 137 QAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-227 |
7.10e-34 |
|
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: 131.62 E-value: 7.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIK 81
Cdd:TIGR03797 452 IEVDRVT--FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL---AGLDVQAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKKskteikqRVTEMLEFVGLSDKKDQFP-------DE----LSGGQKQRVA 150
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENIAGGAPLTLD-------EAWEAARMAGLAEDIRAMPmgmhtviSEgggtLSGGQRQRLL 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNqtfgITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKE 227
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-249 |
1.08e-33 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.45 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 4 FRQVSKSFHKKKQTidalKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDghdimnysDKMMRDI--- 80
Cdd:PRK11000 6 LRNVTKAYGDVVIS----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--------EKRMNDVppa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK11000 74 ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIA--- 237
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVagf 233
|
250
....*....|....*...
gi 493203783 238 -----QNFVS-TVIQTEP 249
Cdd:PRK11000 234 igspkMNFLPvKVTATAI 251
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
1.22e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 125.10 E-value: 1.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFhkkKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDkmMRDI 80
Cdd:PRK13644 1 MIRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQhfnllNSATVF-------------KNVAMPlilskksKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQ 147
Cdd:PRK13644 76 RKLVGIVFQ-----NPETQFvgrtveedlafgpENLCLP-------PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 148 RVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKE 227
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPEN 221
|
....*
gi 493203783 228 VFSHP 232
Cdd:PRK13644 222 VLSDV 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-229 |
3.04e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 124.46 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTID-ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYS-DKMMR 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DIKKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVF 229
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-234 |
4.33e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 124.81 E-value: 4.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKS-----------------FHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVI 63
Cdd:COG4586 1 IIEVENLSKTyrvyekepglkgalkglFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 64 VDGHDImnYSDKmmRDIKKDIGMIF-Q----HFNLlnsatvfknvamPLI----LSKK----SKTEIKQRVTEMLEFVGL 130
Cdd:COG4586 81 VLGYVP--FKRR--KEFARRIGVVFgQrsqlWWDL------------PAIdsfrLLKAiyriPDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 131 SDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNR 210
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
|
250 260
....*....|....*....|....*..
gi 493203783 211 VAVMEKGQVVETGTV---KEVFSHPKT 234
Cdd:COG4586 225 VIVIDHGRIIYDGSLeelKERFGPYKT 251
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-243 |
9.27e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 123.66 E-value: 9.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQT-IDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSD------ 74
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 75 ---------------KMMRDIKKDIGMIFQ--HFNLLNSaTVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKK-DQ 136
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 137 FPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEK 216
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260
....*....|....*....|....*..
gi 493203783 217 GQVVETGTVKEVFSHPKTTIAQNFVST 243
Cdd:PRK13651 241 GKIIKDGDTYDILSDNKFLIENNMEPP 267
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-228 |
9.79e-33 |
|
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: 121.48 E-value: 9.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMrdIKKDIG------MIFQHFnl 93
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER--ARAGIAyvpqgrEIFPRL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 94 lnsaTVFKNVAMPLILSKKSKTEIKQRVTEMleFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDP 173
Cdd:TIGR03410 91 ----TVEENLLTGLAALPRRSRKIPDEIYEL--FPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 174 ATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-223 |
1.15e-32 |
|
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: 121.10 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFH------------------KKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVI 63
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 64 VDGhdimnysdkmmrdikKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSG 143
Cdd:cd03220 81 VRG---------------RVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 144 GQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITImMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVI-LVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-230 |
1.41e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 122.58 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQ-TIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYS-DKMMRD 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQhfnlLNSATVF------------KNVAMPLilskkskTEIKQRVTEMLEFVGLS-DKKDQFPDELSGGQK 146
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFedtvereiifgpKNFKMNL-------DEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 147 QRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVK 226
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
....
gi 493203783 227 EVFS 230
Cdd:PRK13646 232 ELFK 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-220 |
1.95e-32 |
|
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: 119.58 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKK--KQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVN--HLEAASNGQVIVDGHDImnysdkMM 77
Cdd:cd03213 4 LSFRNLTVTVKSSpsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 RDIKKDIGMIFQHFNLLNSATVFKNVAMPLILSKkskteikqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVT 157
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMR-VIKDICNRVAVMEKGQVV 220
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRVI 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-201 |
4.78e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 120.19 E-value: 4.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhdimnysdKMMRDIKKDIGMIFQHFNLLNSATV 99
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--------KPVEGPGAERGVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|..
gi 493203783 180 LTLLKNVNQTFGITIMMITHEM 201
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDI 189
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
1.03e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 117.97 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysDKMMRDI 80
Cdd:COG4133 2 MLEAENLSCRRGER--LL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFqHFNLLNSA-TVFKNVAMPLILSKKSKTEIkqRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG4133 74 RRRLAYLG-HADGLKPElTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGItIMMITHE 200
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-232 |
1.82e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.94 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdiKKDIGMIFQHFNLLNSATV 99
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKN--VAMPLILS-------------KKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLC 164
Cdd:PRK11300 98 IENllVAQHQQLKtglfsgllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 165 DEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-238 |
1.96e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 119.10 E-value: 1.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSksFHKKKQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEM-LEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQ 238
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQ 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-223 |
2.22e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.07 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 6 QVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIKKDIG 85
Cdd:PRK13647 6 EVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 86 MIFQH-FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLC 164
Cdd:PRK13647 83 LVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 165 DEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-230 |
5.39e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 118.27 E-value: 5.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 12 HKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIKKDIGMIFQH- 90
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELL---TAENVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 91 FNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 171 LDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
8.30e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.11 E-value: 8.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDkmmRDI 80
Cdd:COG4604 1 MIEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS---REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQ--HFNL-LnsaTVFKNVAM---PLilSK-KSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:COG4604 74 AKRLAILRQenHINSrL---TVRELVAFgrfPY--SKgRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 154 ALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMithemrVIKDI------CNRVAVMEKGQVVETGTVKE 227
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVI------VLHDInfascyADHIVAMKDGRVVAQGTPEE 222
|
.
gi 493203783 228 V 228
Cdd:COG4604 223 I 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
8.79e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.18 E-value: 8.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAASnGQVIVDGHDIMNYSDkmmRD 79
Cdd:PRK13548 2 MLEARNLSVRLGGR--TL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRaLSGELSPDS-GEVRLNGRPLADWSP---AE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV--- 156
Cdd:PRK13548 74 LARRRAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 157 ---TNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHemrvikDI------CNRVAVMEKGQVVETGTVKE 227
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH------DLnlaaryADRIVLLHQGRLVADGTPAE 227
|
...
gi 493203783 228 VFS 230
Cdd:PRK13548 228 VLT 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-231 |
1.22e-30 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 122.05 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIK 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSaTVFKNVAMPLiLSKKSKTEIKQ--RVTEMLEFVglsDKKDQFPDE--------LSGGQKQRVAI 151
Cdd:PRK11176 417 NQVALVSQNVHLFND-TIANNIAYAR-TEQYSREQIEEaaRMAYAMDFI---NKMDNGLDTvigengvlLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 152 ARALVTNPKILLCDEATSALDP----ATTASILTLLKNVnqtfgiTIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKE 227
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTeserAIQAALDELQKNR------TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
....
gi 493203783 228 VFSH 231
Cdd:PRK11176 565 LLAQ 568
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-232 |
1.38e-30 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 122.14 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSF--HKKKQTidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRd 79
Cdd:TIGR00958 479 IEFQDVSFSYpnRPDVPV---LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 ikKDIGMIFQHfNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIARA 154
Cdd:TIGR00958 555 --RQVALVGQE-PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFImEFPNGYDTEVGEkgsqLSGGQKQRIAIARA 631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 155 LVTNPKILLCDEATSALDpattASILTLLKNVNQTFGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:TIGR00958 632 LVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
2.13e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 120.66 E-value: 2.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFhkkkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDI 80
Cdd:PRK09700 5 YISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 kkDIGMIFQHFNLLNSATVFKNVAMPLILSKK-------SKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 154 ALVTNPKILLCDEATSALdpaTTASILTLLKNVNQ--TFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-231 |
2.40e-30 |
|
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: 121.01 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAASnGQVIVDGHDIMNYSDkmmRDIKKDIGMIFQHFNLLnSATV 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARlLVGVWPPTA-GSVRLDGADLSQWDR---EELGRHIGYLPQDVELF-DGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNVA-MPLILSkkskteikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:COG4618 423 AENIArFGDADP--------EKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 168 TSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKdICNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-199 |
2.59e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.50 E-value: 2.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAA--SNGQVIVDGHDImnySDKMMRdiKKDIGMIFQ------HF 91
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRL---TALPAE--QRRIGILFQddllfpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 92 NllnsatVFKNV--AMPlilSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:COG4136 92 S------VGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|
gi 493203783 170 ALDPATTASILTLLKNVNQTFGITIMMITH 199
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
2.71e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.62 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysDKMMRDIK 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVnQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
3.06e-30 |
|
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: 114.84 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSF---HKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGH----DIMNYS 73
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 74 DKMMRDIKKD-IGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLsdkkdqfPDEL--------SGG 144
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQ 218
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-242 |
3.07e-30 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 115.57 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 22 KDVSFTVNHNDIFGVIGYSGAGKS-TLVRLVNHLEA---ASNGQVIVDGhdiMNYSDKMMRDIKkdIGMIFQH----FN- 92
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDG---KPVAPCALRGRK--IATIMQNprsaFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 93 LLNSATVFKNVampliLSKKSKTEIKQRVTEMLEFVGLSDKK---DQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK10418 95 LHTMHTHARET-----CLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 170 ALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVS 242
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-234 |
4.10e-30 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 117.21 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLeAASNGQVIVDGH-----DIMNYSDK 75
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMrfddiDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 76 MMRD-IKKDIGMIFQH-FNLLNSAtvfKNVAMPLILSKKSKTEI----------KQRVTEMLEFVGLSDKKD---QFPDE 140
Cdd:PRK15093 82 ERRKlVGHNVSMIFQEpQSCLDPS---ERVGRQLMQNIPGWTYKgrwwqrfgwrKRRAIELLHRVGIKDHKDamrSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|....*..
