|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-341 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 510.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNF 240
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 241 VSTVIQTEPSSQLLQNLNDKQvGDYRDYKLFIEETQLPHPIVNDLIQINQGQVKILFSSMSEIQGKTVCYLWLRFDANQH 320
Cdd:COG1135 241 LPTVLNDELPEELLARLREAA-GGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDA 319
|
330 340
....*....|....*....|.
gi 1109734267 321 FNDtKIKHYFEMNDIQFEEVQ 341
Cdd:COG1135 320 AID-AALAYLREQGVVVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-340 |
4.69e-156 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 440.78 E-value: 4.69e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 241 VSTVIQTEPSSQLLQNLNDKQV-GDYRDYKLFIEETQLPHPIVNDLIQINQGQVKILFSSMSEIQGKTVCYLWLRFDANQ 319
Cdd:PRK11153 241 IQSTLHLDLPEDYLARLQAEPTtGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
|
330 340
....*....|....*....|.
gi 1109734267 320 hFNDTKIKHYFEMNDIQFEEV 340
Cdd:PRK11153 321 -GDIQAAIAYLQEHGVKVEVL 340
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
1.39e-141 |
|
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: 400.03 E-value: 1.39e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-245 |
8.55e-113 |
|
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: 331.08 E-value: 8.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
....*
gi 1109734267 241 VSTVI 245
Cdd:TIGR02314 241 IRSTL 245
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-244 |
2.60e-99 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 293.05 E-value: 2.60e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDySEKAMREI 80
Cdd:COG1126 1 MIEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKK-SKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLAPIKVKKmSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQN 239
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
....*
gi 1109734267 240 FVSTV 244
Cdd:COG1126 235 FLSKV 239
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
3.38e-97 |
|
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: 297.20 E-value: 3.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFN-KKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMRE 79
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 IKKDIGMIFQH-FNLLNSA-TVFKNVAMPL-ILSKKSKKEITQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVAIARAL 155
Cdd:COG1123 340 LRRRVQMVFQDpYSSLNPRmTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
7.82e-97 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 286.17 E-value: 7.82e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 -KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMcVIKDICNRVAVMEKGQVVE 221
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-232 |
5.88e-90 |
|
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: 269.16 E-value: 5.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:COG1127 5 MIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLI-LSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVF--SHP 232
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDP 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-233 |
2.76e-87 |
|
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: 265.38 E-value: 2.76e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLE---AASSGQVIVDGHDITDYSEKAM 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 REIK-KDIGMIFQH-FNLLN-SATVFKNVAMPLILSKK-SKKEITQRVTEMLEFVGLSDKK---DQFPDELSGGQKQRVA 150
Cdd:COG0444 81 RKIRgREIQMIFQDpMTSLNpVMTVGDQIAEPLRIHGGlSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240
|
...
gi 1109734267 231 HPK 233
Cdd:COG0444 241 NPR 243
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
6.31e-87 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 260.76 E-value: 6.31e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG2884 78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVE 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 |
1.65e-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: 259.73 E-value: 1.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIK 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KD-IGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMcVIKDICNRVAVMEKGQV 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-223 |
3.85e-82 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 248.96 E-value: 3.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQH-FNLLN-SATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKK---DQFPDELSGGQKQRVAIARAL 155
Cdd:cd03257 81 RKEIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
3.92e-82 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 249.59 E-value: 3.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:COG3638 2 MLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNV------AMPL---ILSKKSKKEItQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAI 151
Cdd:COG3638 79 RRRIGMIFQQFNLVPRLSVLTNVlagrlgRTSTwrsLLGLFPPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 152 ARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-241 |
9.83e-81 |
|
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: 245.87 E-value: 9.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMRei 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kKDIGMIFQH-FNLLNSA-TVFKNVAMPLILSKKskKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVT 157
Cdd:COG1124 79 -RRVQMVFQDpYASLHPRhTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIA 237
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....
gi 1109734267 238 QNFV 241
Cdd:COG1124 236 RELL 239
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-232 |
1.31e-80 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 245.10 E-value: 1.31e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIK 81
Cdd:cd03261 1 IELRGLTKSFGGR----TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLI-LSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-234 |
1.77e-79 |
|
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: 242.24 E-value: 1.77e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysEKAMREIK 81
Cdd:COG1122 1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG1122 75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKT 234
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-219 |
5.86e-78 |
|
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: 237.81 E-value: 5.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDySEKAMREIK 81
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKK-SKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLAPIKVKGmSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-220 |
1.46e-74 |
|
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: 230.15 E-value: 1.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIK 81
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNV------AMPL---ILSKKSKKEItQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVlsgrlgRRSTwrsLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-233 |
3.08e-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: 237.88 E-value: 3.08e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFnkKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHL---EAASSGQVIVDGHDITDYSEKAM 77
Cdd:COG1123 4 LLEVRDLSVRY--PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 ReikKDIGMIFQHF-NLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV 156
Cdd:COG1123 82 G---RRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-234 |
3.25e-74 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 233.07 E-value: 3.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITD---Ysekam 77
Cdd:COG3842 5 ALELENVSKRYGDV----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlppE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 reiKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:COG3842 76 ---KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITH---EMCVIKDicnRVAVMEKGQVVETGTVTDVFSHPKT 234
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdqeEALALAD---RIAVMNDGRIEQVGTPEEIYERPAT 229
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
7.84e-74 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 228.82 E-value: 7.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysekamrEI 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT--------GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHemcvikDI------CNRVAVMEK--GQVVET 222
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTH------DVdeavflADRVVVLSArpGRIVEE 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-233 |
1.77e-73 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 230.39 E-value: 1.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 11 FNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIKKDIGMIFQH 90
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 91 -FNLLNS-ATVFKNVAMPLILSK-KSKKEITQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:COG4608 104 pYASLNPrMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 167 ATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-244 |
1.36e-72 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 229.99 E-value: 1.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKK-------------KQKIH-------ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSG 60
Cdd:COG4175 3 KIEVRNLYKIFGKRperalklldqgksKDEILektgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 61 QVIVDGHDITDYSEKAMREI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPD 139
Cdd:COG4175 83 EVLIDGEDITKLSKKELRELrRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 140 ELSGGQKQRVAIARALVTNPKILLCDEATSALDPAttasI--------LALLKNVNQtfgiTIMIITHemcvikD----- 206
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDPL----IrremqdelLELQAKLKK----TIVFITH------Dldeal 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 1109734267 207 -ICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVSTV 244
Cdd:COG4175 229 rLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-228 |
5.43e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 223.02 E-value: 5.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekamREIK 81
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-220 |
7.91e-72 |
|
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: 222.94 E-value: 7.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKS--------KKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-246 |
5.75e-71 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 221.75 E-value: 5.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQK-------------IH-------ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQ 61
Cdd:cd03294 1 IKIKGLYKIFGKNPQKafkllakgkskeeILkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 62 VIVDGHDITDYSEKAMREI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDE 140
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 141 LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
250 260
....*....|....*....|....*.
gi 1109734267 221 ETGTVTDVFSHPkttiAQNFVSTVIQ 246
Cdd:cd03294 241 QVGTPEEILTNP----ANDYVREFFR 262
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-223 |
9.32e-71 |
|
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: 219.31 E-value: 9.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysekaMREIK 81
Cdd:cd03259 1 LELKGLSKTYGSV----RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-233 |
3.55e-69 |
|
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: 217.32 E-value: 3.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKK-KQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:TIGR04521 1 IKLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQhF--NLLNSATVFKNVAM-PLILsKKSKKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALV 156
Cdd:TIGR04521 81 RKKVGLVFQ-FpeHQLFEETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-234 |
2.04e-68 |
|
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: 223.02 E-value: 2.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 11 FNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTL----VRLVnhleaASSGQVIVDGHDITDYSEKAMREIKKDIGM 86
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 87 IFQH-FNLLNS-ATVFKNVAMPLIL--SKKSKKEITQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:COG4172 367 VFQDpFGSLSPrMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKT 234
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQH 519
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-218 |
5.48e-68 |
|
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: 211.94 E-value: 5.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKKKQKihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekaMREIKK 82
Cdd:cd03225 1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMIFQHFN--LLNSaTVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03225 76 KVGLVFQNPDdqFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQ 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 |
9.48e-68 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 210.12 E-value: 9.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYsEKAMREIK 81
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLilskkskkeitqrvtemlefvglsdkkdqfpdelSGGQKQRVAIARALVTNPKI 161
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQ 218
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-241 |
3.98e-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: 210.56 E-value: 3.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamreiK 81
Cdd:cd03300 1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITH---EMCVIKDicnRVAVMEKGQVVETGTVTDVFSHPKTTIAQ 238
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHdqeEALTMSD---RIAVMNKGKIQQIGTPEEIYEEPANRFVA 228
|
...
gi 1109734267 239 NFV 241
Cdd:cd03300 229 DFI 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-245 |
1.24e-66 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 213.40 E-value: 1.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamrei 80
Cdd:COG3839 3 SLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHemcvikD------ICNRVAVMEKGQVVETGTVTDVFSHPKT 234
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH------DqveamtLADRIAVMNDGRIQQVGTPEELYDRPAN 227
|
250
....*....|.
gi 1109734267 235 TiaqnFVSTVI 245
Cdd:COG3839 228 L----FVAGFI 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-225 |
2.46e-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: 208.09 E-value: 2.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGhditdyseKAMREIK 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHemcvikDI------CNRVAVMEK--GQVVETGTV 225
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTH------DIdeavflADRVVVLSArpGRIVAEVEV 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-219 |
4.96e-66 |
|
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: 207.26 E-value: 4.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFnkkKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIK 81
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-244 |
9.34e-66 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 207.64 E-value: 9.34e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKaMREI 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ----VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD-ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAM-PLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQN 239
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
....*
gi 1109734267 240 FVSTV 244
Cdd:PRK09493 235 FLQHV 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-233 |
1.14e-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: 1.14e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKS----TLVRLVNHLEAASSGQVIVDGHDITDYSEKA 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 77 MREIK-KDIGMIFQ---------HfnllnsaTVFKNVAMPLILSKK-SKKEITQRVTEMLEFVGLSDKK---DQFPDELS 142
Cdd:COG4172 86 LRRIRgNRIAMIFQepmtslnplH-------TIGKQIAEVLRLHRGlSGAAARARALELLERVGIPDPErrlDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 143 GGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVET 222
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
250
....*....|.
gi 1109734267 223 GTVTDVFSHPK 233
Cdd:COG4172 239 GPTAELFAAPQ 249
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-234 |
1.34e-65 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 210.39 E-value: 1.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdYSEKAMREik 81
Cdd:COG1118 3 IEVRNISKRFGSF----TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:COG1118 75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITH---EMCvikDICNRVAVMEKGQVVETGTVTDVFSHPKT 234
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHdqeEAL---ELADRVVVMNQGRIEQVGTPDEVYDRPAT 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-233 |
1.22e-64 |
|
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: 204.21 E-value: 1.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkamREI- 80
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPP---HEIa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSK----------KSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVA 150
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNQtFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
...
gi 1109734267 231 HPK 233
Cdd:cd03219 233 NPR 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-242 |
4.05e-64 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 203.32 E-value: 4.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDI---TDYSEKAMR 78
Cdd:COG4161 3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EIKKDIGMIFQHFNLLNSATVFKN-VAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTvTDVFSHPKTTIA 237
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAF 236
|
....*
gi 1109734267 238 QNFVS 242
Cdd:COG4161 237 AHYLS 241
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-225 |
4.80e-64 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 202.41 E-value: 4.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLE-----AASSGQVIVDGHDITDYSEKA 76
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 77 MrEIKKDIGMIFQHFNLLNsATVFKNVAMPL-ILSKKSKKEITQRVTEMLEFVGLSD--KKDQFPDELSGGQKQRVAIAR 153
Cdd:cd03260 77 L-ELRRRVGMVFQKPNPFP-GSIYDNVAYGLrLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 154 ALVTNPKILLCDEATSALDPATTASILALLKNVNQTfgITIMIITHEMCVIKDICNRVAVMEKGQVVETGTV 225
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-233 |
1.14e-63 |
|
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: 202.58 E-value: 1.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFnkkkQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDyseKAMREI 80
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG---LPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 -KKDIGMIFQHFNLLNSATVFKNVAM---------------PLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGG 144
Cdd:COG0411 77 aRLGIARTFQNPRLFPELTVLENVLVaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....*....