gi 493203783 221 ETGTVKEVFS---HPKT 234
Cdd:PRK15093 239 ETAPSKELVTtphHPYT 255
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-241 |
8.02e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.75 E-value: 8.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 10 SFHKKKQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHL-----EAASNGQVIVDGHDIMNYSDKMMRdIKKDI 84
Cdd:PRK14258 14 SFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNR-LRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 85 GMIFQHFNLLnSATVFKNVAMPL-ILSKKSKTEIKQRVTEMLEFVGLSD----KKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK14258 91 SMVHPKPNLF-PMSVYDNVAYGVkIVGWRPKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEK-----GQVVETGTVKEVFSHPKT 234
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHD 249
|
....*..
gi 493203783 235 TIAQNFV 241
Cdd:PRK14258 250 SRTREYV 256
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-246 |
8.51e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 114.25 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 5 RQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDG-----HDIMNYSDKMMRD 79
Cdd:PRK11701 10 RGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 I-KKDIGMIFQHF--NLLNSATVFKNVAMPLI-LSKKSKTEIKQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARA 154
Cdd:PRK11701 86 LlRTEWGFVHQHPrdGLRMQVSAGGNIGERLMaVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKT 234
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
250
....*....|..
gi 493203783 235 TIAQNFVSTVIQ 246
Cdd:PRK11701 246 PYTQLLVSSVLQ 257
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-242 |
1.65e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 114.04 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNG-----QVIVDGHDIMNYSDKMmrDIKKDIGMIFQHFNLLn 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVL--EFRRRVGMLFQRPNPF- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 96 SATVFKNV-----AMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK14271 114 PMSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 171 LDPATTASILTLLKNVNQTfgITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVS 242
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-231 |
3.38e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 114.13 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhKKKQTIDALkdvSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmmRDIK 81
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGL---SFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVampLILSKK---SKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENL---LVFGRYfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-219 |
4.17e-29 |
|
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: 111.79 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIdALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIk 81
Cdd:cd03248 12 VKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdIGMIFQHfNLLNSATVFKNVAMPL-------ILSKKSKTEIKQRVTEMLEfvGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:cd03248 90 --VSLVGQE-PVLFARSLQDNIAYGLqscsfecVKEAAQKAHAHSFISELAS--GYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQTFgiTIMMITHEMRVIKDiCNRVAVMEKGQV 219
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-224 |
1.72e-28 |
|
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: 109.42 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIKKDIGMIFQHFNLLnSATV 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSSLTIIPQDPTLF-SGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNVAmplILSKKSKTEIKQ--RVTEMlefvGLSdkkdqfpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:cd03369 99 RSNLD---PFDEYSDEEIYGalRVSEG----GLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493203783 178 SIltlLKNVNQTF-GITIMMITHEMRVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03369 163 LI---QKTIREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-223 |
1.92e-28 |
|
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: 110.11 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSF-----------------HKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIV 64
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 65 DGhdIMNYSDKmmRDIKKDIGMIF-QHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSG 143
Cdd:cd03267 81 AG--LVPWKRR--KKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 144 GQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
3.94e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 114.54 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIk 81
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdIGMIFQHFNLLnSATVFKNvampLILSKKSKTEikQRVTEMLEFVGLSDKKDQfpDE------------LSGGQKQRV 149
Cdd:PRK11160 416 --ISVVSQRVHLF-SATLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLED--DKglnawlgeggrqLSGGEQRRL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 150 AIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDIcNRVAVMEKGQVVETGT 224
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-230 |
6.52e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 108.83 E-value: 6.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkMMRDIKKDIGMIFQHFNLLNSATVF 100
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP--LHARARRGIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAMPLILSKKSKTEIKQ-RVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493203783 180 LTLLKNVnQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK10895 177 KRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-232 |
6.75e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 108.81 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 33 IFGVigySGAGKSTLVRLVNHLEAASNGQVIVDGHdIMNYSDKmmrDI-----KKDIGMIFQHFNLLNSATVFKNV--AM 105
Cdd:PRK11144 29 IFGR---SGAGKTSLINAISGLTRPQKGRIVLNGR-VLFDAEK---GIclppeKRRIGYVFQDARLFPHYKVRGNLryGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 106 plilsKKSKTEIKQRVTEMLefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKN 185
Cdd:PRK11144 102 -----AKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493203783 186 VNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:PRK11144 174 LAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-242 |
1.79e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 105.63 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLE-----AASNGQVIVDGHDImNYSDKMMRDIKKDIGMIFQHFNLL 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNL-YAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 95 nSATVFKNVAM-PLILSKKSktEIKQRVTEMLEFVGLSDK-KDQFPDE---LSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK14243 104 -PKSIYDNIAYgARINGYKG--DMDELVERSLRQAALWDEvKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 170 ALDPATTASILTLLKNVNQTFgiTIMMITHEMRVIKDICNRVAVM---------EKGQVVETGTVKEVFSHPKTTIAQNF 240
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQATRDY 258
|
..
gi 493203783 241 VS 242
Cdd:PRK14243 259 VS 260
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-219 |
1.98e-26 |
|
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: 104.40 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhkKKQTidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDimnysdkMMRDIK 81
Cdd:TIGR03740 1 LETKNLSKRF--GKQT--AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP-------WTRKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNVAM-PLILSKKskteiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVhTTLLGLP-----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-219 |
2.03e-26 |
|
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: 103.28 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 19 DALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMrdIKKDIGMI---FQHFNLLN 95
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IRAGIAYVpedRKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 96 SATVFKNVAMPLILSkkskteikqrvtemlefvglsdkkdqfpdelsGGQKQRVAIARALVTNPKILLCDEATSALDPAT 175
Cdd:cd03215 92 DLSVAENIALSSLLS--------------------------------GGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493203783 176 TASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:cd03215 140 KAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
2.36e-26 |
|
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: 103.16 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMmrdiK 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL----S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNsATVFKNVAMPLilskkskteikqrvtemlefvglsdkkdqfpdelSGGQKQRVAIARALVTNPKI 161
Cdd:cd03247 75 SLISVLNQRPYLFD-TTLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 162 LLCDEATSALDPATTASILTLLknVNQTFGITIMMITHEMRVIKDIcNRVAVMEKGQVVETG 223
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
4.09e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 104.19 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKkkqtIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNY-SDKMMRD 79
Cdd:PRK11614 5 MLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 ikkDIGMIFQHFNLLNSATVFKNVAMPLILSkkSKTEIKQRVTEMLE-FVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK11614 81 ---AVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-228 |
1.30e-25 |
|
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: 107.52 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYsdkmmrdikkDIGMIFQHFNLLN---- 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI----------DRHTLRQFINYLPqepy 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 96 --SATVFKNvampLILSKKSKTEIkQRVTEMLEFVGLSDKKDQFP-----------DELSGGQKQRVAIARALVTNPKIL 162
Cdd:TIGR01193 559 ifSGSILEN----LLLGAKENVSQ-DEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 163 LCDEATSALDPATTASILTLLKNVNQTfgiTIMMITHEMRVIKDIcNRVAVMEKGQVVETGTVKEV 228
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDEL 695
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
1.79e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 102.89 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDK----- 75
Cdd:COG4559 1 MLEAENLSVRLGGR--TL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 76 --MMRdikkdigmifQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:COG4559 77 raVLP----------QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 154 ALV-------TNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHemrvikDI------CNRVAVMEKGQVV 220
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLH------DLnlaaqyADRILLLHQGRLV 219
|
250
....*....|
gi 493203783 221 ETGTVKEVFS 230
Cdd:COG4559 220 AQGTPEEVLT 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-223 |
2.15e-25 |
|
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: 101.96 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 3 EFRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLV-----RLVNHleAASNGQVIVDGhdiMNYSDKMM 77
Cdd:cd03234 5 PWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILFNG---QPRKPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 RDIkkdIGMIFQHFNLLNSATVFKNVAMPLILS---KKSKTEIKQRV-TEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:cd03234 80 QKC---VAYVRQDDILLPGLTVRETLTYTAILRlprKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 154 ALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMItHEMRV-IKDICNRVAVMEKGQVVETG 223
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI-HQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-227 |
3.50e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 106.28 E-value: 3.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 11 FHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAAS---NGQVIVDGHDImnySDKMMRDIKkdiGMI 87
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAIS---AYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 88 FQHFNLLNSATVFKN------VAMPLILSKKSKteiKQRVTEMLEFVGLSDKKD---QFPDE---LSGGQKQRVAIARAL 155
Cdd:TIGR00955 105 QQDDLFIPTLTVREHlmfqahLRMPRRVTKKEK---RERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 156 VTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKE 227
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-224 |
4.32e-25 |
|
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: 106.64 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdIKKDIGMIFQHFNLLNSATV 99
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA----VRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493203783 180 LTLLknVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGT 224
Cdd:TIGR01257 1101 WDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-230 |
6.80e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.24 E-value: 6.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 15 KQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDkmmRDIKKDIGMIFQHFNLL 94
Cdd:PRK11231 14 TKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQHHLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 95 NSATVFKNVAM---P-LILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK11231 89 EGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 171 LDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
1.36e-24 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 104.41 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtiDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdik 81
Cdd:PRK10790 341 IDIDNVSFAYRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKkskteikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:PRK10790 415 QGVAMVQQDPVVL-ADTFLANVTLGRDISE-------EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 151 IARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfgITIMMITHEMRVIKDiCNRVAVMEKGQVVETGT 224
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-214 |
1.54e-24 |
|
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: 103.91 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhkkKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDik 81
Cdd:TIGR02857 322 LEFSGVSVAY---PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kDIGMIFQHFNLLNsATVFKNVAmpLILSKKSKTEIKQ--RVTEMLEFV-----GLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:TIGR02857 397 -QIAWVPQHPFLFA-GTIAENIR--LARPDASDAEIREalERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEmRVIKDICNRVAVM 214
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-230 |
2.18e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.08 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 16 QTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhDIMNYSDKMMRDIKKDIGMIFQH----- 90
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRGLLALRQQVATVFQDpeqqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 91 -FNLLNSATVF--KNVAMPlilskksKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:PRK13638 91 fYTDIDSDIAFslRNLGVP-------EAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 168 TSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-230 |
1.03e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.13 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 36 VIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrDIKKDIGMIFQHFNLLNSATVFKNVA------MPLIl 109
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---EVARRIGLLAQNATTPGDITVQELVArgryphQPLF- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 110 sKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQT 189
Cdd:PRK10253 114 -TRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493203783 190 FGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK10253 193 KGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
12-228 |
2.17e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.17 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 12 HKKKQTIDALKDVSFTVNHNDIF-------------GVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMr 78
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 diKKDIGMIFQHFNLLNSATVFKNVAM---PL--ILSKKSKTEiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:PRK10575 84 --ARKVAYLPQQLPAAEGMTVRELVAIgryPWhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 154 ALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
3.45e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 100.13 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIkkdIGMIFQHFNLLnSATV 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQDAHLF-DTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNvampLILSKKSKTEikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:TIGR02868 426 REN----LRLARPDATD--EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|.
gi 493203783 169 SALDPATTASILTLLKNVNQtfGITIMMITH 199
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
9.45e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 9.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 4 FRQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDghdimnysdkmmRDIKkd 83
Cdd:COG0488 1 LENLSKSFGGR--PL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 84 IGMIFQHFNLLNSATVFKNVAMPL-----ILSKKSKTEIK---------------------------QRVTEMLEFVGLS 131
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVLDGDaelraLEAELEELEAKlaepdedlerlaelqeefealggweaeARAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 132 DKKDQFP-DELSGGQKQRVAIARALVTNPKILLCDEATSALDpatTASILTL---LKNvnqtFGITIMMITHEMRVIKDI 207
Cdd:COG0488 143 EEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLeefLKN----YPGTVLVVSHDRYFLDRV 215
|
250
....*....|..
gi 493203783 208 CNRVAVMEKGQV 219
Cdd:COG0488 216 ATRILELDRGKL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-223 |
1.73e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.81 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFhkkkQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdi 80
Cdd:PRK15439 11 LLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAmpLILSKKSKTeiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK15439 85 QLGIYLVPQEPLLFPNLSVKENIL--FGLPKRQAS--MQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-224 |
1.76e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.66 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQV-----IVDGHDImnysdkmmrDIKKDIGMIFQHFNLL 94
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDI---------ATRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 95 NSATVFKNvampLILSKK----SKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:NF033858 352 GELTVRQN----LELHARlfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 171 LDPATTASILTLLKNVNQTFGITIMMITHEM----RvikdiCNRVAVMEKGQVVETGT 224
Cdd:NF033858 428 VDPVARDMFWRLLIELSREDGVTIFISTHFMneaeR-----CDRISLMHAGRVLASDT 480
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-221 |
1.92e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKkqTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVdGHDImnysdkmmrdi 80
Cdd:COG0488 315 VLELEGLSKSYGDK--TL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 kkDIGMIFQHFNLLN-SATVFKNVAmpLILSKKSKTEIKQRVTEMLeFVGlsDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG0488 379 --KIGYFDQHQEELDpDKTVLDELR--DGAPGGTEQEVRGYLGRFL-FSG--DDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 160 KILLCDEATSALDPATtasiLTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVE 221
Cdd:COG0488 452 NVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-251 |
2.54e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFhkKKQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDI 80
Cdd:PRK09536 3 MIDVSDLSVEF--GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS---ARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAM---PLILSKKSKTEIKQR-VTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK09536 76 SRRVASVPQDTSLSFEFDVRQVVEMgrtPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSHPktTI 236
Cdd:PRK09536 156 QATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD--TL 232
|
250
....*....|....*.
gi 493203783 237 AQNF-VSTVIQTEPST 251
Cdd:PRK09536 233 RAAFdARTAVGTDPAT 248
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-205 |
3.20e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRdikKDIGMIFQHFNLLNSaTVF 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---QQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAMPLILSKKSKTEikQRVTEMLEFVGLSDKKDQFP-DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK10247 99 DNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|....*.
gi 493203783 180 LTLLKNVNQTFGITIMMITHEMRVIK 205
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDEIN 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-222 |
5.12e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.52 E-value: 5.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 3 EFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDiMNYSDkmMRD-IK 81
Cdd:PRK11288 6 SFDGIGKTFPGVK----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-MRFAS--TTAaLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSATVFKNV---AMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK11288 79 AGVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVET 222
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
5-220 |
6.71e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 5 RQVSKSFHKKKQTIDA-------------LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGH--DI 69
Cdd:COG1129 239 RELEDLFPKRAAAPGEvvleveglsvggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 70 MNYSDKmmrdIKKDIGM---------IFQHFnllnsaTVFKNVAMPLI--LSKK---SKTEIKQRVTEMLEFVGL-SDKK 134
Cdd:COG1129 319 RSPRDA----IRAGIAYvpedrkgegLVLDL------SIRENITLASLdrLSRGgllDRRRERALAEEYIKRLRIkTPSP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 135 DQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVM 214
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVM 467
|
....*.