gi 1109734267 225 VTDVFSHPK 233
Cdd:COG0411 237 PAEVRADPR 245
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
2.02e-63 |
|
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: 201.12 E-value: 2.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKD-IGMIFQHFNLLNSATVFKNVAMPLILskKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMcVIKDICNRVAVMEKGQVVETGTVT 226
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDP-ALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-242 |
3.29e-63 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 201.01 E-value: 3.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItDYS----EKAMREIKKDIGMIFQHFNLLN 95
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSktpsDKAIRELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 96 SATVFKN-VAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPA 174
Cdd:PRK11124 96 HLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 175 TTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTvTDVFSHPKTTIAQNFVS 242
Cdd:PRK11124 176 ITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYLS 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-246 |
1.14e-59 |
|
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: 191.75 E-value: 1.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKK--DQFPDELSGGQKQRVAIARALVTNP 159
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPkttiAQN 239
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP----AND 230
|
....*..
gi 1109734267 240 FVSTVIQ 246
Cdd:cd03295 231 FVAEFVG 237
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
13-245 |
3.57e-59 |
|
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: 190.24 E-value: 3.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 13 KKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysekaMREIKKDIGMIFQHFN 92
Cdd:cd03299 7 SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-----LPPEKRDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 LLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:cd03299 82 LFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 173 PATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVSTVI 245
Cdd:cd03299 162 VRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNN 234
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
3.72e-59 |
|
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: 191.49 E-value: 3.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFnkKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysEKAMREIK 81
Cdd:TIGR04520 1 IEVENVSFSY--PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQH-FNLLNSATVFKNVA-------MPLilskkskKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:TIGR04520 77 KKVGMVFQNpDNQFVGATVEDDVAfglenlgVPR-------EEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 154 ALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEM--CVIKDicnRVAVMEKGQVVETGTVTDVFSH 231
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeeAVLAD---RVIVMNKGKIVAEGTPREIFSQ 226
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
21-246 |
1.28e-58 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 189.63 E-value: 1.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDI------------TDysEKAMREIKKDIGMIF 88
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpAD--RRQLQRIRTRLGMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 89 QHFNLLNSATVFKNV-AMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:COG4598 102 QSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEP 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 168 TSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVSTVIQ 246
Cdd:COG4598 182 TSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFLSSSLK 259
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-241 |
5.24e-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: 184.85 E-value: 5.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamreiK 81
Cdd:cd03296 3 IEVRNVSKRFGDFV----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-----E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPL----ILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:cd03296 74 RNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIA 237
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
....
gi 1109734267 238 QNFV 241
Cdd:cd03296 234 YSFL 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
2.37e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 183.03 E-value: 2.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNkkkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSeKAMREI 80
Cdd:COG3840 1 MLRLDDLTYRYG------DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KkdigMIFQHFNLLNSATVFKNVAM---P-LILSKKSKkeitQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV 156
Cdd:COG3840 74 S----MLFQENNLFPHLTVAQNIGLglrPgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
11-281 |
1.61e-55 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 184.14 E-value: 1.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 11 FNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIKKDIGMIFQH 90
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 91 -FNLLN-SATVFKNVAMPLIL--SKKSKKEITQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARALVTNPKILLCD 165
Cdd:PRK15079 107 pLASLNpRMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 166 EATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVSTVI 245
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
250 260 270
....*....|....*....|....*....|....*.
gi 1109734267 246 QTEPssqllqnlnDKQvgdyRDYKLFIEETQLPHPI 281
Cdd:PRK15079 267 IPDP---------DLE----RNKTIQLLEGELPSPI 289
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
1.84e-55 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 181.49 E-value: 1.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDghDITDYSEKAM--- 77
Cdd:PRK11264 3 AIEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSLsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 ----REIKKDIGMIFQHFNLLNSATVFKNVAM-PLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:PRK11264 77 kgliRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
250
....*....|
gi 1109734267 233 KTTIAQNFVS 242
Cdd:PRK11264 236 QQPRTRQFLE 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-232 |
4.16e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 180.28 E-value: 4.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdysekamREI 80
Cdd:COG1121 6 AIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNS--ATVFKNVAMPLI----LSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 155 LVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVEtGTVTDVFSHP 232
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPE 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-220 |
5.39e-55 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 179.30 E-value: 5.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK10908 78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-242 |
1.13e-54 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 179.46 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHL-----EAASSGQVIVDGHDITDYSEKA 76
Cdd:COG1117 12 IEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 77 MrEIKKDIGMIFQHFNLLnSATVFKNVAMPL-ILSKKSKKEITQRVTEMLEFVGL----SDKKDQFPDELSGGQKQRVAI 151
Cdd:COG1117 88 V-ELRRRVGMVFQKPNPF-PKSIYDNVAYGLrLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 152 ARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFgiTIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSH 231
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTN 243
|
250
....*....|.
gi 1109734267 232 PKTTIAQNFVS 242
Cdd:COG1117 244 PKDKRTEDYIT 254
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-241 |
1.87e-54 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 179.26 E-value: 1.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNK-----KKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDIT--DYSE 74
Cdd:COG4167 5 LEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 75 KAmreikKDIGMIFQHFNL-LN-SATVFKNVAMPLIL-SKKSKKEITQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVA 150
Cdd:COG4167 85 RC-----KHIRMIFQDPNTsLNpRLNIGQILEEPLRLnTDLTAEEREERIFATLRLVGLLpEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:COG4167 160 LARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFA 239
|
250
....*....|.
gi 1109734267 231 HPKTTIAQNFV 241
Cdd:COG4167 240 NPQHEVTKRLI 250
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-228 |
2.84e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 178.13 E-value: 2.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAmrei 80
Cdd:COG4555 1 MIEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
4.80e-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: 177.54 E-value: 4.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkamREI 80
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR---REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAM---PLI--LSKKSKKEItQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARAL 155
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHemcvikDI------CNRVAVMEKGQVVETGTVTDVF 229
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH------DLnlaaryADRLVLLKDGRIVAQGPPEEVL 226
|
.
gi 1109734267 230 S 230
Cdd:COG1120 227 T 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-223 |
5.67e-54 |
|
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: 176.29 E-value: 5.67e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamreiK 81
Cdd:cd03301 1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
1.03e-53 |
|
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: 187.35 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:COG2274 474 IELENVSFRYPGDSPPV--LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR--- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHfNLLNSATVFKNVAMplilskkSKKEIT-QRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRV 149
Cdd:COG2274 549 RQIGVVLQD-VFLFSGTIRENITL-------GDPDATdEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGT 692
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-219 |
1.62e-53 |
|
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: 173.74 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkamrEIK 81
Cdd:cd03230 1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE----EVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVamplilskkskkeitqrvtemlefvglsdkkdqfpdELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03230 73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-224 |
3.80e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 183.83 E-value: 3.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIk 81
Cdd:COG1132 340 IEFENVSFSYPGDRP---VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLnSATVFKNVAMplilskkSKKEIT-QRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRV 149
Cdd:COG1132 416 --IGVVPQDTFLF-SGTIRENIRY-------GRPDATdEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRI 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-226 |
6.01e-53 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 174.23 E-value: 6.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 5 RQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIK-KD 83
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 84 IGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILL 163
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 164 CDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDIcNRVAVMEKGQVVETGTVT 226
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSLM 230
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
6-233 |
9.07e-53 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 176.69 E-value: 9.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 6 QVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIKKDIG 85
Cdd:PRK11308 16 PVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 86 MIFQH-FNLLN-SATVFKNVAMPL-ILSKKSKKEITQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK11308 96 IVFQNpYGSLNpRKKVGQILEEPLlINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-230 |
2.03e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 174.53 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysEKAMREI 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEK-YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK13650 80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKdICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-281 |
2.94e-52 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 176.95 E-value: 2.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysekaMREI 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH-----VPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK11607 90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNF 240
Cdd:PRK11607 170 LLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1109734267 241 VSTViqtepssqllqNLNDKQVGDYRDYKLFIEETQLPHPI 281
Cdd:PRK11607 250 IGSV-----------NVFEGVLKERQEDGLVIDSPGLVHPL 279
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-229 |
5.05e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 173.70 E-value: 5.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKaMREIKKDIGMIFQH--FNLLNSa 97
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLVFQYpeYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLS--DKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPAT 175
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 176 TASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVF 229
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-227 |
1.81e-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: 169.86 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdyseKAMREIKKDIGMIFQHFNLLNSATV 99
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:cd03265 91 WENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1109734267 180 LALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTD 227
Cdd:cd03265 171 WEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
19-217 |
2.57e-51 |
|
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: 169.25 E-value: 2.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysekamreIKKDIGMIFQHFNLLNS-- 96
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--------ERKRIGYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 ATVFKNVAMPLI----LSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:cd03235 85 ISVRDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1109734267 173 PATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKG 217
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-241 |
4.33e-51 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 170.64 E-value: 4.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 14 KKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIKKDIGMIFQH-FN 92
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 LLNS-ATVFKNVAMPLI-LSKKSKKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK10419 101 AVNPrKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 170 ALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV--FSHPKTTIAQNFV 241
Cdd:PRK10419 181 NLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltFSSPAGRVLQNAV 254
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
7.99e-51 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 165.90 E-value: 7.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReikKDIGMIFQHFNLLNSATVF 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLR---KEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 101 KNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPD----ELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
8.91e-50 |
|
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: 164.09 E-value: 8.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIk 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLNsATVFKNVamplilskkskkeitqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKI 161
Cdd:cd03228 78 --IAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQ 218
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-241 |
2.68e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 168.97 E-value: 2.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamreiK 81
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----N 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITH---EMCVIKDicnRVAVMEKGQVVETGTVTDVFSHPKTTIAQ 238
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdqeEALTMSD---RIVVMRDGRIEQDGTPREIYEEPKNLFVA 242
|
...
gi 1109734267 239 NFV 241
Cdd:PRK09452 243 RFI 245
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-219 |
4.36e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.45 E-value: 4.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekaMREIK 81
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKKSKKEitQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG4619 74 RQVAYVPQEPALW-GGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-231 |
4.68e-49 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 165.57 E-value: 4.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 10 TFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGhdiTDYSEKAMREIKKDIGMIFQ 89
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 90 H-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:PRK13635 89 NpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 169 SALDPATTASILALLKNVNQTFGITIMIITHemcvikDI-----CNRVAVMEKGQVVETGTVTDVFSH 231
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLSITH------DLdeaaqADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
1.64e-48 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 164.10 E-value: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItDYSEKAMREI 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHF-NLLNSATVFKNVAM-PLILsKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK13639 77 RKTVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 159 PKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKT 234
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-240 |
4.41e-48 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 165.28 E-value: 4.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamreiK 81
Cdd:PRK11432 7 VVLKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-----Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNF 240
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-244 |
4.50e-48 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 165.26 E-value: 4.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:PRK10851 3 IEIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLNSATVFKNVAMPLIL----SKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:PRK10851 76 --VGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIA 237
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFV 233
|
....*..
gi 1109734267 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 ... |
2-225 |
4.64e-48 |
|
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: 161.13 E-value: 4.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdyseKAMREIK 81
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03263 75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTV 225
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-242 |
9.80e-48 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 161.68 E-value: 9.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDI-----TD-----YSEKAMREIKKDIGMIFQH 90
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDgqlkvADKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 91 FNLLNSATVFKNV-AMPLILSKKSKKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:PRK10619 101 FNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPT 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 169 SALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVS 242
Cdd:PRK10619 181 SALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-223 |
2.09e-47 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 159.28 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNrNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYsekaMREIK 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ----PQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTfgITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-242 |
1.18e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 158.54 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHL-----EAASSGQVIVDGHDITdysEKA 76
Cdd:PRK14247 4 IEIRDLKVSFGQVE----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIF---KMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 77 MREIKKDIGMIFQHFNLLNSATVFKNVAMPLILSK--KSKKEITQRVTEMLEFVGLSDK-KDQF---PDELSGGQKQRVA 150
Cdd:PRK14247 77 VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEvKDRLdapAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfgITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
250
....*....|..