gi 493203783 215 EKGQVV 220
Cdd:COG1129 468 REGRIV 473
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-230 |
1.13e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 93.26 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhkKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKS----TLVRLVnHLEaasNGQVIVDGHDIMNYSdkmM 77
Cdd:PLN03130 1238 IKFEDVVLRY--RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIV-ELE---RGRILIDGCDISKFG---L 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 RDIKKDIGMIFQHfNLLNSATVFKNVAmPLilSKKSKTEIkqrvTEMLEFVGLSD--KKDQFP---------DELSGGQK 146
Cdd:PLN03130 1309 MDLRKVLGIIPQA-PVLFSGTVRFNLD-PF--NEHNDADL----WESLERAHLKDviRRNSLGldaevseagENFSVGQR 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 147 QRVAIARALVTNPKILLCDEATSALDPATTASIltlLKNVNQTF-GITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTV 225
Cdd:PLN03130 1381 QLLSLARALLRRSKILVLDEATAAVDVRTDALI---QKTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTP 1456
|
....*
gi 493203783 226 KEVFS 230
Cdd:PLN03130 1457 ENLLS 1461
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-230 |
5.61e-20 |
|
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: 91.16 E-value: 5.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhkkKQTID-ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhdiMNYSDKMMRDI 80
Cdd:TIGR00957 1285 VEFRNYCLRY---REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG---LNIAKIGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHfNLLNSATVFKNVAmPLilSKKSKTEI--KQRVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIAR 153
Cdd:TIGR00957 1359 RFKITIIPQD-PVLFSGSLRMNLD-PF--SQYSDEEVwwALELAHLKTFVsALPDKLDHECAEggenLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 154 ALVTNPKILLCDEATSALDPATTASILTLLKnvNQTFGITIMMITHEMRVIKDIcNRVAVMEKGQVVETGTVKEVFS 230
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-222 |
6.11e-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: 90.27 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVN--HLEAASNGQVIVDGHDIMNYSdkmMR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPLKASN---IR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSK----TEIKQRVTEMLEFVGLSDKKDQFP-DELSGGQKQRVAIA 152
Cdd:TIGR02633 74 DTeRAGIVIIHQELTLVPELSVAENIFLGNEITLPGGrmayNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVET 222
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-220 |
1.33e-19 |
|
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: 85.39 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 4 FRQVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLE--AASNGQVIVDGHDImnysdkmmrdi 80
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKaLANRTEgnVSVEGDIHYNGIPY----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 kKDIGMIFQHFNLLNSAtvfKNVAMPLILskkskteikqrVTEMLEFVgLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03233 75 -KEFAEKYPGEIIYVSE---EDVHFPTLT-----------VRETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRV-IKDICNRVAVMEKGQVV 220
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-221 |
1.39e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 3 EFRQVSKSFHKK--KQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVnhLEAASNGQV--IVDGHDIMNYSDKmmr 78
Cdd:COG2401 26 RVAIVLEAFGVElrVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLL--AGALKGTPVagCVDVPDNQFGREA--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 dikkdigmifqhfnllnsatvfknvamPLILSKKSKTEIKQrVTEMLEFVGLSD-----KKdqfPDELSGGQKQRVAIAR 153
Cdd:COG2401 101 ---------------------------SLIDAIGRKGDFKD-AVELLNAVGLSDavlwlRR---FKELSTGQKFRFRLAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 154 ALVTNPKILLCDEATSALDPaTTASILTL-LKNVNQTFGITIMMITHEMRVIKDIC-NRVAVMEKGQVVE 221
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDR-QTAKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
3.95e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.06 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVN--HLEAASNGQVIVDGHDIMNYSdkmMR 78
Cdd:PRK13549 5 LLEMKNITKTFGGVK----ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEGEELQASN---IR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKT---EIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:PRK13549 78 DTeRAGIAIIHQELALVKELSVLENIFLGNEITPGGIMdydAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVnQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVET 222
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-243 |
4.14e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 88.49 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIKKDIGMIFQHfNLLNSATVF 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQS-PVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAmPLilSKKSKTEIkqrvTEMLEFVGLSDKKDQFP-----------DELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PLN03232 1328 FNID-PF--SEHNDADL----WEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 170 ALDPATTASIltlLKNVNQTF-GITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFSHPKTTIAQNFVST 243
Cdd:PLN03232 1401 SVDVRTDSLI---QRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHST 1471
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-227 |
4.26e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.98 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 24 VSFTVNHNDIFGVIGYSGAGKSTLVrlvNHLE--AASNGQVIVDGHDImnySDKMMRDIKKDIGMIFQHFNLLNsATVFK 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIEL---RELDPESWRKHLSWVGQNPQLPH-GTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 102 NVAmpliLSKKSKTEikQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK11174 442 NVL----LGNPDASD--EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 171 LDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKE 227
Cdd:PRK11174 516 LDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-232 |
1.18e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 9 KSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIKKDIGMIF 88
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---TKLQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 89 QHfNLLNSATVFKNVAmpliLSKKSKTeiKQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVAIARALVT 157
Cdd:PRK10789 396 QT-PFLFSDTVANNIA----LGRPDAT--QQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 158 NPKILLCDEATSALDPATTASILTLLKNVNQtfGITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFSHP 232
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-231 |
1.26e-18 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 86.48 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIDALKD----------------VSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVivd 65
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDlffrskdgeyhyalnnISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 66 ghdimnysdkmmrDIKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQ 145
Cdd:PRK13545 82 -------------DIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 146 KQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTV 225
Cdd:PRK13545 149 KSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDI 227
|
....*.
gi 493203783 226 KEVFSH 231
Cdd:PRK13545 228 KEVVDH 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-230 |
1.32e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.16 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysDKMMRdiKKDIGMIFQH------FNL 93
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQ--KNLVAYVPQSeevdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 94 LNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDP 173
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 174 ATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNrVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
2.30e-18 |
|
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: 82.13 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTID-ALKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAaSNGQVIVDGHdimnysdkmmrd 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 ikkdIGMIFQHFNLLNsATVFKNVAMplilskkSKTEIKQRVTEMLEFVGLSDKKDQFPD-------E----LSGGQKQR 148
Cdd:cd03250 68 ----IAYVSQEPWIQN-GTIRENILF-------GKPFDEERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 149 VAIARALVTNPKILLCDEATSALDPATTASI-----LTLLKNvnqtfGITIMMITHEMRVIKDiCNRVAVMEKGQ 218
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN-----NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-199 |
2.57e-18 |
|
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: 81.05 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDimnysdkmmrdikkdiGMIFqhfnllnsatvf 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------------DLLF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 knvaMPlilskkskteikQRvtemlEFVGLSDKKDQ--FP--DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATT 176
Cdd:cd03223 69 ----LP------------QR-----PYLPLGTLREQliYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 493203783 177 ASILTLLKnvnqTFGITIMMITH 199
Cdd:cd03223 128 DRLYQLLK----ELGITVISVGH 146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-233 |
2.63e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.85 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGqvivdghdimnysdKMMRDI 80
Cdd:PRK09544 4 LVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------------VIKRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLlnSATVFKNVAMPLILSKKSKteiKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK09544 66 KLRIGYVPQKLYL--DTTLPLTVNRFLRLRPGTK---KEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMeKGQVVETGTVKEVFSHPK 233
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-199 |
4.65e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.86 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIV-DGHDIM-----NYsdkmmrdikkdigmifqhfnlL 94
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqrPY---------------------L 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 95 NSATVFKNVAMPLILSKKSKTEIKqrvtEMLEFVGLSDKKDQFPDE------LSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:COG4178 438 PLGTLREALLYPATAEAFSDAELR----EALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|.
gi 493203783 169 SALDPATTASILTLLKnvNQTFGITIMMITH 199
Cdd:COG4178 514 SALDEENEAALYQLLR--EELPGTTVISVGH 542
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
8.27e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhdimnysdkmmrdik 81
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdiGMIFQHFnllnsatvfknvamplilskkskteikqrvtemlefvglsdkkdqfpDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03221 62 ---TVKIGYF-----------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 162 LLCDEATSALDPATtasiLTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVMEKGQ 218
Cdd:cd03221 92 LLLDEPTNHLDLES----IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-219 |
9.40e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 22 KDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmrdIKKDIGMIF-----QHFNLLNS 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA----QRLARGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 97 ATVFKNVA------MPLILSKKSKTEIKQRVTEMLEfVGLSDKkDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK15439 356 APLAWNVCalthnrRGFWIKPARENAVLERYRRALN-IKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493203783 171 LDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-264 |
1.02e-17 |
|
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: 84.58 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLeAASNGQVIVDGhdiMNYSDKMMRDIKKDIGMIFQHFNLLnSATVF 100
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG---VSWNSVTLQTWRKAFGVIPQKVFIF-SGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAmPLilSKKSKTEIkQRVTEMlefVGLSDKKDQFPDEL-----------SGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:TIGR01271 1310 KNLD-PY--EQWSDEEI-WKVAEE---VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 170 ALDPATTASILTLLKnvnQTFG-ITIMMITHEMRVIKDiCNRVAVMEKGQV----------VETGTVKEVFSHP---KTT 235
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLK---QSFSnCTVILSEHRVEALLE-CQQFLVIEGSSVkqydsiqkllNETSLFKQAMSAAdrlKLF 1458
|
250 260
....*....|....*....|....*....