gi 1109734267 231 HPKTTIAQNFVS 242
Cdd:PRK14247 235 NPRHELTEKYVT 246
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-218 |
2.46e-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: 154.71 E-value: 2.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReikK 82
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMIFQhfnllnsatvfknvamplilskkskkeitqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKIL 162
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 163 LCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQ 218
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-230 |
2.67e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 158.86 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItDYSEKAMREIKKDIGMIFQH-FNLLNSA 97
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQDpDNQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 178 SILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-230 |
5.06e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 157.94 E-value: 5.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTF--NKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysEKAMR 78
Cdd:PRK13633 4 MIKCKNVSYKYesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD--EENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EIKKDIGMIFQH-FNLLNSATVFKNVAM-PLILSKKSKkEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFgPENLGIPPE-EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
6.14e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 157.22 E-value: 6.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSktFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekaMREI 80
Cdd:PRK13648 7 IIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN---FEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTDVFSH 231
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-244 |
6.83e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 160.97 E-value: 6.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIK-KDIGMIFQHFNLLNSAT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 99 VFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAS 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 179 ILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVSTV 244
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-223 |
6.88e-46 |
|
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: 155.53 E-value: 6.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 14 KKQKIHALKdVSFKVNRNAIfGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKA-MREIKKDIGMIFQHFN 92
Cdd:cd03297 8 KRLPDFTLK-IDFDLNEEVT-GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInLPPQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 LLNSATVFKNVAmpLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:cd03297 86 LFPHLNVRENLA--FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 173 PATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
1.47e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 156.50 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFnkkKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysEKAMREI 80
Cdd:PRK13652 3 LIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFN-LLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK13652 77 RKFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-224 |
1.60e-45 |
|
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: 154.51 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 17 KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMreIKKDIGMIFQHFNLLNS 96
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 ATVFKNVAMPLILSKKSK-KEITQRVTEMleFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPAT 175
Cdd:cd03224 90 LTVEENLLLGAYARRRAKrKARLERVYEL--FPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1109734267 176 TASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:cd03224 168 VEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-223 |
5.88e-45 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 151.82 E-value: 5.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamrEIKK 82
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK---ELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMIFQhfnllnsatvfknvamplilskkskkeitqrvteMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKIL 162
Cdd:cd03214 74 KIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 163 LCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-223 |
1.66e-44 |
|
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: 151.97 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSktFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekaMREIK 81
Cdd:cd03245 3 IEFRNVS--FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKkskkeiTQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVnqTFGITIMIITHEMCVIkDICNRVAVMEKGQVVETG 223
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL--LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-252 |
2.73e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 160.41 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 8 SKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIKKDIGMI 87
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 88 FQ--HFNLLNSATVFKNVAMPLILSKKSKKEITQ-RVTEMLEFVGLSDKKD-QFPDELSGGQKQRVAIARALVTNPKILL 163
Cdd:PRK10261 407 FQdpYASLDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 164 CDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVST 243
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
....*....
gi 1109734267 244 VIQTEPSSQ 252
Cdd:PRK10261 567 VPVADPSRQ 575
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-223 |
5.98e-44 |
|
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: 150.34 E-value: 5.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 23 DVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysekAMREIKKDIGMIFQHFNLLNSATVFKN 102
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-----AAPPADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 103 VAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILAL 182
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1109734267 183 LKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
7.61e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 151.55 E-value: 7.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekAMRei 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--ADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkdiGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITH 199
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-233 |
1.07e-43 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 157.56 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKST----LVRLVNhleaaSSGQVIVDGHDITDYSEKAMREIKKDIGMIFQHFN-L 93
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 94 LNSA-TVFKNVAMPLILSKK--SKKEITQRVTEMLEFVGLS-DKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK15134 375 LNPRlNVLQIIEEGLRVHQPtlSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 170 ALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-245 |
2.03e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 150.38 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHL-----EAASSGQVIVDGHDItdYSEKAMR-EIKKDIGMIFQHFN 92
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPiEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 LLNSATVFKNVAMPLILSK--KSKKEITQRVTEMLEFVGLSDK-KDQ---FPDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEvKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 167 ATSALDPATTASILALLKNVNQTFgiTIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVSTVI 245
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
2.35e-43 |
|
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: 149.30 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSaTVFKNVAMplilskkSKKEITQ-RVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRV 149
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIAY-------GRPGATReEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDIcNRVAVMEKGQVVETGT 224
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERGT 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-228 |
2.78e-43 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 155.96 E-value: 2.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGH--DITDySEKAmr 78
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 eIKKDIGMIFQHFNLLNSATVFKNVAM---PLILSKKSKKEITQRVTEMLEFVGLS-DkkdqfPD----ELSGGQKQRVA 150
Cdd:COG3845 78 -IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvD-----PDakveDLSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKN-VNQtfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRlAAE--GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-228 |
4.99e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 152.48 E-value: 4.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREi 80
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kKDIGMIFQHFNLLNSATVFKNVAMPLILSKK---SKKEITQRVTEMLEFVGLS-DkkdqfPD----ELSGGQKQRVAIA 152
Cdd:COG1129 79 -AGIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDiD-----PDtpvgDLSVAQQQLVEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-232 |
5.39e-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: 149.48 E-value: 5.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 23 DVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysekAMREI-----KKDIGMIFQHFNLLNSA 97
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD----SARGIflpphRRRIGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNV--AMplilsKKSKKEITQ----RVTEMLefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSAL 171
Cdd:COG4148 93 SVRGNLlyGR-----KRAPRAERRisfdEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 172 DPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:COG4148 165 DLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
1.08e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 146.70 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKK--QKIhALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDIT-DYSEKAMR 78
Cdd:PRK13634 3 ITFQKVEHRYQYKTpfERR-ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EIKKDIGMIFQhF--NLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARAL 155
Cdd:PRK13634 82 PLRKKVGIVFQ-FpeHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-240 |
1.25e-41 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 146.09 E-value: 1.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKK-----KQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDIT--DYS 73
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 74 EKAMReikkdIGMIFQH-FNLLN-SATVFKNVAMPLILSKK-SKKEITQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRV 149
Cdd:PRK15112 84 YRSQR-----IRMIFQDpSTSLNpRQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVF 229
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
250
....*....|....*.
gi 1109734267 230 SHP-----KTTIAQNF 240
Cdd:PRK15112 239 ASPlheltKRLIAGHF 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-242 |
1.51e-41 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 145.30 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHL-----EAASSGQVIVDGHDItdYSEK 75
Cdd:PRK14239 5 ILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI--YSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 76 A-MREIKKDIGMIFQHFNLLnSATVFKNVAMPL-ILSKKSKKEITQRVTEMLEFVGLSDK-KDQFPDE---LSGGQKQRV 149
Cdd:PRK14239 79 TdTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLrLKGIKDKQVLDEAVEKSLKGASIWDEvKDRLHDSalgLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFgiTIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVF 229
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
|
250
....*....|...
gi 1109734267 230 SHPKTTIAQNFVS 242
Cdd:PRK14239 236 MNPKHKETEDYIS 248
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-231 |
1.63e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 146.04 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQ-KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSE-KAMRE 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 IKKDIGMIFQhF--NLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSH 231
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-224 |
2.45e-41 |
|
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: 144.17 E-value: 2.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVskTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:cd03252 1 ITFEHV--RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHfNLLNSATVFKNVA-----MPLilskkskkeitQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQ 145
Cdd:cd03252 76 RQVGVVLQE-NVLFNRSIRDNIAladpgMSM-----------ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 146 KQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
5.17e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.36 E-value: 5.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSktFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGhdiTDYSEKAMREI 80
Cdd:PRK13632 7 MIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK13632 82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMC-VIKdiCNRVAVMEKGQVVETGTVTDVF 229
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-223 |
6.57e-41 |
|
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: 142.36 E-value: 6.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKeitqRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03268 74 --IGALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-233 |
1.45e-40 |
|
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: 142.22 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMreikkdigMIFQHFNLLNSATVF 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAMPL--ILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAS 178
Cdd:TIGR01184 73 ENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 179 ILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV-FSHPK 233
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-231 |
2.50e-40 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 148.75 E-value: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:COG4988 337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR--- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNsATVFKNVAMplilskkSKKEIT-QRVTEMLEFVGLSDKKDQFPD-------E----LSGGQKQRV 149
Cdd:COG4988 411 RQIAWVPQNPYLFA-GTIRENLRL-------GRPDASdEELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTDVF 229
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
..
gi 1109734267 230 SH 231
Cdd:COG4988 560 AK 561
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-223 |
2.81e-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: 140.97 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdyseKAMREI 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-224 |
3.54e-40 |
|
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: 148.81 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIk 81
Cdd:COG5265 358 VRFENVSFGYDPERP-I--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQH---FNllnsATVFKNVAM--PlilsKKSKKEITQ--RVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRV 149
Cdd:COG5265 434 --IGIVPQDtvlFN----DTIAYNIAYgrP----DASEEEVEAaaRAAQIHDFIeSLPDGYDTRVGErglkLSGGEKQRV 503
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:COG5265 504 AIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-224 |
3.64e-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: 141.21 E-value: 3.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:cd03253 1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNsATVFKNVAMplilSKKSKKEitQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:cd03253 75 RAIGVVPQDTVLFN-DTIGYNIRY----GRPDATD--EEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-200 |
3.67e-40 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 141.07 E-value: 3.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 K-KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHE 200
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-261 |
3.79e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 142.63 E-value: 3.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFnkKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHL---EAASSGQVIVDGHDITdysEKAMR 78
Cdd:PRK13640 6 VEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLT---AKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EIKKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCViKDICNRVAVMEKGQVVETGTVTDVFshPKTTIA 237
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQGSPVEIF--SKVEML 237
|
250 260 270
....*....|....*....|....*....|..
gi 1109734267 238 QN------FVSTVIQ--TEPSSQLLQNLNDKQ 261
Cdd:PRK13640 238 KEigldipFVYKLKNklKEKGISVPQEINTEE 269
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-224 |
5.07e-40 |
|
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: 147.99 E-value: 5.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIk 81
Cdd:COG4987 334 LELEDVSFRYPGAGRP--VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLNsATVFKNVAMplilskkSKKEIT-QRVTEMLEFVGLSDKKDQFPD-------E----LSGGQKQRV 149
Cdd:COG4987 411 --IAVVPQRPHLFD-TTLRENLRL-------ARPDATdEELWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIkDICNRVAVMEKGQVVETGT 224
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGT 552
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
6-233 |
6.71e-40 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 142.96 E-value: 6.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 6 QVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKS----TLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI- 80
Cdd:PRK11022 8 KLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQhfNLLNSATVFKNVAMPLILSKK-----SKKEITQRVTEMLEFVGLSD---KKDQFPDELSGGQKQRVAIA 152
Cdd:PRK11022 88 GAEVAMIFQ--DPMTSLNPCYTVGFQIMEAIKvhqggNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
.
gi 1109734267 233 K 233
Cdd:PRK11022 246 R 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-222 |
8.75e-40 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 137.95 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIK 81
Cdd:cd03216 1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQhfnllnsatvfknvamplilskkskkeitqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKI 161
Cdd:cd03216 77 --IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVET 222
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-233 |
1.27e-39 |
|
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: 139.60 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDY--SEKAmre 79
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 iKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:cd03218 74 -RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQtFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
1.49e-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: 139.60 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTF-NKKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPI--LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkdIGMIFQHFNLLNsATVFKNVAMplilskkSKKEITQ-------RVTEMLEFV-GLSDKKD----QFPDELSGGQKQR 148
Cdd:cd03249 79 ---IGLVSQEPVLFD-GTIAENIRY-------GKPDATDeeveeaaKKANIHDFImSLPDGYDtlvgERGSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 149 VAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-232 |
2.43e-39 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 141.79 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 10 TFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAAS---SGQVIVDGHDITDYSEKAMREIK-KDIG 85
Cdd:PRK09473 21 TFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRaEQIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 86 MIFQH-FNLLNS-ATVFKNVAMPLILSKK-SKKEITQRVTEMLEFVGLSDKKDQ---FPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK09473 101 MIFQDpMTSLNPyMRVGEQLMEVLMLHKGmSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-224 |
5.23e-39 |
|
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: 137.74 E-value: 5.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIk 81
Cdd:cd03254 3 IEFENVNFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLnSATVFKNVAMPLILSKKSKKEITQRVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIARALV 156
Cdd:cd03254 79 --IGVVLQDTFLF-SGTIMENIRLGRPNATDEEVIEAAKEAGAHDFImKLPNGYDTVLGEnggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
17-233 |
5.75e-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: 137.81 E-value: 5.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 17 KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS-EKAMReikKDIGM------IFQ 89
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIAR---LGIGYvpegrrIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 90 HFnllnsaTVFKNVAMPLILsKKSKKEITQRVTEMLE-FVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:COG0410 92 SL------TVEENLLLGAYA-RRDRAEVRADLERVYElFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 169 SALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-303 |
7.34e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 139.47 E-value: 7.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysekamREI 80
Cdd:COG4152 1 MLELKGLTKRFGDK----TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMifqhfnllnsatvfknvaMP--------------LI----LSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELS 142
Cdd:COG4152 70 RRRIGY------------------LPeerglypkmkvgeqLVylarLKGLSKAEAKRRADEWLERLGLGDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 143 GGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVET 222
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 223 GTVTDVfshpKTTIAQNFVstVIQTEPSSQLLQNLNDKQVGDYRD--YKLFIEETQLPHPIVNDLIQinQGQVKiLFS-- 298
Cdd:COG4152 211 GSVDEI----RRQFGRNTL--RLEADGDAGWLRALPGVTVVEEDGdgAELKLEDGADAQELLRALLA--RGPVR-EFEev 281
|
....*..
gi 1109734267 299 --SMSEI 303
Cdd:COG4152 282 rpSLNEI 288
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-245 |
9.67e-39 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 140.75 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkIHALKDVSFKVnRNAIFGVI-GYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYsEKAMRe 79
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDV-ADGEFIVLvGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPADR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 ikkDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTE---MLEFVGLSDKKdqfPDELSGGQKQRVAIARALV 156
Cdd:PRK11650 77 ---DIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITH---EMCVIKDicnRVAVMEKGQVVETGTVTDVFSHPK 233
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHdqvEAMTLAD---RVVVMNGGVAEQIGTPVEVYEKPA 227
|
250
....*....|..
gi 1109734267 234 TTiaqnFVSTVI 245
Cdd:PRK11650 228 ST----FVASFI 235
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-231 |
1.12e-38 |
|
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: 144.47 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekaMREIK 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSaTVFKNVAMplilsKKSKKEITQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:TIGR02203 406 RQVALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTDVFS 230
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
.
gi 1109734267 231 H 231
Cdd:TIGR02203 557 R 557
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-246 |
1.54e-38 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 144.61 E-value: 1.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKS-TLVRLVNHLEAAS-------------SGQVIvdg 66
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGglvqcdkmllrrrSRQVI--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 67 hDITDYSEKAMREIK-KDIGMIFQH-FNLLNSA-TVFKNVAMPLILSKK-SKKEITQRVTEMLEFVGLSDKK---DQFPD 139
Cdd:PRK10261 89 -ELSEQSAAQMRHVRgADMAMIFQEpMTSLNPVfTVGEQIAESIRLHQGaSREEAMVEAKRMLDQVRIPEAQtilSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 140 ELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260
....*....|....*....|....*..
gi 1109734267 220 VETGTVTDVFSHPKTTIAQNFVSTVIQ 246
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVPQ 274
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-220 |
2.42e-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: 135.46 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 13 KKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdysekAMREIKKDIGMIFQHfn 92
Cdd:cd03226 10 KKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI------KAKERRKSIGYVMQD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 lLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:cd03226 80 -VDYQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1109734267 173 PATTASILALLKNVnQTFGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:cd03226 159 YKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-260 |
1.17e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 136.29 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 7 VSKTFNKKKQ-KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEK--AMREIKKD 83
Cdd:PRK13645 12 VSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVKRLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 84 IGMIFQ--HFNLLNSaTVFKNVAMPLILSKKSKKEITQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK13645 92 IGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKttiaqnf 240
Cdd:PRK13645 171 TLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE------- 243
|
250 260
....*....|....*....|..
gi 1109734267 241 VSTVIQTEPSS--QLLQNLNDK 260
Cdd:PRK13645 244 LLTKIEIDPPKlyQLMYKLKNK 265
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-233 |
2.14e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 134.00 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS--EKAmr 78
Cdd:COG1137 3 TLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 eiKKDIGM------IFQhfNLlnsaTVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:COG1137 77 --RLGIGYlpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTA---SILALLKNvnqtFGITIMIITH---EMCvikDICNRVAVMEKGQVVETGTVT 226
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVAdiqKIIRHLKE----RGIGVLITDHnvrETL---GICDRAYIISEGKVLAEGTPE 221
|
....*..
gi 1109734267 227 DVFSHPK 233
Cdd:COG1137 222 EILNNPL 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-200 |
2.23e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 141.40 E-value: 2.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKD-IGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHE 200
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-230 |
3.81e-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: 139.55 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTF-NKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVD-GHDITDYSEKAMR 78
Cdd:TIGR03269 279 IIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 E---IKKDIGMIFQHFNLLNSATVFKNV--AMPLILSKKSKKeitQRVTEMLEFVGLSDKK-----DQFPDELSGGQKQR 148
Cdd:TIGR03269 359 GrgrAKRYIGILHQEYDLYPHRTVLDNLteAIGLELPDELAR---MKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 149 VAIARALVTNPKILLCDEATSALDPAT----TASILALLKNVNQTFgitiMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITkvdvTHSILKAREEMEQTF----IIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
|
....*.
gi 1109734267 225 VTDVFS 230
Cdd:TIGR03269 512 PEEIVE 517
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-224 |
7.81e-37 |
|
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: 140.09 E-value: 7.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVskTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:TIGR03797 452 IEVDRV--TFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR--- 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKKskkeitqRVTEMLEFVGLSDKKDQFP-------DE----LSGGQKQRVA 150
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENIAGGAPLTLD-------EAWEAARMAGLAEDIRAMPmgmhtviSEgggtLSGGQRQRLL 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNqtfgITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
13-245 |
9.93e-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: 135.24 E-value: 9.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 13 KKKQKIHALkDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI-KKDIGMIFQHF 91
Cdd:TIGR02142 6 SKRLGDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 92 NLLNSATVFKNVAMPLILSKKSKKEIT-QRVTEMLefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:TIGR02142 85 RLFPHLSVRGNLRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 171 LDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPK-TTIAQNFVSTVI 245
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlPWLAREDQGSLI 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-241 |
1.49e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 132.48 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDI---TDYSEKAMREIKKDIGMIFQHFNLLNSA 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNVAMPLILSK-KSKKEITQRVTEMLEFVGL----SDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PRK14246 106 SIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 173 PATTASILALLKNVNQTfgITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFV 241
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-228 |
1.58e-36 |
|
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: 131.49 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYseKAMREIKKDIG------MIFQHFn 92
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL--PPHERARAGIAyvpqgrEIFPRL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 llnsaTVFKNVAMPLILSKKSKKEITQRVTEMleFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:TIGR03410 91 -----TVEENLLTGLAALPRRSRKIPDEIYEL--FPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 173 PATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:TIGR03410 164 PSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-223 |
2.15e-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: 130.48 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysekamrEIK 81
Cdd:cd03269 1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-------AAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 162 LLCDEATSALDPATTasilALLKNVNQTF---GITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03269 150 LILDEPFSGLDPVNV----ELLKDVIRELaraGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-229 |
2.73e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 132.55 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQ-KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS-EKAMR 78
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EIKKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVAIARALV 156
Cdd:PRK13643 81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVF 229
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-232 |
2.91e-36 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 133.49 E-value: 2.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 17 KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEaaSSGQVIVD-----GHDITDYSEKAMREI-KKDIGMIFQ 89
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITK--DNWHVTADrfrwnGIDLLKLSPRERRKIiGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 90 HFN--LLNSATVFKNV--AMPLILSK----KSKKEITQRVTEMLEFVGLSDKKD---QFPDELSGGQKQRVAIARALVTN 158
Cdd:COG4170 97 EPSscLDPSAKIGDQLieAIPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 159 PKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-224 |
6.54e-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: 6.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKihALKDVSFKVNRNAIFGVIGYSGAGKSTLV----RLVNhleaASSGQVIVDGHDITDYSEKAM 77
Cdd:cd03244 3 IEFKNVSLRYRPNLPP--VLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDGVDISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 REIkkdIGMIFQHfNLLNSATVFKNVAmplILSKKSKKEItQRVTE---MLEFVGLSDKKDQFPDE-----LSGGQKQRV 149
Cdd:cd03244 77 RSR---ISIIPQD-PVLFSGTIRSNLD---PFGEYSDEEL-WQALErvgLKEFVESLPGGLDTVVEeggenLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKnvNQTFGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
11-245 |
1.57e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 131.51 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 11 FNKKK-QKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQV----IVDGHDITDYSE---------KA 76
Cdd:PRK13631 31 FDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELitnpyskkiKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 77 MREIKKDIGMIFQ--HFNLLNSaTVFKNVAMPLILSKKSKKEITQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIAR 153
Cdd:PRK13631 111 FKELRRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 154 ALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP- 232
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQh 268
|
250
....*....|....*.
gi 1109734267 233 ---KTTIAQNFVSTVI 245
Cdd:PRK13631 269 iinSTSIQVPRVIQVI 284
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-219 |
2.56e-35 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.03 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 5 RQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVdghditdySEKAMREIKKDI 84
Cdd:PRK11247 16 NAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA--------GTAPLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 85 GMIFQHFNLLNSATVFKNVAMPLilskksKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLC 164
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 165 DEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-224 |
2.62e-35 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 135.09 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNsatvfKNVAMPLILSKKSKKEITQR----VTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIA 152
Cdd:PRK13657 409 RNIAVVFQDAGLFN-----RSIEDNIRVGRPDATDEEMRaaaeRAQAHDFIeRKPDGYDTVVGErgrqLSGGERQRLAIA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-220 |
2.91e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 129.05 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQ-KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysekAMRE 79
Cdd:COG1101 1 MLELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-----KLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 IK--KDIGMIFQhfN-LLNSA---TVFKNVAM--------PLILS-KKSKKEITQRVTEMLEfVGLSDKKDQFPDELSGG 144
Cdd:COG1101 76 YKraKYIGRVFQ--DpMMGTApsmTIEENLALayrrgkrrGLRRGlTKKRRELFRELLATLG-LGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMcviKD---ICNRVAVMEKGQVV 220
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM---EQaldYGNRLIMMHEGRII 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-219 |
3.49e-35 |
|
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: 126.18 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIkkdIGMIFQHFNLLnSATVF 100
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH---VGYLPQDDELF-SGSIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVamplilskkskkeitqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL 180
Cdd:cd03246 94 ENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1109734267 181 ALLKNVnQTFGITIMIITHEMCVIKdICNRVAVMEKGQV 219
Cdd:cd03246 137 QAIAAL-KAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-234 |
1.24e-34 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 132.52 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAAS-----SGQVIVDGHDITDYSEK 75
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 76 AMREIKKD-IGMIFQH----FNLLNsaTVFKNVAMPLILSKKSKKEITQrvTEM---LEFVGLSDKKDQ---FPDELSGG 144
Cdd:PRK15134 85 TLRGVRGNkIAMIFQEpmvsLNPLH--TLEKQLYEVLSLHRGMRREAAR--GEIlncLDRVGIRQAAKRltdYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250
....*....|...
gi 1109734267 225 VTDVFS---HPKT 234
Cdd:PRK15134 241 AATLFSaptHPYT 253
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-224 |
1.43e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 127.44 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRlvnHLEAASSGQVIVDGH-----DITDYSEK 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLR---HLSGLITGDKSAGSHiellgRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 76 AMREIKKD---IGMIFQHFNLLNSATVFKNVAMPLILS--------KKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGG 144
Cdd:PRK09984 77 LARDIRKSranTGYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-231 |
1.44e-34 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 126.73 E-value: 1.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTF------------------NKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQV 62
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 63 IVDGHdITdysekAMREikkdIGMIFQhfnllNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDkkdqFPDE-- 140
Cdd:COG1134 84 EVNGR-VS-----ALLE----LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGD----FIDQpv 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 141 --LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQ 218
Cdd:COG1134 145 ktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
|
250
....*....|...
gi 1109734267 219 VVETGTVTDVFSH 231
Cdd:COG1134 224 LVMDGDPEEVIAA 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-223 |
2.56e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.85 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 25 SFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamreiKKDIGMIFQHFNLLNSATVFKNVA 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 105 MPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLK 184
Cdd:PRK10771 94 LGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1109734267 185 NVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:PRK10771 174 QVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-233 |
2.86e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 127.25 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVS------KTFNKKkqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDIT-DYSE 74
Cdd:PRK13641 3 IKFENVDyiyspgTPMEKK-----GLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 75 KAMREIKKDIGMIFQhF--NLLNSATVFKNVAM-PLILSKkSKKEITQRVTEMLEFVGLSDK-KDQFPDELSGGQKQRVA 150
Cdd:PRK13641 78 KNLKKLRKKVSLVFQ-FpeAQLFENTVLKDVEFgPKNFGF-SEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVnQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
...
gi 1109734267 231 HPK 233
Cdd:PRK13641 235 DKE 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-229 |
3.47e-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: 125.97 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVI-VDGHDITDYSekaMRE 79
Cdd:COG1119 3 LLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGED---VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 IKKDIGMI--FQHFNLLNSATVFkNVamplILS---------KKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQR 148
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVL-DV----VLSgffdsiglyREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 149 VAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEmcvIKDI--C-NRVAVMEKGQVVETGTV 225
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIppGiTHVLLLKDGRVVAAGPK 227
|
....