gi 493203783 236 IAQNFVSTVIQTEPSTSLIRRLNDEQVGD 264
Cdd:TIGR01271 1459 PLHRRNSSKRKPQPKITALREEAEEEVQN 1487
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-239 |
2.03e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.54 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQtIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIV-DGHDIMN--------- 71
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDinlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 72 ----------YSDKMMRDIK------KDIGMIFQHF-----------NLLNSATVFKNVAMPLILSKKSKTEIKQ----- 119
Cdd:PTZ00265 462 igvvsqdpllFSNSIKNNIKyslyslKDLEALSNYYnedgndsqenkNKRNSCRAKCAGDLNDMSNTTDSNELIEmrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 120 RVTEMLEFVGLSDKK------DQFPDE-----------LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTL 182
Cdd:PTZ00265 542 QTIKDSEVVDVSKKVlihdfvSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 183 LKNVNQTFGITIMMITHEMRVIKdICNRVAVMEKGQVVETGTVKEVFSHPKTTIAQN 239
Cdd:PTZ00265 622 INNLKGNENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDPTKDNKEN 677
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-219 |
2.87e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDK---------MMRDIKKD---IGMif 88
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyISEDRKRDglvLGM-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 89 qhfnllnsaTVFKNVAMPLI--LSKKS-KTEIKQRVTEMLEFVGLSDKK----DQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK10762 346 ---------SVKENMSLTALryFSRAGgSLKHADEQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 162 LLCDEATSALDPATTASILTLlknVNQtF---GITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQL---INQ-FkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-231 |
1.92e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 77.93 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 13 KKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGhdimnysdkmmrdikkDIGMIFQHFN 92
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 93 LLNSATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PRK13546 96 LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 173 PATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFSH 231
Cdd:PRK13546 176 QTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-230 |
3.33e-16 |
|
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: 77.59 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTL----VRLVNhleaaSNGQVIVDGhdiMNYSDKMMRDIKKDIGMIFQHFNLLnS 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDG---VSWNSVPLQKWRKAFGVIPQKVFIF-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 97 ATVFKNvampLILSKKSKTEIKQRVTEMlefVGLSDKKDQFPDEL-----------SGGQKQRVAIARALVTNPKILLCD 165
Cdd:cd03289 91 GTFRKN----LDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 166 EATSALDPATTASILTLLKnvnQTF-GITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFS 230
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLK---QAFaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLN 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-258 |
3.61e-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: 80.06 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 28 VNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNysdkMMRDIKKDIGMIFQHFNLLNSATVFKNVAMPL 107
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQFDAIDDLLTGREHLYLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 108 ILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVN 187
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 188 QTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKevfsHPKTTIAQNFVSTVIQTEPSTSLIRRLN 258
Cdd:TIGR01257 2118 RE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ----HLKSKFGDGYIVTMKIKSPKDDLLPDLN 2183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-221 |
3.64e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 22 KDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDkmMRDIKKDIGMI---------FQHFN 92
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAYItesrrdngfFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 93 LLNSATVFKNV-------AMPLILSKKS-KTEIKQRVTEMLEFVGLsdkkDQFPDELSGGQKQRVAIARALVTNPKILLC 164
Cdd:PRK09700 358 IAQNMAISRSLkdggykgAMGLFHEVDEqRTAENQRELLALKCHSV----NQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 165 DEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVE 221
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-228 |
5.35e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.26 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEA--ASNGQVIVDGHDIMNYSdkMMRDIKKDIGMIFQHfnllnsat 98
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLP--PEERARLGIFLAFQY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 99 vfkNVAMPLIlskkskteikqRVTEMLEFVGLSdkkdqfpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDpattAS 178
Cdd:cd03217 86 ---PPEIPGV-----------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD----ID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493203783 179 ILTLLKNVNQTF---GITIMMITHEMRVIKDI-CNRVAVMEKGQVVETGTVKEV 228
Cdd:cd03217 139 ALRLVAEVINKLreeGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELA 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-183 |
6.00e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDI--------MNYsdkmmrdikkdIGmifqHFN 92
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIddpdvaeaCHY-----------LG----HRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 93 LLNSA-TVFKNvampLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSAL 171
Cdd:PRK13539 83 AMKPAlTVAEN----LEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|..
gi 493203783 172 DPATTASILTLL 183
Cdd:PRK13539 159 DAAAVALFAELI 170
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-222 |
1.13e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.52 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVN--HLEAASNGQVIVDGhDIMNYSDkmMR 78
Cdd:NF040905 1 ILEMRGITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvYPHGSYEGEILFDG-EVCRFKD--IR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 79 DI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKK---SKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:NF040905 74 DSeALGIVIIHQELALIPYLSIAENIFLGNERAKRgviDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 155 LVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVET 222
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-228 |
1.90e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 19 DALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIkkdiGMIF-----QHFNL 93
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRL----GVAYipedrLGRGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 94 LNSATVFKNVAM------PL----ILSKKsktEIKQRVTEMLEfvglsdkkdQF----PDE------LSGGQKQRVAIAR 153
Cdd:COG3845 348 VPDMSVAENLILgryrrpPFsrggFLDRK---AIRAFAEELIE---------EFdvrtPGPdtparsLSGGNQQKVILAR 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 154 ALVTNPKILLCDEATSALDPATTASILTLLKNV-NQtfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrDA--GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-227 |
1.99e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDi 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 kKDIGMIFQHFNLLNSATVFKNV--------AMPLILSKKskteIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:PRK10762 79 -AGIGIIHQELNLIPQLTIAENIflgrefvnRFGRIDWKK----MYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 153 RALVTNPKILLCDEATSALDPATTASILTLLKNVnQTFGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKE 227
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-219 |
2.60e-15 |
|
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: 76.40 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSkSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAASNGQVIVDGH--DIMNYSDKmm 77
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKpvDIRNPAQA-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 78 rdIKKDIGMI---FQHFNLLNSATVFKNVAMPLILSKKSKTEIKQRVTE--MLEFVGLSDKKDQFPD----ELSGGQKQR 148
Cdd:TIGR02633 334 --IRAGIAMVpedRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPFlpigRLSGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 149 VAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-205 |
3.25e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 76.99 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 58 SNGQVIVDGHDIMNYSdkmMRDIKKDIGMIFQHFNLLNsATVFKNVAMPLILSKKSKTEIKQRVTEMLEFV-GLSDKKDQ 136
Cdd:PTZ00265 1275 NSGKILLDGVDICDYN---LKDLRNLFSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAIDEFIeSLPNKYDT 1350
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 137 ----FPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIK 205
Cdd:PTZ00265 1351 nvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-230 |
3.25e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLvrlvnhLEAAS-----NGQVIVDGHDIMNYSdkmMRDIKKDIGMIFQHfnlln 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL------LARMAgllpgQGEILLNGRPLSDWS---AAELARHRAYLSQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 96 SATVFknvAMP----LIL---SKKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV-----TNP--KI 161
Cdd:COG4138 78 QSPPF---AMPvfqyLALhqpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHemrvikDI------CNRVAVMEKGQVVETGTVKEVFS 230
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSH------DLnhtlrhADRVWLLKQGKLVASGETAEVMT 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-227 |
9.32e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.77 E-value: 9.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 7 VSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmmRDIKKDIGM 86
Cdd:PRK10982 4 ISKSFPGVK----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK--EALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 87 IFQHFNLLNSATVFKNVAM-------PLILSKKSKTEIKQRVTEMLEFVglsDKKDQFPDeLSGGQKQRVAIARALVTNP 159
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLgryptkgMFVDQDKMYRDTKAIFDELDIDI---DPRAKVAT-LSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKE 227
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAG 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-199 |
9.44e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.01 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 24 VSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKKdIGmifqHFNLLNSA-TVFKN 102
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILY-LG----HLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 103 VA-MPLILSKKSKTeikqrVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILT 181
Cdd:TIGR01189 94 LHfWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAG 168
|
170
....*....|....*...
gi 493203783 182 LLKNVNQTFGITIMMiTH 199
Cdd:TIGR01189 169 LLRAHLARGGIVLLT-TH 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-231 |
1.56e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSksFHKKKQTIdALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRDIK 81
Cdd:PRK10522 323 LELRNVT--FAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFNLLNSatvfknvamplILSKKSKTEIKQRVTEMLEFVGLSDKKD----QFPD-ELSGGQKQRVAIARALV 156
Cdd:PRK10522 397 KLFSAVFTDFHLFDQ-----------LLGPEGKPANPALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 157 TNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIkDICNRVAVMEKGQVVE-TGTVKEVFSH 231
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-219 |
1.52e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 12 HKKKqtidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAASNGQVIVDGH--DIMNYSDKmmrdIKKDIGMI- 87
Cdd:PRK13549 274 HIKR-----VDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKpvKIRNPQQA----IAQGIAMVp 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 88 --FQHFNLLNSATVFKNVAMPLI--LSKKSKTEIKQRVTEMLEFVGLSDKKDQFPD----ELSGGQKQRVAIARALVTNP 159
Cdd:PRK13549 345 edRKRDGIVPVMGVGKNITLAALdrFTGGSRIDDAAELKTILESIQRLKVKTASPElaiaRLSGGNQQKAVLAKCLLLNP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 160 KILLCDEATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:PRK13549 425 KILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-228 |
1.56e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 24 VSFTVNHNDIFGVIGYSGAGKSTLV-RLVNHLEAAsnGQVIVDGHDIMNYSdkmMRDIKKDIGMIFQHfnllnSATVFkn 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLLPGS--GSIQFAGQPLEAWS---AAELARHRAYLSQQ-----QTPPF-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 103 vAMP----LILSKKSKTEIKQ---RVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARAL-----VTNP--KILLCDEAT 168
Cdd:PRK03695 83 -AMPvfqyLTLHQPDKTRTEAvasALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 169 SALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-200 |
2.27e-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: 70.73 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhKKKQTIDalkDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKmMRDik 81
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLID---DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ-SRD-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 kdigmifqhfNLLNSATVFKNVAMPLILSKKSKTEIKQRVtemleFVGLSDKK--DQ--FPDELSGGQKQRVAIARALVT 157
Cdd:TIGR03719 396 ----------ALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKgsDQqkKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493203783 158 NPKILLCDEATSALDPATtasiLTLLKNVNQTFGITIMMITHE 200
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHD 499
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-199 |
2.86e-13 |
|
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: 67.52 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 24 VSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIkkdigMIFQHFNLLNSA-TVFKN 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-----LYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 103 VAMPLILSKKSKTEikqrvtEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTL 182
Cdd:cd03231 94 LRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*..