gi 1109734267 226 TDVF 229
Cdd:COG1119 228 EEVL 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-223 |
3.74e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.39 E-value: 3.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamrEIKKDIGMIFQH-FNLLNSA 97
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRSKVGLVFQDpDDQVFSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1109734267 178 SILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:PRK13647 176 TLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-223 |
4.96e-34 |
|
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: 124.57 E-value: 4.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTF------------------NKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVI 63
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 64 VDGhditdysekamreikKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSG 143
Cdd:cd03220 81 VRG---------------RVSSLLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 144 GQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMiITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIL-VSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-238 |
8.52e-34 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 125.26 E-value: 8.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSktFNKKKQKIHAlkDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCIFD--NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEM-LEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK11831 83 RKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQ 238
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQ 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-243 |
1.57e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 125.58 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKK-KQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQV---IVDGHDITDYSE--- 74
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 75 ---------------KAMREIKKDIGMIFQ--HFNLLNSaTVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKK-DQ 136
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 137 FPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEK 216
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250 260
....*....|....*....|....*..
gi 1109734267 217 GQVVETGTVTDVFSHPKTTIAQNFVST 243
Cdd:PRK13651 241 GKIIKDGDTYDILSDNKFLIENNMEPP 267
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-249 |
2.54e-33 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 126.68 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 4 FRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDghditdysEKAMREI--- 80
Cdd:PRK11000 6 LRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--------EKRMNDVppa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK11000 74 ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIA--- 237
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVagf 233
|
250
....*....|....*...
gi 1109734267 238 -----QNFVS-TVIQTEP 249
Cdd:PRK11000 234 igspkMNFLPvKVTATAI 251
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-230 |
2.76e-33 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 128.77 E-value: 2.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEA--ASSGQVIV--------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKE----VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 65 -DGH--------------DITDYSEKAMREIKKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFV 128
Cdd:TIGR03269 77 kVGEpcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 129 GLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260
....*....|....*....|..
gi 1109734267 209 NRVAVMEKGQVVETGTVTDVFS 230
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVA 258
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-232 |
5.26e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 123.56 E-value: 5.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFnkkKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkaMREI 80
Cdd:PRK13644 1 MIRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQhfnllNSATVF-------------KNVAMPLIlskkskkEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQ 147
Cdd:PRK13644 76 RKLVGIVFQ-----NPETQFvgrtveedlafgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 148 RVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTD 227
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPEN 221
|
....*
gi 1109734267 228 VFSHP 232
Cdd:PRK13644 222 VLSDV 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-228 |
5.85e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 122.50 E-value: 5.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkamREI 80
Cdd:COG4604 1 MIEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS---REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQ--HFNL-LnsaTVFKNVAM---PLilSK-KSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:COG4604 74 AKRLAILRQenHINSrL---TVRELVAFgrfPY--SKgRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 154 ALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIithemcVIKDI------CNRVAVMEKGQVVETGTVTD 227
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVI------VLHDInfascyADHIVAMKDGRVVAQGTPEE 222
|
.
gi 1109734267 228 V 228
Cdd:COG4604 223 I 223
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-231 |
5.87e-33 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 128.60 E-value: 5.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREik 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRN-- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kDIGMIFQHFNLLNSaTVFKNVAMPLIlSKKSKKEITQ--RVTEMLEFVglsDKKDQFPDE--------LSGGQKQRVAI 151
Cdd:PRK11176 418 -QVALVSQNVHLFND-TIANNIAYART-EQYSREQIEEaaRMAYAMDFI---NKMDNGLDTvigengvlLSGGQRQRIAI 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 152 ARALVTNPKILLCDEATSALDP----ATTASILALLKNVnqtfgiTIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTD 227
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTeserAIQAALDELQKNR------TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
....
gi 1109734267 228 VFSH 231
Cdd:PRK11176 565 LLAQ 568
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-230 |
7.83e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.57 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS--EKAMR 78
Cdd:PRK13548 2 MLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 eikkdIGMIFQHFNLLNSATVFKNVAM---PLILSKKSKKEITQRVtemLEFVGLSDKKDQFPDELSGGQKQRVAIARAL 155
Cdd:PRK13548 78 -----RAVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAA---LAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 156 V------TNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHemcvikDI------CNRVAVMEKGQVVETG 223
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH------DLnlaaryADRIVLLHQGRLVADG 223
|
....*..
gi 1109734267 224 TVTDVFS 230
Cdd:PRK13548 224 TPAEVLT 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-220 |
1.53e-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: 119.96 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIHA--LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVN--HLEAASSGQVIVDGHDITdysekaM 77
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD------K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 REIKKDIGMIFQHFNLLNSATVFKNVAMPLILSKkskkeitqrvtemlefvglsdkkdqfpdeLSGGQKQRVAIARALVT 157
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHE-MCVIKDICNRVAVMEKGQVV 220
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-234 |
2.04e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.89 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKT-----------------FNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVI 63
Cdd:COG4586 1 IIEVENLSKTyrvyekepglkgalkglFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 64 VDGHDItdYSEKamREIKKDIGMIF-Q----HFNLlnsatvfknvamPLI----LSKK----SKKEITQRVTEMLEFVGL 130
Cdd:COG4586 81 VLGYVP--FKRR--KEFARRIGVVFgQrsqlWWDL------------PAIdsfrLLKAiyriPDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 131 SDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNR 210
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
|
250 260
....*....|....*....|....*..
gi 1109734267 211 VAVMEKGQVVETGTVTDV---FSHPKT 234
Cdd:COG4586 225 VIVIDHGRIIYDGSLEELkerFGPYKT 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-228 |
4.43e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 125.28 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:PRK09700 5 YISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkDIGMIFQHFNLLNSATVFKNVAMPLILSKK-------SKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 154 ALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-257 |
5.55e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.97 E-value: 5.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 13 KKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysEKAMREIKKDIGMIFQH-F 91
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT---AENVWNLRRKIGMVFQNpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 92 NLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSAL 171
Cdd:PRK13642 92 NQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 172 DPATTASILALLKNVNQTFGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTDVFShpkttIAQNFVSTVIQTEPSS 251
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA-----TSEDMVEIGLDVPFSS 245
|
....*.
gi 1109734267 252 QLLQNL 257
Cdd:PRK13642 246 NLMKDL 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-246 |
6.04e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 120.03 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 5 RQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDG-----HDITDYSEKAMRE 79
Cdd:PRK11701 10 RGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 I-KKDIGMIFQHF--NLLNSATVFKNVAMPLI-LSKKSKKEITQRVTEMLEFVGL-SDKKDQFPDELSGGQKQRVAIARA 154
Cdd:PRK11701 86 LlRTEWGFVHQHPrdGLRMQVSAGGNIGERLMaVGARHYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 155 LVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG---TVTDVFSH 231
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGltdQVLDDPQH 245
|
250
....*....|....*
gi 1109734267 232 PKTtiaQNFVSTVIQ 246
Cdd:PRK11701 246 PYT---QLLVSSVLQ 257
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-199 |
7.60e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 118.35 E-value: 7.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAA--SSGQVIVDGHDITDYSEKAMReikkdIGMIFQ------HF 91
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQRR-----IGILFQddllfpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 92 NllnsatVFKNV--AMPLILSKKSKKeitQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:COG4136 92 S------VGENLafALPPTIGRAQRR---ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|
gi 1109734267 170 ALDPATTASILALLKNVNQTFGITIMIITH 199
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-224 |
1.02e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 125.60 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTF-NKKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMRei 80
Cdd:TIGR00958 479 IEFQDVSFSYpNRPDVPV--LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH-- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kKDIGMIFQHfNLLNSATVFKNVAMPLilSKKSKKEITQRVTEML--EFV-GLSDKKDQFPDE----LSGGQKQRVAIAR 153
Cdd:TIGR00958 555 -RQVALVGQE-PVLFSGSVRENIAYGL--TDTPDEEIMAAAKAANahDFImEFPNGYDTEVGEkgsqLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 154 ALVTNPKILLCDEATSALDpattASILALLKNVNQTFGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-218 |
1.70e-31 |
|
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: 118.31 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTF---NKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVD-GHDITDYSEKA 76
Cdd:COG4778 4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 77 MREI----KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLsdkkdqfPDEL--------SGG 144
Cdd:COG4778 84 PREIlalrRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL-------PERLwdlppatfSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQ 218
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-201 |
1.78e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 119.03 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekAMReikkdiGMIFQHFNLLNSATV 99
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG--AER------GVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180
....*....|....*....|..
gi 1109734267 180 LALLKNVNQTFGITIMIITHEM 201
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDI 189
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-232 |
2.94e-31 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.17 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDY-SEKAMREikkdiGMI--FQHFNLLNS 96
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARM-----GVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 ATVFKN--VAMPLILS-------------KKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK11300 95 MTVIENllVAQHQQLKtglfsgllktpafRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-200 |
3.43e-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: 116.81 E-value: 3.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdysEKAMREI 80
Cdd:COG4133 2 MLEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFqHFNLLNSA-TVFKNVAMpliLSKKSKKEITQ-RVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:COG4133 74 RRRLAYLG-HADGLKPElTVRENLRF---WAALYGLRADReAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1109734267 159 PKILLCDEATSALDPATTASILALLKNVNQTFGItIMIITHE 200
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-242 |
6.79e-31 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 117.11 E-value: 6.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 22 KDVSFKVNRNAIFGVIGYSGAGKS-TLVRLVNHLEA---ASSGQVIVDGhdiTDYSEKAMREIKkdIGMIFQH----FN- 92
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDG---KPVAPCALRGRK--IATIMQNprsaFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 LLNSATVFKNVampliLSKKSKKEITQRVTEMLEFVGLSDKK---DQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK10418 95 LHTMHTHARET-----CLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 170 ALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVS 242
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-231 |
2.12e-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: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkamREIKKDIGMIFQHFNLLnSATVF 100
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR---EELGRHIGYLPQDVELF-DGTIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVA-MPlilskkskkEIT-QRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:COG4618 424 ENIArFG---------DADpEKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 168 TSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKdICNRVAVMEKGQVVETGTVTDVFSH 231
Cdd:COG4618 495 NSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
4.52e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.24 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAmreiK 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA----R 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVnQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-223 |
9.36e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 115.67 E-value: 9.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKA-MRei 80
Cdd:PRK13537 8 IDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArQR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkdIGMIFQHFNLLNSATVFKNVampLILSKK---SKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:PRK13537 82 ---VGVVPQFDNLDPDFTVRENL---LVFGRYfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-224 |
1.28e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 118.77 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSktFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIk 81
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLnSATVFKNvampLILSKKSKKEitQRVTEMLEFVGLSDKKDQfpDE------------LSGGQKQRV 149
Cdd:PRK11160 416 --ISVVSQRVHLF-SATLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLED--DKglnawlgeggrqLSGGEQRRL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 150 AIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITH------EMcvikdicNRVAVMEKGQVVETG 223
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHrltgleQF-------DRICVMDNGQIIEQG 555
|
.
gi 1109734267 224 T 224
Cdd:PRK11160 556 T 556
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-241 |
1.33e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 113.98 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 10 TFNKKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHL-----EAASSGQVIVDGHDItdYSEKA-MREIKKD 83
Cdd:PRK14258 14 SFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNI--YERRVnLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 84 IGMIFQHFNLLnSATVFKNVAMPL-ILSKKSKKEITQRVTEMLEFVGLSD----KKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK14258 90 VSMVHPKPNLF-PMSVYDNVAYGVkIVGWRPKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 159 PKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEK-----GQVVETGTVTDVFSHPK 233
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPH 248
|
....*...
gi 1109734267 234 TTIAQNFV 241
Cdd:PRK14258 249 DSRTREYV 256
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-230 |
1.58e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.49 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIH-ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS-EKAMRE 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 IKKDIGMIFQhfnlLNSATVF------------KNVAMPLilskkskKEITQRVTEMLEFVGLS-DKKDQFPDELSGGQK 146
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFedtvereiifgpKNFKMNL-------DEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 147 QRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVT 226
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
....