gi 493203783 183 LKNVNQTFGItIMMITH 199
Cdd:cd03231 168 MAGHCARGGM-VVLTTH 183
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-228 |
3.11e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.96 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmMRDIKKDIGMIFQHfNLLNSATVF 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQD-PVLFDGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAmPliLSKKSKTEikqrVTEMLEFVGL-------SDKKDQFPDE----LSGGQKQRVAIARALVT-NPKILLCDEAT 168
Cdd:PTZ00243 1402 QNVD-P--FLEASSAE----VWAALELVGLrervaseSEGIDSRVLEggsnYSVGQRQLMCMARALLKkGSGFILMDEAT 1474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 169 SALDPATTASILTllkNVNQTF-GITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEV 228
Cdd:PTZ00243 1475 ANIDPALDRQIQA---TVMSAFsAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPREL 1531
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-255 |
6.83e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 6.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 4 FRQVSKSFHKKKQTIdaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLV----NHLEAASNGQVIVDGHDimnySDKMMRD 79
Cdd:TIGR00956 62 FRKLKKFRDTKTFDI--LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGIT----PEEIKKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQ---HFNLLNSATVFKNVAM-------PLILSKKskTEIKQRVTEMLEFVGLSDKKD-----QFPDELSGG 144
Cdd:TIGR00956 136 YRGDVVYNAEtdvHFPHLTVGETLDFAARcktpqnrPDGVSRE--EYAKHIADVYMATYGLSHTRNtkvgnDFVRGVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKN----VNQTFGITIMMITHEmrvIKDICNRVAVMEKGQVV 220
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTsaniLDTTPLVAIYQCSQD---AYELFDKVIVLYEGYQI 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 493203783 221 ETGT---VKEVFS------HPKTTIAqNFVSTViqTEPSTSLIR 255
Cdd:TIGR00956 291 YFGPadkAKQYFEkmgfkcPDRQTTA-DFLTSL--TSPAERQIK 331
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-220 |
1.15e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.82 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNysdKMMRDIKKDIgmifqhfnllnSATVF 100
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA---RLQQDPPRNV-----------EGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVA----------------MPLILSKKSKTEIKQ------------------RVTEMLEFVGLSdkkdqfPD----ELS 142
Cdd:PRK11147 85 DFVAegieeqaeylkryhdiSHLVETDPSEKNLNElaklqeqldhhnlwqlenRINEVLAQLGLD------PDaalsSLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 143 GGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNvnqtFGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-200 |
6.67e-12 |
|
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: 66.11 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 7 VSKSFHKKKQTidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVivdghdimnysdKMMRDIKkdIGM 86
Cdd:TIGR03719 10 VSKVVPPKKEI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA------------RPQPGIK--VGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 87 IFQHFNLLNSATVFKNVAMPLilskkskTEIKQRVTEMLE-FVGLSDKKDQF---------------------------- 137
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEEGV-------AEIKDALDRFNEiSAKYAEPDADFdklaaeqaelqeiidaadawdldsqlei 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 138 -------PD------ELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAsiltLLKNVNQTFGITIMMITHE 200
Cdd:TIGR03719 146 amdalrcPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA----WLERHLQEYPGTVVAVTHD 217
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
264-340 |
3.01e-11 |
|
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: 58.68 E-value: 3.01e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 264 DFKDYKIFVEETQVTQPIINDLIQICGREVKILFSSMSEIQGNTVCYMWLRFNIDQQFDDTAInQYFKEKNIQFEEV 340
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAAL-AYLREQGVEVEVL 76
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-215 |
4.49e-11 |
|
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: 62.04 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 27 TVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImNYSDKMmrdIKKDIGMIFQHFnlLNSATvfknvamp 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQY---IKADYEGTVRDL--LSSIT-------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 107 lilskKSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDP----ATTASILTL 182
Cdd:cd03237 87 -----KDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRF 161
|
170 180 190
....*....|....*....|....*....|...
gi 493203783 183 LKNVNQtfgiTIMMITHEMRVIKDICNRVAVME 215
Cdd:cd03237 162 AENNEK----TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
113-228 |
6.71e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 113 SKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTfGI 192
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GA 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 493203783 193 TIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEV 228
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-225 |
7.51e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 9 KSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAAS--NGQVIVDGHDImNYSDKMMRDiKKDIGM 86
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESI-LDLEPEERA-HLGIFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 87 IFQH-----------FNLL--NSATVFKNvampliLSKKSKTEIKQRVTEMLEFVGLSDK------KDQFpdelSGGQKQ 147
Cdd:CHL00131 89 AFQYpieipgvsnadFLRLayNSKRKFQG------LPELDPLEFLEIINEKLKLVGMDPSflsrnvNEGF----SGGEKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 148 RVAIARALVTNPKILLCDEATSALDP---ATTASILTLLKNVNQtfgiTIMMITHEMRVIKDIC-NRVAVMEKGQVVETG 223
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
|
..
gi 493203783 224 TV 225
Cdd:CHL00131 235 DA 236
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-220 |
7.69e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 24 VSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDK------MM---RDIKKDiGMIFQHfnll 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdairagIMlcpEDRKAE-GIIPVH---- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 95 nsaTVFKNVAMP---------LILSKKSKTEIKQRVTEMLEFVGLSdkKDQFPDELSGGQKQRVAIARALVTNPKILLCD 165
Cdd:PRK11288 347 ---SVADNINISarrhhlragCLINNRWEAENADRFIRSLNIKTPS--REQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 166 EATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVV 220
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-243 |
1.07e-10 |
|
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: 61.08 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTL----VRLVNHLEaasnGQVIVDGHDImnySDKMMRDIKKDIGMIFQHfNLLNS 96
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDI---SKLPLHTLRSRLSIILQD-PILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 97 ATVFKNVamplilsKKSKTEIKQRVTEMLEFVGLSDKKDQFP-----------DELSGGQKQRVAIARALVTNPKILLCD 165
Cdd:cd03288 109 GSIRFNL-------DPECKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 166 EATSALDPATTAsilTLLKNVNQTFG-ITIMMITHEMRVIKDiCNRVAVMEKGQVVETGTVKEVFSHpKTTIAQNFVST 243
Cdd:cd03288 182 EATASIDMATEN---ILQKVVMTAFAdRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ-EDGVFASLVRT 255
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-199 |
1.14e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFhKKKQTIDalkDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVdGHDI-MNYSDKmMRDi 80
Cdd:PRK11819 325 IEAENLSKSF-GDRLLID---DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVkLAYVDQ-SRD- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 kkdigmifqhfNLLNSATVFKNVAMPLILSKKSKTEIKQRVtemleFVGLSDKK--DQ--FPDELSGGQKQRVAIARALV 156
Cdd:PRK11819 398 -----------ALDPNKTVWEEISGGLDIIKVGNREIPSRA-----YVGRFNFKggDQqkKVGVLSGGERNRLHLAKTLK 461
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493203783 157 TNPKILLCDEATSALDPATtasiLTLLKNVNQTFGITIMMITH 199
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISH 500
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-200 |
2.60e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 32 DIFGVIGYSGAGKSTLVR-LVNHLEAAS-NGQVIVDGHdimnysdKMMRDIKKDIGMIFQHFNLLNSATVFKNVA----- 104
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNR-------KPTKQILKRTGFVTQDDILYPHLTVRETLVfcsll 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 105 -MPLILSKKSKTEIKQRVTEMLefvGLSDKKD-----QFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAS 178
Cdd:PLN03211 168 rLPKSLTKQEKILVAESVISEL---GLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180
....*....|....*....|..
gi 493203783 179 ILTLLKNVNQTfGITIMMITHE 200
Cdd:PLN03211 245 LVLTLGSLAQK-GKTIVTSMHQ 265
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-236 |
3.05e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 14 KKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVrlvNHLEAASNGQVIVDGHDIMNYSdKMMRDIKKDIGMIFQHFNL 93
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRLVNGR-PLDSSFQRSIGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 94 LNSATVFKNVA------MPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFPDE-LSGGQKQRVAIARALVTNPKILL-CD 165
Cdd:TIGR00956 848 LPTSTVRESLRfsaylrQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLD 927
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 166 EATSALDPATTASILTLLKNVNQTfGITIMMITHE-MRVIKDICNRVAVMEKG-QVVETGTVKEvfsHPKTTI 236
Cdd:TIGR00956 928 EPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQpSAILFEEFDRLLLLQKGgQTVYFGDLGE---NSHTII 996
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-173 |
4.93e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKqtidALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLV--NHLEAASNgQVIVDGHdiMNYSDKMMRD 79
Cdd:PRK10938 261 IVLNNGVVSYNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgDHPQGYSN-DLTLFGR--RRGSGETIWD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 80 IKKDIGMIFQ--HFNLLNSATVfKNVamplILS---------KKSKTEIKQRVTEMLEFVGLSDKKDQFP-DELSGGQKQ 147
Cdd:PRK10938 334 IKKHIGYVSSslHLDYRVSTSV-RNV----ILSgffdsigiyQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQR 408
|
170 180
....*....|....*....|....*.