gi 1109734267 227 DVFS 230
Cdd:PRK13646 232 ELFK 235
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-224 |
1.68e-29 |
|
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: 112.12 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdySEKAMREIKKDIGMIFQHFNLLnSATV 99
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSSLTIIPQDPTLF-SGTI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNVAmplILSKKSKKEITQ--RVTEMlefvGLSdkkdqfpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:cd03369 99 RSNLD---PFDEYSDEEIYGalRVSEG----GLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1109734267 178 SIlalLKNVNQTF-GITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:cd03369 163 LI---QKTIREEFtNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-242 |
2.49e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 113.65 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSG-----QVIVDGHDITDYSEkaMREIKKDIGMIFQHFNLLn 95
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRRVGMLFQRPNPF- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 96 SATVFKNV-----AMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK14271 114 PMSIMDNVlagvrAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 171 LDPATTASILALLKNVNQTfgITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQNFVS 242
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
32-232 |
1.08e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 113.43 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 32 AIFGVigySGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamreI-----KKDIGMIFQHFNLLNSATVFKNV--A 104
Cdd:PRK11144 28 AIFGR---SGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKG----IclppeKRRIGYVFQDARLFPHYKVRGNLryG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 105 MplilsKKSKKEITQRVTEMLefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLK 184
Cdd:PRK11144 101 M-----AKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1109734267 185 NVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHP 232
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-242 |
1.31e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 111.41 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLE-----AASSGQVIVDGHDITDySEKAMREIKKDIGMIFQHFNLL 94
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 95 nSATVFKNVAM-PLILSKKSkkEITQRVTEMLEFVGLSDK-KDQFPDE---LSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK14243 104 -PKSIYDNIAYgARINGYKG--DMDELVERSLRQAALWDEvKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 170 ALDPATTASILALLKNVNQTFgiTIMIITHEMcvikDICNRVAVM-------------EKGQVVETGTVTDVFSHPKTTI 236
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQY--TIIIVTHNM----QQAARVSDMtaffnveltegggRYGYLVEFDRTEKIFNSPQQQA 254
|
....*.
gi 1109734267 237 AQNFVS 242
Cdd:PRK14243 255 TRDYVS 260
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-219 |
1.80e-28 |
|
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: 109.80 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKkqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdysekamREIK 81
Cdd:TIGR03740 1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSATVFKNVAM-PLILSKKskkeiTQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVhTTLLGLP-----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-219 |
2.59e-28 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 109.48 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFnKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIk 81
Cdd:cd03248 12 VKFQNVTFAY-PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHfNLLNSATVFKNVAMPLI-LSKKSKKEITQR------VTEMLEfvGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:cd03248 90 --VSLVGQE-PVLFARSLQDNIAYGLQsCSFECVKEAAQKahahsfISELAS--GYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 155 LVTNPKILLCDEATSALDPATTASILALLKNVNQTFgiTIMIITHEMCVIKDiCNRVAVMEKGQV 219
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
11-315 |
3.65e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 115.14 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 11 FNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAAS---SGQVIVDGHDITdysEKAMREIKkdiGMI 87
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID---AKEMRAIS---AYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 88 FQHFNLLNSATVFKN------VAMPLILSKKSKKeitQRVTEMLEFVGLSDKKD---QFPDE---LSGGQKQRVAIARAL 155
Cdd:TIGR00955 105 QQDDLFIPTLTVREHlmfqahLRMPRRVTKKEKR---ERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVT---DVFSHP 232
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDqavPFFSDL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 233 KTTIAQN-----FVSTVIQTEPSSQ-----LLQNLND-KQVGDY-RDYklfIEETQLPHPIVNDLIQINQGQVKILFSSM 300
Cdd:TIGR00955 262 GHPCPENynpadFYVQVLAVIPGSEnesreRIEKICDsFAVSDIgRDM---LVNTNLWSGKAGGLVKDSENMEGIGYNAS 338
|
330
....*....|....*
gi 1109734267 301 SEIQgktVCYLWLRF 315
Cdd:TIGR00955 339 WWTQ---FYALLKRS 350
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-230 |
5.09e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 109.21 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDIT--DYSEKAMReikkDIGMIFQHFNLLNSAT 98
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARR----GIGYLPQEASIFRRLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 99 VFKNVAMPLILSKKSKKEITQ-RVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:PRK10895 95 VYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 178 SILALLKNVnQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK10895 175 DIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-230 |
5.14e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 110.10 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 16 QKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItDYSEKAMREIKKDIGMIFQH----- 90
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDpeqqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 91 -FNLLNSATVF--KNVAMPlilskksKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:PRK13638 91 fYTDIDSDIAFslRNLGVP-------EAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 168 TSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-223 |
1.14e-27 |
|
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: 108.19 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTF-----------------NKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIV 64
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 65 DGhdITDYSEKamREIKKDIGMIF-QHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSG 143
Cdd:cd03267 81 AG--LVPWKRR--KKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 144 GQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-219 |
1.28e-27 |
|
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: 106.36 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMreIKKDIGMI---FQHFNLLNS 96
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IRAGIAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 ATVFKNVAMPLILSkkskkeitqrvtemlefvglsdkkdqfpdelsGGQKQRVAIARALVTNPKILLCDEATSALDPATT 176
Cdd:cd03215 93 LSVAENIALSSLLS--------------------------------GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1109734267 177 ASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:cd03215 141 AEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-220 |
2.38e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.27 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDY-SEKAMRE 79
Cdd:PRK11614 5 MLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 ikkDIGMIFQHFNLLNSATVFKNVAMPLILSkkSKKEITQRVTEMLE-FVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK11614 81 ---AVAIVPEGRRVFSRMTVEENLAMGGFFA--ERDQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 159 PKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
3.89e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.12 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS--EKAMR 78
Cdd:COG4559 1 MLEAENLSVRLGGRT----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 eikkdIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV-- 156
Cdd:COG4559 77 -----RAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 157 -----TNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHemcvikDI------CNRVAVMEKGQVVETGTV 225
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLH------DLnlaaqyADRILLLHQGRLVAQGTP 224
|
....*
gi 1109734267 226 TDVFS 230
Cdd:COG4559 225 EEVLT 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-234 |
7.85e-27 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 107.97 E-value: 7.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEA----ASSGQVIVDGHDITDYSEKA 76
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 77 MRE-IKKDIGMIFQH-FNLLNSATVFKNVAMPLILSKKSKKEITQRV-------TEMLEFVGLSDKKD---QFPDELSGG 144
Cdd:PRK15093 83 RRKlVGHNVSMIFQEpQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFgwrkrraIELLHRVGIKDHKDamrSFPYELTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 145 QKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
250
....*....|...
gi 1109734267 225 VTDVFS---HPKT 234
Cdd:PRK15093 243 SKELVTtphHPYT 255
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
1.70e-26 |
|
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: 109.68 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNsATVFKNVAmpLILSKKSKKEITQ--RVTEMLEFV-----GLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:TIGR02857 396 DQIAWVPQHPFLFA-GTIAENIR--LARPDASDAEIREalERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1109734267 155 LVTNPKILLCDEATSALDPATTASILALLKNVNQtfGITIMIITH 199
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTH 515
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-223 |
5.35e-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: 102.01 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSktFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYsEKAMREIk 81
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kdIGMIFQHFNLLNsATVFKNVAMPLilskkskkeitqrvtemlefvglsdkkdqfpdelSGGQKQRVAIARALVTNPKI 161
Cdd:cd03247 77 --ISVLNQRPYLFD-TTLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 162 LLCDEATSALDPATTASILALLknVNQTFGITIMIITHEMCVIKDIcNRVAVMEKGQVVETG 223
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-223 |
4.50e-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: 100.81 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLV-----RLVNHleAASSGQVIVDGhditdySEKAM 77
Cdd:cd03234 5 PWWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLdaisgRVEGG--GTTSGQILFNG------QPRKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 REIKKDIGMIFQHFNLLNSATVFKNVAMPLILS---KKSKKEITQRV-TEMLEFVGLSDKKDQFPDELSGGQKQRVAIAR 153
Cdd:cd03234 77 DQFQKCVAYVRQDDILLPGLTVRETLTYTAILRlprKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 154 ALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
6.47e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 105.57 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSktFNKKKQKIhALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReik 81
Cdd:PRK10790 341 IDIDNVS--FAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLnSATVFKNVAMPLILSKkskkeitQRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVA 150
Cdd:PRK10790 415 QGVAMVQQDPVVL-ADTFLANVTLGRDISE-------EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 151 IARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfgITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-224 |
8.26e-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: 105.21 E-value: 8.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReikkdigmifQHFNLLN---- 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR----------QFINYLPqepy 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 96 --SATVFKNvampLILSKKSKKEItQRVTEMLEFVGLSDKKDQFP-----------DELSGGQKQRVAIARALVTNPKIL 162
Cdd:TIGR01193 559 ifSGSILEN----LLLGAKENVSQ-DEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 163 LCDEATSALDPATTASILALLKNVNQTfgiTIMIITHEMCVIKDIcNRVAVMEKGQVVETGT 224
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
31-224 |
2.17e-24 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 104.33 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 31 NAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdysEKAMREIKKDIGMIFQHFNLLNSATVFKNVAMPLILS 110
Cdd:TIGR01257 956 NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 111 KKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLknVNQTF 190
Cdd:TIGR01257 1032 GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
170 180 190
....*....|....*....|....*....|....
gi 1109734267 191 GITIMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:TIGR01257 1110 GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-224 |
2.33e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.86 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIF-------------GVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMreiKKDIGM 86
Cdd:PRK10575 13 ALRNVSFRVPGRTLLhplsltfpagkvtGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF---ARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 87 IFQHFNLLNSATVFKNVAM---PL--ILSKKSKKEiTQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIgryPWhgALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGT 224
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-199 |
3.63e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 102.82 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIkkdIGMIFQHFNLLnSATV 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQDAHLF-DTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNVAMplilskkSKKEIT-QRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:TIGR02868 426 RENLRL-------ARPDATdEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|..
gi 1109734267 168 TSALDPATTASILALLKNVNQtfGITIMIITH 199
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-224 |
3.80e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 103.28 E-value: 3.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQV-----IVDGHDItdysekamrEIKKDIGMIFQHFNLL 94
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDI---------ATRRRVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 95 NSATVFKNvampLILSKK----SKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:NF033858 352 GELTVRQN----LELHARlfhlPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 171 LDPATTASILALLKNVNQTFGITIMIITHEMcvikdiCNRVAVMEKGQVVETGT 224
Cdd:NF033858 428 VDPVARDMFWRLLIELSREDGVTIFISTHFMnea-erCDRISLMHAGRVLASDT 480
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-252 |
5.33e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 5.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 15 KQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkamREIKKDIGMIFQHFNLL 94
Cdd:PRK11231 14 TKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQHHLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 95 NSATVFKNVAM---P-LILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK11231 89 EGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 171 LDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFShpKTTIAQNF-VSTVIQTEP 249
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT--PGLLRTVFdVEAEIHPEP 245
|
...
gi 1109734267 250 SSQ 252
Cdd:PRK11231 246 VSG 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-222 |
1.89e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.76 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAmrEIKK 82
Cdd:PRK11288 6 SFDGIGKTFPGVK----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--ALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMIFQHFNLLNSATVFKNV---AMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK11288 80 GVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVET 222
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
36-230 |
5.70e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.21 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 36 VIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKamrEIKKDIGMIFQHFNLLNSATVFKNVA------MPLIl 109
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK---EVARRIGLLAQNATTPGDITVQELVArgryphQPLF- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 110 sKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQT 189
Cdd:PRK10253 114 -TRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNRE 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1109734267 190 FGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK10253 193 KGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-221 |
7.79e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 94.64 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKK--KQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:COG2401 26 RVAIVLEAFGVElrVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkdigmifqhfnllnsatvfknvamplILSKKSKKEitqrVTEMLEFVGLSD-----KKdqfPDELSGGQKQRVAIARAL 155
Cdd:COG2401 106 ---------------------------IGRKGDFKD----AVELLNAVGLSDavlwlRR---FKELSTGQKFRFRLALLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 156 VTNPKILLCDEATSALDPaTTASILAL-LKNVNQTFGITIMIITHEMCVIKDIC-NRVAVMEKGQVVE 221
Cdd:COG2401 152 AERPKLLVIDEFCSHLDR-QTAKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-249 |
2.62e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkamREI 80
Cdd:PRK09536 3 MIDVSDLSVEFGD----TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLLNSATVFKNVAM---PLiLSKKSKKEITQR--VTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARAL 155
Cdd:PRK09536 76 SRRVASVPQDTSLSFEFDVRQVVEMgrtPH-RSRFDTWTETDRaaVERAMERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSHPktT 235
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD--T 231
|
250
....*....|....*
gi 1109734267 236 IAQNF-VSTVIQTEP 249
Cdd:PRK09536 232 LRAAFdARTAVGTDP 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-200 |
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 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReikKDIGMIFQHFNLLNSaTVF 100
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---QQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAMPLILSKKSKKEitQRVTEMLEFVGLSDKKDQFP-DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK10247 99 DNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|.
gi 1109734267 180 LALLKNVNQTFGITIMIITHE 200
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHD 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-227 |
6.15e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKQkihaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVdGHDITdysekamrei 80
Cdd:COG0488 315 VLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkdIGMIFQHFNLLN-SATVFKNVAmpLILSKKSKKEITQRVTEMLeFVGlsDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:COG0488 380 ---IGYFDQHQEELDpDKTVLDELR--DGAPGGTEQEVRGYLGRFL-FSG--DDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNvnqtFGITIMIITHEMCVIKDICNRVAVMEKGQVVE-TGTVTD 227
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDD----FPGTVLLVSHDRYFLDRVATRILEFEDGGVREyPGGYDD 516
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
8.55e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 8.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 4 FRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGhDITdysekamreikkd 83
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 84 IGMIFQHFNLLNSATVFKNVAM---PLILSKKSKKEITQ-----------------------------RVTEMLEFVGLS 131
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVLDgdaELRALEAELEELEAklaepdedlerlaelqeefealggweaeaRAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 132 DKKDQFP-DELSGGQKQRVAIARALVTNPKILLCDEATSALDpatTASILAL---LKNvnqtFGITIMIITHemcvikD- 206
Cdd:COG0488 143 EEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLeefLKN----YPGTVLVVSH------Dr 209
|
250
....*....|....*...
gi 1109734267 207 -----ICNRVAVMEKGQV 219
Cdd:COG0488 210 yfldrVATRILELDRGKL 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-220 |
9.44e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.86 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMreIKKDIGM---------IFQ 89
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA--IRAGIAYvpedrkgegLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 90 HFNLLN--SATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDkkDQFPDELSGGQKQRVAIARALVTNPKILLCDEA 167
Cdd:COG1129 344 DLSIREniTLASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSP--EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 168 TSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-231 |
4.90e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKkkqkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS-EKAMre 79
Cdd:PRK15439 11 LLCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAH-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 iKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMlefvGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PRK15439 85 -QLGIYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAAL----GCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTvTDVFSH 231
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGK-TADLST 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-220 |
8.74e-21 |
|
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: 88.47 E-value: 8.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 4 FRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLE--AASSGQVIVDGHDITDYSEKAMREI 80
Cdd:cd03233 6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKaLANRTEgnVSVEGDIHYNGIPYKEFAEKYPGEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkdigmIFqhfnllNSAtvfKNVAMPLILskkskkeitqrVTEMLEFVgLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:cd03233 86 ------IY------VSE---EDVHFPTLT-----------VRETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCV-IKDICNRVAVMEKGQVV 220
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQI 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-222 |
9.34e-21 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 92.97 E-value: 9.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVN--HLEAASSGQVIVDGHDItdySEKAMR 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvYPHGTWDGEIYWSGSPL---KASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSKK----EITQRVTEMLEFVGLSDKKDQFP-DELSGGQKQRVAIA 152
Cdd:TIGR02633 74 DTeRAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRmaynAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVET 222
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-230 |
1.42e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdysEKAMReiKKDIGMIFQH------FNL 93
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT----RQALQ--KNLVAYVPQSeevdwsFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 94 LNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDP 173
Cdd:PRK15056 96 LVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 174 ATTASILALLKNVNQTfGITIMIITHEMCVIKDICNrVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-222 |
2.39e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.53 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVN--HLEAASSGQVIVDGHDITDYSekaMR 78
Cdd:PRK13549 5 LLEMKNITKTFGGVK----ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgvYPHGTYEGEIIFEGEELQASN---IR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EI-KKDIGMIFQHFNLLNSATVFKNVAMPLILSKKSK---KEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARA 154
Cdd:PRK13549 78 DTeRAGIAIIHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 155 LVTNPKILLCDEATSALDPATTASILALLKNVnQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVET 222
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-224 |
4.53e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 91.72 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKS----TLVRLVnHLEaasSGQVIVDGHDItdySEKAMREIKKDIGMIFQ------- 89
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIV-ELE---RGRILIDGCDI---SKFGLMDLRKVLGIIPQapvlfsg 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 90 --HFNL-----LNSATVFKNvampliLSKKSKKEITQRVTemlefVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKIL 162
Cdd:PLN03130 1328 tvRFNLdpfneHNDADLWES------LERAHLKDVIRRNS-----LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKIL 1396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 163 LCDEATSALDPATTASIlalLKNVNQTF-GITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:PLN03130 1397 VLDEATAAVDVRTDALI---QKTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDT 1455
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-183 |
8.21e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.38 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSekaMREIKKDIGmifqHFNLLNSA-TV 99
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHYLG----HRNAMKPAlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNvampLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK13539 91 AEN----LEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
....
gi 1109734267 180 LALL 183
Cdd:PRK13539 167 AELI 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-257 |
1.25e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 87.34 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYsekAMREIKKDIGMIFQHfNLLNSATVF 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRRVLSIIPQS-PVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAmPLilSKKSKKEITqrvtEMLEFVGLSDKKDQFP-----------DELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PLN03232 1328 FNID-PF--SEHNDADLW----EALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 170 ALDPATTASIlalLKNVNQTF-GITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTDVFSHPKTTiaqnFVSTVIQTE 248
Cdd:PLN03232 1401 SVDVRTDSLI---QRTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSA----FFRMVHSTG 1472
|
250
....*....|
gi 1109734267 249 PS-SQLLQNL 257
Cdd:PLN03232 1473 PAnAQYLSNL 1482
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-230 |
2.02e-18 |
|
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: 86.54 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIhaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYsekAMREIK 81
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLR 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHfNLLNSATVFKNVAmPLilSKKSKKEI--TQRVTEMLEFV-GLSDKKDQFPDE----LSGGQKQRVAIARA 154
Cdd:TIGR00957 1360 FKITIIPQD-PVLFSGSLRMNLD-PF--SQYSDEEVwwALELAHLKTFVsALPDKLDHECAEggenLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 155 LVTNPKILLCDEATSALDPATTASILALLKnvNQTFGITIMIITHEMCVIKDIcNRVAVMEKGQVVETGTVTDVFS 230
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-233 |
2.30e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.61 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKKkqkihaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEkaMREIKK 82
Cdd:PRK09700 267 EVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMI---------FQHFNLLNSATVFKNV-------AMPLILSKKSKKeITQRVTEMLEFVGLSdkKDQFPDELSGGQK 146
Cdd:PRK09700 339 GMAYItesrrdngfFPNFSIAQNMAISRSLkdggykgAMGLFHEVDEQR-TAENQRELLALKCHS--VNQNITELSGGNQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 147 QRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVT 226
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
|
....*..
gi 1109734267 227 DVFSHPK 233
Cdd:PRK09700 495 DDMSEEE 501
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-222 |
3.55e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.23 E-value: 3.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASS--GQVIVDG-----HDITDyS 73
Cdd:NF040905 1 ILEMRGITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRD-S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 74 EKamreikKDIGMIFQHFNLLNSATVFKNvampLILSKKSKK-------EITQRVTEMLEFVGLSDKKDQFPDELSGGQK 146
Cdd:NF040905 76 EA------LGIVIIHQELALIPYLSIAEN----IFLGNERAKrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 147 QRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVET 222
Cdd:NF040905 146 QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-219 |
1.14e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 22 KDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAmreiKKDIGMIF-----QHFNLLNS 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 ATVFKNVA------MPLILSKKSKKEITQRVTEMLEfVGLSDKkDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PRK15439 356 APLAWNVCalthnrRGFWIKPARENAVLERYRRALN-IKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1109734267 171 LDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-220 |
1.15e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREikkdIGMIF-----QHFNLL 94
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR----LGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 95 NSATVFKNVAMPLILSKK-------SKKEITQRVTEMLEfvglsdkkdQF----PDE------LSGGQKQRVAIARALVT 157
Cdd:COG3845 349 PDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIE---------EFdvrtPGPdtparsLSGGNQQKVILARELSR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 158 NPKILLCDEATSALDPATTASILALLKNV-NQtfGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELrDA--GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-218 |
1.25e-17 |
|
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: 79.82 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIH-ALKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAaSSGQVIVDGHdITDYSEKAMre 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS-IAYVSQEPW-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 80 ikkdigmifqhfnlLNSATVFKNVAMplilskkSKKEITQRVTEMLEFVGLSDKKDQFPD-------E----LSGGQKQR 148
Cdd:cd03250 77 --------------IQNGTIRENILF-------GKPFDEERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 149 VAIARALVTNPKILLCDEATSALDPATTASIL------ALLKNVnqtfgiTIMIITHEMCVIKDiCNRVAVMEKGQ 218
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFencilgLLLNNK------TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
119-199 |
1.26e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 119 QRVTEMLEFVGLSDKKDQFPDE------LSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKnvNQTFGI 192
Cdd:COG4178 458 AELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGT 535
|
....*..