gi 493203783 148 RVAIARALVTNPKILLCDEATSALDP 173
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-222 |
5.22e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.51 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDG--------HDIMNYSDKMMRDIKKDIGmIFQH- 90
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnhnaNEAINHGFALVTEERRSTG-IYAYl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 91 ---FN-LLNSATVFKNvAMPLILSKKSKTEIKQRVTEMLefVGLSDKKDQFpDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:PRK10982 342 digFNsLISNIRNYKN-KVGLLDNSRMKSDTQWVIDSMR--VKTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 167 ATSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQV---VET 222
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVagiVDT 475
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-173 |
1.31e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnySDKMMRD-IKKDIGMIFQHF--NLLNS 96
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM---ADARHRRaVCPRIAYMPQGLgkNLYPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 97 ATVFKNVAMPLILSKKSKTEIKQRVTEMLEFVGLsdkkDQFPD----ELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:NF033858 93 LSVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
.
gi 493203783 173 P 173
Cdd:NF033858 169 P 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-199 |
2.12e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 7 VSKSFHKKKQTidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVdghdimnysdkmMRDIKkdIGM 86
Cdd:PRK11819 12 VSKVVPPKKQI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------------APGIK--VGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 87 IFQHFNLLNSATVFKNVAMPLilskKSKTEIKQRVTE-MLEFVGLSDKKDQFPDE------------------------- 140
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEEGV----AEVKAALDRFNEiYAAYAEPDADFDALAAEqgelqeiidaadawdldsqleiamd 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 141 -------------LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAsiltLLKNVNQTFGITIMMITH 199
Cdd:PRK11819 151 alrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVA----WLEQFLHDYPGTVVAVTH 218
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-204 |
3.00e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 23 DVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIkkdigMIFQHFNLLNSA-TVFK 101
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL-----LYLGHQPGIKTElTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 102 NVAMPLILSKKSKTEikqRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILT 181
Cdd:PRK13538 94 NLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170 180
....*....|....*....|...
gi 493203783 182 LLKNVNQTFGITIMMITHEMRVI 204
Cdd:PRK13538 171 LLAQHAEQGGMVILTTHQDLPVA 193
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
6.85e-09 |
|
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: 53.92 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 30 HNDIFGVIGYSGAGKSTLVR-LVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKKDIGMIfqhfnllnsatvfknvampli 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 109 lskkskteikqrvtemlefvglsdkkdqfpdELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL-----TLL 183
Cdd:smart00382 60 -------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLL 108
|
170 180
....*....|....*....|...
gi 493203783 184 KNVNQTFGITIMMITHEMRVIKD 206
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP 131
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-172 |
1.96e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.29 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 33 IFGVIGYSGAGKSTLVRLV--------NHLEAASNGQVIVD---GHDIMNYSDKMmRDIKKDIGMIFQHFNLLNSAtvFK 101
Cdd:cd03236 28 VLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDefrGSELQNYFTKL-LEGDVKVIVKPQYVDLIPKA--VK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 102 NVAMpLILSKKSKTEIKQRVTEMLEFVGLSDKKdqfPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:cd03236 105 GKVG-ELLKKKDERGKLDELVDQLELRHVLDRN---IDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
139-205 |
2.13e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.53 E-value: 2.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493203783 139 DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNvnqtFGITIMMITHEMRVIK 205
Cdd:TIGR00954 581 DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE----FGITLFSVSHRKSLWK 643
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
268-339 |
2.69e-08 |
|
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: 50.14 E-value: 2.69e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493203783 268 YKIFVEETQVTQPIINDLIQICGREVKILFSSMSEIQGNTVCYMWLRFNIDQQFDDTAInQYFKEKNIQFEE 339
Cdd:pfam09383 3 VRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAAL-AYLREQGVEVEV 73
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-230 |
2.83e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 25 SFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAASnGQVIVDGHDIMNYSdkmMRDIKKDIGMIFQHFN--LLNSATV-F 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARaLAGELPLLS-GERQSQFSHITRLS---FEQLQKLVSDEWQRNNtdMLSPGEDdT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAMPLILSKKSKTEIKQRVTEMLEFVGLSDKKDQFpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL 180
Cdd:PRK10938 99 GRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493203783 181 TLLKNVNQTfGITIMMITHEMRVIKDICNRVAVMEKGQVVETGTVKEVFS 230
Cdd:PRK10938 176 ELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-173 |
3.09e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 26 FTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNySDKM--------MRDIKKDIGMIfQHFNLLNSA 97
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSrfmaylghLPGLKADLSTL-ENLHFLCGL 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 98 TVFKNVAMPlilskkskteikqrvTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDP 173
Cdd:PRK13543 110 HGRRAKQMP---------------GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-229 |
9.66e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 9.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 15 KQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAASNGQVIVDGHdiMNYSDKmmrdikkdIGMIFqhfnl 93
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS--VAYVPQ--------VSWIF----- 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 94 lnSATVFKNVAMplilskKSKTEiKQRVTEMLEFVGLSDKKDQFPDE-----------LSGGQKQRVAIARALVTNPKIL 162
Cdd:PLN03232 692 --NATVRENILF------GSDFE-SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 163 LCDEATSALDPATTASIL-TLLKNVNQtfGITIMMITHEMRVIKDIcNRVAVMEKGQVVETGTVKEVF 229
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
141-229 |
1.36e-07 |
|
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: 53.41 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILT-------LLKNVnqtfgiTIMMITHEMRVIKDIcNRVAV 213
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLKNK------TRILVTHGISYLPQV-DVIIV 833
|
90
....*....|....*.
gi 493203783 214 MEKGQVVETGTVKEVF 229
Cdd:TIGR00957 834 MSGGKISEMGSYQELL 849
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-215 |
3.42e-07 |
|
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: 51.71 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 2 IEFRQVSKSFHKKKQTIDAlkdvsFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDghdiMNYSDKMMRdIK 81
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEG-----GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYKPQY-IS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQhfnllnsaTVFKNVAMPLILSKKSKTEIKQRVtemlefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:COG1245 412 PDYDGTVE--------EFLRSANTDDFGSSYYKTEIIKPL-------GLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493203783 162 LLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAVME 215
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
141-228 |
5.59e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIARAL---------VTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRV 211
Cdd:PRK13547 146 LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI 225
|
90
....*....|....*..
gi 493203783 212 AVMEKGQVVETGTVKEV 228
Cdd:PRK13547 226 AMLADGAIVAHGAPADV 242
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-202 |
6.56e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 49.64 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 6 QVSKSFHKKKQTIDALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSDKMMRDIKK-DI 84
Cdd:cd03290 2 QVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 85 GMIFQHFNLLNsATVFKNVAMPLILSKkskteikQRVTEMLEFVGLSDKKDQFP--DE---------LSGGQKQRVAIAR 153
Cdd:cd03290 82 AYAAQKPWLLN-ATVEENITFGSPFNK-------QRYKAVTDACSLQPDIDLLPfgDQteigerginLSGGQRQRICVAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493203783 154 ALVTNPKILLCDEATSALDPATT-----ASILTLLKNVNQtfgiTIMMITHEMR 202
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKLQ 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
9.10e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.79 E-value: 9.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDImnysDKMMRDIKKDIGMIFQHFNLLNSATVF 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 101 KNVAMPLILSKKSkteikQRVTEMLEFVGLSDKKDqFP-DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK13540 93 ENCLYDIHFSPGA-----VGITELCRLFSLEHLID-YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|.
gi 493203783 180 LTLLKNvNQTFGITIMMITHE 200
Cdd:PRK13540 167 ITKIQE-HRAKGGAVLLTSHQ 186
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-223 |
4.29e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVR-LVNHLEAaSNGQVIVDghdimnysdkmmrdikKDIGMIFQHFNLLNsATV 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEGRVWAE----------------RSIAYVPQQAWIMN-ATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 100 FKNVampLILSKKSKTEIKQ--RVTEMLEFV-----GLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PTZ00243 738 RGNI---LFFDEEDAARLADavRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493203783 173 PATTASIltllknVNQTF-----GITIMMITHEMRVIKdICNRVAVMEKGQVVETG 223
Cdd:PTZ00243 815 AHVGERV------VEECFlgalaGKTRVLATHQVHVVP-RADYVVALGDGRVEFSG 863
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-205 |
5.68e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 20 ALKDVSFTVNHNDIFGVIGYSGAGKSTLV----------RLVNHLEAASNGQVIVdghdimnySDKMMRDIKKDIGMifq 89
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVneglyasgkaRLISFLPKFSRNKLIF--------IDQLQFLIDVGLGY--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 90 hfnllnsatvfknvampLILSKKSKTeikqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPK--ILLCDEA 167
Cdd:cd03238 79 -----------------LTLGQKLST-------------------------LSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190
....*....|....*....|....*....|....*...
gi 493203783 168 TSALDPATTASILTLLKNVNQTfGITIMMITHEMRVIK 205
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLS 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-219 |
1.04e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 22 KDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVivdghdimnysdkmMRDIKKDIGMIFQH----FNLLNSA 97
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHhvdgLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 98 TVFKNVAMPLILskkskteiKQRVTEMLEFVGLSDKKDQFPD-ELSGGQKQRVAIARALVTNPKILLCDEATSALD-PAT 175
Cdd:PLN03073 592 LLYMMRCFPGVP--------EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAV 663
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493203783 176 TASILTLLknvnqTFGITIMMITHEMRVIKDICNRVAVMEKGQV 219
Cdd:PLN03073 664 EALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-215 |
1.12e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 27 TVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDghdiMNYSDKMMRdIKKDIGMIFQHFnlLNSATvfknvamP 106
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYKPQY-IKPDYDGTVEDL--LRSIT-------D 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 107 LILSKKSKTEIKQRVtemlefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNV 186
Cdd:PRK13409 427 DLGSSYYKSEIIKPL-------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180
....*....|....*....|....*....
gi 493203783 187 NQTFGITIMMITHEMRVIKDICNRVAVME 215
Cdd:PRK13409 500 AEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-172 |
1.98e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 35 GVIGYSGAGKSTLVR---------LVNHLEAASNGQVI--VDGHDIMNY----SDKMMRDIKKDigmifQHFNLLnsATV 99
Cdd:PRK13409 103 GILGPNGIGKTTAVKilsgelipnLGDYEEEPSWDEVLkrFRGTELQNYfkklYNGEIKVVHKP-----QYVDLI--PKV 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 100 FKNVAMPLIlskkSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PRK13409 176 FKGKVRELL----KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-172 |
1.99e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 19 DALKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNhLEA----ASNGQVI-----VDGHDIMNYSDKMMRDIKKDIGM--- 86
Cdd:PLN03073 191 DLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAidgiPKNCQILhveqeVVGDDTTALQCVLNTDIERTQLLeee 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 87 --IFQHFNLLNSATVFKNVAMPLILSKKsKTEIKQRVTEM---LEFV--------------GLS---DKKDQFPDELSGG 144
Cdd:PLN03073 270 aqLVAQQRELEFETETGKGKGANKDGVD-KDAVSQRLEEIykrLELIdaytaearaasilaGLSftpEMQVKATKTFSGG 348
|
170 180
....*....|....*....|....*...
gi 493203783 145 QKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PLN03073 349 WRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
134-235 |
2.11e-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: 44.49 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 134 KDQFPDeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGITIMMITHEMRVIKDICNRVAV 213
Cdd:cd03222 66 KPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
90 100
....*....|....*....|..
gi 493203783 214 MEkGQVVETGTvkevFSHPKTT 235
Cdd:cd03222 145 FE-GEPGVYGI----ASQPKGT 161
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-205 |
2.18e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 1 MIEFRQVSKSFHKKKqtidaLKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNYSdkmmrdi 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKN-----LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKTeikqrVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK13541 69 KPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493203783 161 ILLCDEATSALDPATTASILTLLKNVNQTFGItIMMITHEMRVIK 205
Cdd:PRK13541 144 LWLLDEVETNLSKENRDLLNNLIVMKANSGGI-VLLSSHLESSIK 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
141-220 |
2.38e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLlknVNQ--TFGITIMMITHEMRVIKDICNRVAVMEKGQ 218
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
..
gi 493203783 219 VV 220
Cdd:NF040905 482 IT 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
141-227 |
2.94e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL-TLLKNVNQtfGITIMMITHEMRVIKDIcNRVAVMEKGQV 219
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdKCIKDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
....*...
gi 493203783 220 VETGTVKE 227
Cdd:PLN03130 818 KEEGTYEE 825
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-221 |
3.46e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 21 LKDVSFTVNHNDIFGVIGYSGAGKSTLVRLVNHLEAASNGQVIVDGHDIMNY------------------SDKMMRDIKK 82
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWvnqetpalpqpaleyvidGDREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 83 DIgmifQHFNLLNSATvfknvAMPLILSKKSKTE---IKQRVTEMLEFVGLSDKKDQFP-DELSGGQKQRVAIARALVTN 158
Cdd:PRK10636 97 QL----HDANERNDGH-----AIATIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493203783 159 PKILLCDEATSALDPATTASILTLLKNVNQtfgiTIMMITHEMRVIKDICNRVAVMEKGQVVE 221
Cdd:PRK10636 168 SDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-172 |
1.18e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 43.62 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 33 IFGVIGYSGAGKSTLVR---------LVNHLEAASNGQVI--VDGHDIMNY----SDKMMRDIKKDigmifQHFNLLnsA 97
Cdd:COG1245 101 VTGILGPNGIGKSTALKilsgelkpnLGDYDEEPSWDEVLkrFRGTELQDYfkklANGEIKVAHKP-----QYVDLI--P 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493203783 98 TVFKNVAMPLIlskkSKTEIKQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:COG1245 174 KVFKGTVRELL----EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
125-223 |
1.91e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 125 LEFVGLSDKKDQF-PDEL----SGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKN-VNQTFGITIMMIT 198
Cdd:PLN03140 316 LKILGLDICKDTIvGDEMirgiSGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQiVHLTEATVLMSLL 395
|
90 100
....*....|....*....|....*
gi 493203783 199 HEMRVIKDICNRVAVMEKGQVVETG 223
Cdd:PLN03140 396 QPAPETFDLFDDIILLSEGQIVYQG 420
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-228 |
3.65e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIARAL---VTNPKILLCDEATSALDPATTASILTLLKN-VNQtfGITIMMITHEMRVIKdicnrVA---- 212
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRlVDK--GNTVVVIEHNLDVIK-----TAdyii 902
|
90 100
....*....|....*....|..
gi 493203783 213 ------VMEKGQVVETGTVKEV 228
Cdd:TIGR00630 903 dlgpegGDGGGTVVASGTPEEV 924
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
140-185 |
9.53e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.98 E-value: 9.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 493203783 140 ELSGGQKQR---VAIARALV----------TNPKILLCDEATSALDPATTASILTLLKN 185
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
140-217 |
1.95e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 1.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493203783 140 ELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILTLLKNVNQTFGItimmITHEMRVIKDICNRVAVMEKG 217
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMII----ISHDRHFLNSVCTHMADLDYG 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
9-210 |
3.52e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.97 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 9 KSFHKKkQTIDALKDvsftvnhndIFGVIGYSGAGKSTLvrlvnhLEAASngqVIVDGHDIMNYS-----DKMMR--DIK 81
Cdd:cd03240 10 RSFHER-SEIEFFSP---------LTLIVGQNGAGKTTI------IEALK---YALTGELPPNSKggahdPKLIRegEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 82 KDIGMIFQHFN-----LLNSATVFKNVAMplilskKSKTEIKQRVTEMLEFvglsdkkdqfpdeLSGGQKQ------RVA 150
Cdd:cd03240 71 AQVKLAFENANgkkytITRSLAILENVIF------CHQGESNWPLLDMRGR-------------CSGGEKVlasliiRLA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493203783 151 IARALVTNPKILLCDEATSALDPAT-TASILTLLKNVNQTFGITIMMITHE----------MRVIKDICNR 210
Cdd:cd03240 132 LAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIVITHDeelvdaadhiYRVEKDGRQK 202
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
140-224 |
4.10e-03 |
|
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: 38.36 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 140 ELSGGQKQRVAIARAL---VTNPKILLCDEATSALDPATTASILTLLKN-VNQtfGITIMMITHEMRVIKdICNRVAVM- 214
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDK--GNTVVVIEHNLDVIK-CADWIIDLg 245
|
90
....*....|....*
gi 493203783 215 -----EKGQVVETGT 224
Cdd:cd03271 246 peggdGGGQVVASGT 260
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
62-238 |
4.43e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 62 VIVDGHDIMNYSDKMMRDIkkdigMIFqhFNLLNSATVFKNVAMPLIlskkskTEIKQRVTEMLEfVGLSD-KKDQFPDE 140
Cdd:TIGR00630 423 VTVGGKSIADVSELSIREA-----HEF--FNQLTLTPEEKKIAEEVL------KEIRERLGFLID-VGLDYlSLSRAAGT 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493203783 141 LSGGQKQRVAIAR----ALVTNPKILlcDEATSALDPATTASILTLLKNVnQTFGITIMMITHEMRVIK------DICNR 210
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRaadyviDIGPG 565
|
170 180
....*....|....*....|....*...
gi 493203783 211 vAVMEKGQVVETGTVKEVFSHPKTTIAQ 238
Cdd:TIGR00630 566 -AGEHGGEVVASGTPEEILANPDSLTGQ 592
|
|
| |