gi 1109734267 193 TIMIITH 199
Cdd:COG4178 536 TVISVGH 542
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-239 |
1.94e-17 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.54 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQkIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIV-DGHDITDYSEKAMREi 80
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS- 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kkDIGMIFQHfNLLNSATVFKNVAMPLI-------LSKKSKKEI--------------------------TQRVTEMLE- 126
Cdd:PTZ00265 461 --KIGVVSQD-PLLFSNSIKNNIKYSLYslkdleaLSNYYNEDGndsqenknkrnscrakcagdlndmsnTTDSNELIEm 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 127 -----------------------FV-GLSDKKDQF----PDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTAS 178
Cdd:PTZ00265 538 rknyqtikdsevvdvskkvlihdFVsALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 179 ILALLKNVNQTFGITIMIITHEMCVIKdICNRVAVMEKGQVVETGTVTDVFSHPKTTIAQN 239
Cdd:PTZ00265 618 VQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLSNRERGSTVDVDIIGEDPTKDNKEN 677
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-218 |
2.72e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 77.49 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGqvivdghditdysekamrEIK 81
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG------------------IVT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFnllnsatvfknvamplilskkskkeitqrvtemlefvglsdkkdqfpDELSGGQKQRVAIARALVTNPKI 161
Cdd:cd03221 59 WGSTVKIGYF-----------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 162 LLCDEATSALDPATTASILALLKNvnqtFGITIMIITHEMCVIKDICNRVAVMEKGQ 218
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE----YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-224 |
2.87e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 82.59 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 24 VSFKVNRNAIFGVIGYSGAGKSTLVrlvNHLE--AASSGQVIVDGHDITDYSEKAMReikKDIGMIFQHFNLLNsATVFK 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELRELDPESWR---KHLSWVGQNPQLPH-GTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 102 NVAMplilskkSKKEIT-QRVTEMLEFVGLSDKKDQFPD-----------ELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK11174 442 NVLL-------GNPDASdEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 170 ALDPATTASILALLKNV--NQTfgiTIMiITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:PRK11174 515 SLDAHSEQLVMQALNAAsrRQT---TLM-VTHQLEDLAQ-WDQIWVMQDGQIVQQGD 566
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-224 |
2.88e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 82.45 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 9 KTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMReikKDIGMIF 88
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR---SRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 89 QHfNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLE-FVGLSDKKDQFPDE----LSGGQKQRVAIARALVTNPKILL 163
Cdd:PRK10789 396 QT-PFLFSDTVANNIALGRPDATQQEIEHVARLASVHDdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 164 CDEATSALDPATTASILALLKNVNQtfGITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGN 532
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-199 |
3.85e-17 |
|
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: 77.58 E-value: 3.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDitdysekamreikkdiGMIFqhfnllnsatvf 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------------DLLF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 knvamplilskkskkeITQRvtemlEFVGLSDKKDQ--FP--DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATT 176
Cdd:cd03223 69 ----------------LPQR-----PYLPLGTLREQliYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 1109734267 177 ASILALLKnvnqTFGITIMIITH 199
Cdd:cd03223 128 DRLYQLLK----ELGITVISVGH 146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-227 |
4.34e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREi 80
Cdd:PRK10762 4 LLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 kKDIGMIFQHFNLLNSATVFKNV--------AMPLILSKKskkeITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIA 152
Cdd:PRK10762 79 -AGIGIIHQELNLIPQLTIAENIflgrefvnRFGRIDWKK----MYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 153 RALVTNPKILLCDEATSALDPATTASILALLKNVnQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTD 227
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
11-231 |
1.44e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 80.32 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 11 FNKKKQKIH-ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVivdghditdysekamrEIKKDIGMIFQ 89
Cdd:PRK13545 29 FRSKDGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------------DIKGSAALIAI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 90 HFNLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:PRK13545 93 SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 170 ALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSH 231
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-258 |
2.64e-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: 80.44 E-value: 2.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 34 FGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITdyseKAMREIKKDIGMIFQHFNLLNSATVFKNVAMPLILSKKS 113
Cdd:TIGR01257 1968 FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL----TNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 114 KKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGIT 193
Cdd:TIGR01257 2044 AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRA 2122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 194 IMIITHEMCVIKDICNRVAVMEKGQVVETGTVtdvfSHPKTTIAQNFVSTVIQTEPSSQLLQNLN 258
Cdd:TIGR01257 2123 VVLTSHSMEECEALCTRLAIMVKGAFQCLGTI----QHLKSKFGDGYIVTMKIKSPKDDLLPDLN 2183
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-219 |
3.34e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKA--------MREIKKDIGMIFqhfn 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRDGLVL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 llnSATVFKNVAMPLI--LSKKS----KKEITQRVTEmleFVGLSDKK----DQFPDELSGGQKQRVAIARALVTNPKIL 162
Cdd:PRK10762 344 ---GMSVKENMSLTALryFSRAGgslkHADEQQAVSD---FIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 163 LCDEATSALDPATTASILALlknVNQtF---GITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQL---INQ-FkaeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
58-205 |
3.38e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.07 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 58 SSGQVIVDGHDITDYSEKAMREIkkdIGMIFQHFNLLNsATVFKNVAMPlilSKKSKKEITQRVTEML---EFV-GLSDK 133
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNL---FSIVSQEPMLFN-MSIYENIKFG---KEDATREDVKRACKFAaidEFIeSLPNK 1347
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 134 KDQ----FPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIK 205
Cdd:PTZ00265 1348 YDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-223 |
3.60e-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: 75.64 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEA--ASSGQVIVDGHDITDYS--EKAmreiKKDIGMIFQHfnllns 96
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPpeERA----RLGIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 atvfkNVAMPLIlskkskkeitqRVTEMLEFVGLSdkkdqfpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDpatt 176
Cdd:cd03217 86 -----PPEIPGV-----------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD---- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 177 ASILALLKNVNQTF---GITIMIITHEMCVIKDI-CNRVAVMEKGQVVETG 223
Cdd:cd03217 137 IDALRLVAEVINKLreeGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-201 |
4.55e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIvdghditdysekamREI 80
Cdd:PRK09544 4 LVSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQHFNLlnSATVFKNVAMPLILSKKSKKeitQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPK 160
Cdd:PRK09544 66 KLRIGYVPQKLYL--DTTLPLTVNRFLRLRPGTKK---EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1109734267 161 ILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEM 201
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-219 |
2.19e-15 |
|
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: 75.28 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTL----VRLVNhleaaSSGQVIVDGhdiTDYSEKAMREIKKDIGMIFQHFNLLnS 96
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDG---VSWNSVPLQKWRKAFGVIPQKVFIF-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 ATVFKNvampLILSKKSKKEITQRVTEMlefVGLSDKKDQFPDEL-----------SGGQKQRVAIARALVTNPKILLCD 165
Cdd:cd03289 91 GTFRKN----LDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 166 EATSALDPATTASILALLKnvnQTF-GITIMIITHEMCVIKDiCNRVAVMEKGQV 219
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLK---QAFaDCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-219 |
2.70e-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: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 17 KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAASSGQVIVDGHDITdySEKAMREIKKDIGMI---FQHFN 92
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRNPAQAIRAGIAMVpedRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 93 LLNSATVFKNVAMPLI--LSKKSKKEITQRVTEMLEFVGLSDKKDQFPD----ELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:TIGR02633 350 IVPILGVGKNITLSVLksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 167 ATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-230 |
2.90e-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: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLvrlvnhLEAAS-----SGQVIVDGHDITDYSEKAMREIKkdiGMIFQHfnlln 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL------LARMAgllpgQGEILLNGRPLSDWSAAELARHR---AYLSQQ----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 96 SATVFknvAMP----LIL---SKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALV-----TNP--KI 161
Cdd:COG4138 78 QSPPF---AMPvfqyLALhqpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTfGITIMIITHemcvikDI------CNRVAVMEKGQVVETGTVTDVFS 230
Cdd:COG4138 155 LLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSH------DLnhtlrhADRVWLLKQGKLVASGETAEVMT 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-219 |
3.09e-15 |
|
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: 76.87 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLeAASSGQVIVDGhdiTDYSEKAMREIKKDIGMIFQHFNLLnSATVF 100
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDG---VSWNSVTLQTWRKAFGVIPQKVFIF-SGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAmPLilSKKSKKEItQRVTEMlefVGLSDKKDQFPDEL-----------SGGQKQRVAIARALVTNPKILLCDEATS 169
Cdd:TIGR01271 1310 KNLD-PY--EQWSDEEI-WKVAEE---VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 170 ALDPATTASILALLKnvnQTFG-ITIMIITHEMCVIKDiCNRVAVMEKGQV 219
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLK---QSFSnCTVILSEHRVEALLE-CQQFLVIEGSSV 1429
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-231 |
5.94e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 73.70 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 12 NKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGhditdysekamreikkDIGMIFQHF 91
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 92 NLLNSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSAL 171
Cdd:PRK13546 95 GLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 172 DPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFSH 231
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-200 |
6.59e-15 |
|
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: 75.36 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 7 VSKTFNKKKqkiHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRlvnhleaassgqvIVDGHDiTDYSEKAMREIKKDIGM 86
Cdd:TIGR03719 10 VSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVD-KDFNGEARPQPGIKVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 87 IFQHFNLLNSATVFKNVAMPLilskKSKKEITQRVTE-MLEFVGLSDKKDQFPDE------------------------- 140
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEEGV----AEIKDALDRFNEiSAKYAEPDADFDKLAAEqaelqeiidaadawdldsqleiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 141 -------------LSGGQKQRVAIARALVTNPKILLCDEATSALDpattASILALLKNVNQTFGITIMIITHE 200
Cdd:TIGR03719 149 alrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-200 |
8.06e-15 |
|
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: 75.36 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVdGHDItdysekamreik 81
Cdd:TIGR03719 323 IEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kDIGMIFQ-HFNLLNSATVFKNVAMPLILSKKSKKEITQRVtemleFVGLSDKK--DQ--FPDELSGGQKQRVAIARALV 156
Cdd:TIGR03719 386 -KLAYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRFNFKgsDQqkKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1109734267 157 TNPKILLCDEATSALDPATtasiLALLKNVNQTFGITIMIITHE 200
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVET----LRALEEALLNFAGCAVVISHD 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-227 |
8.51e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.15 E-value: 8.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 7 VSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREikKDIGM 86
Cdd:PRK10982 4 ISKSFPGVK----ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 87 IFQHFNLLNSATVFKNVAM-------PLILSKKSKKEiTQRVTEMLEFVglSDKKDQFPDeLSGGQKQRVAIARALVTNP 159
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLgryptkgMFVDQDKMYRD-TKAIFDELDID--IDPRAKVAT-LSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 160 KILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTD 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 |
1.97e-14 |
|
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: 70.85 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 24 VSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIKKdIGmifqHFNLLNSA-TVFKN 102
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILY-LG----HLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 103 VAMPLILSKKSKKEITqrvtEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILAL 182
Cdd:TIGR01189 94 LHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGL 169
|
170
....*....|....*..
gi 1109734267 183 LKNVNQTFGITIMiITH 199
Cdd:TIGR01189 170 LRAHLARGGIVLL-TTH 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-224 |
4.90e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.27 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYsekAMREIKKDIGMIFQHfNLLNSATVF 100
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY---GLRELRRQFSMIPQD-PVLFDGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAmPliLSKKSKKEitqrVTEMLEFVGL-------SDKKDQFPDE----LSGGQKQRVAIARALVT-NPKILLCDEAT 168
Cdd:PTZ00243 1402 QNVD-P--FLEASSAE----VWAALELVGLrervaseSEGIDSRVLEggsnYSVGQRQLMCMARALLKkGSGFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 169 SALDPATTASILAllkNVNQTF-GITIMIITHEMCVIKDiCNRVAVMEKGQVVETGT 224
Cdd:PTZ00243 1475 ANIDPALDRQIQA---TVMSAFsAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGS 1527
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-219 |
1.85e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.11 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 12 NKKKQKIHalkDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAASSGQVIVDGHDITDYS-EKAMR-------EIKK 82
Cdd:PRK13549 272 NPHIKRVD---DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNpQQAIAqgiamvpEDRK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMIFQhfnllnsATVFKNVAMPlILSKKSK-------KEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARAL 155
Cdd:PRK13549 349 RDGIVPV-------MGVGKNITLA-ALDRFTGgsriddaAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-231 |
3.02e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.39 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVskTFNKKKQKIhALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDyseKAMREIK 81
Cdd:PRK10522 323 LELRNV--TFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQHFNLLNSatvfknvamplILSKKSKKEITQRVTEMLEFVGLSDKKD----QFPD-ELSGGQKQRVAIARALV 156
Cdd:PRK10522 397 KLFSAVFTDFHLFDQ-----------LLGPEGKPANPALVEKWLERLKMAHKLEledgRISNlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109734267 157 TNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIkDICNRVAVMEKGQVVE-TGTVTDVFSH 231
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
37-220 |
1.28e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 37 IGYSGAGKSTLVRLVNHLEAASSGQVIVDG-------------------------------------HDI-----TDYSE 74
Cdd:PRK11147 35 VGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdpprnvegtvydfvaegieeqaeylkryHDIshlveTDPSE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 75 KAMREIKKdIGMIFQHFNL--LNSatvfknvamplilskkskkeitqRVTEMLEFVGLSdkkdqfPD----ELSGGQKQR 148
Cdd:PRK11147 115 KNLNELAK-LQEQLDHHNLwqLEN-----------------------RINEVLAQLGLD------PDaalsSLSGGWLRK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 149 VAIARALVTNPKILLCDEATSALDPATTASILALLKNvnqtFGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
24-199 |
1.98e-12 |
|
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: 65.21 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 24 VSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIkkdigMIFQHFNLLNSA-TVFKN 102
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-----LYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 103 vampliLSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILAL 182
Cdd:cd03231 94 ------LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*..
gi 1109734267 183 LKNVNQTFGITIMiITH 199
Cdd:cd03231 168 MAGHCARGGMVVL-TTH 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-199 |
2.65e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVdGHDItdysekamreik 81
Cdd:PRK11819 325 IEAENLSKSFGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------------ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 kDIGMIFQ-HFNLLNSATVFKNVAMPLILSKKSKKEITQRVtemleFVGLSDKK--DQ--FPDELSGGQKQRVAIARALV 156
Cdd:PRK11819 388 -KLAYVDQsRDALDPNKTVWEEISGGLDIIKVGNREIPSRA-----YVGRFNFKggDQqkKVGVLSGGERNRLHLAKTLK 461
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1109734267 157 TNPKILLCDEATSALDPATtasiLALLKNVNQTFGITIMIITH 199
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDVET----LRALEEALLEFPGCAVVISH 500
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-220 |
3.82e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 24 VSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEK-AMR-------EIKKDIGMIFQHfnlln 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdAIRagimlcpEDRKAEGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 96 saTVFKNVAMP---------LILSKKSKKEITQRVTEMLEFVGLSdkKDQFPDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:PRK11288 347 --SVADNINISarrhhlragCLINNRWEAENADRFIRSLNIKTPS--REQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 167 ATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-228 |
3.96e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 24 VSFKVNRNAIFGVIGYSGAGKSTLV-RLVNHLEaaSSGQVIVDGHDITDYSekaMREIKKDIGMIFQHFNLLNSATVFKN 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLLP--GSGSIQFAGQPLEAWS---AAELARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 103 VAMPLIlSKKSKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARAL-----VTNP--KILLCDEATSALDPAT 175
Cdd:PRK03695 90 LTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 176 TASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:PRK03695 169 QAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-226 |
7.66e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYS-EKAMR-------EIKKDIGmIFQH- 90
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINhgfalvtEERRSTG-IYAYl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 91 ---FN-LLNSATVFKNvAMPLILSKKSKKEiTQRVTEMLEFVGLSDKKDqfPDELSGGQKQRVAIARALVTNPKILLCDE 166
Cdd:PRK10982 342 digFNsLISNIRNYKN-KVGLLDNSRMKSD-TQWVIDSMRVKTPGHRTQ--IGSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109734267 167 ATSALDPATTASILALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQV---VETGTVT 226
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVagiVDTKTTT 479
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-243 |
1.73e-11 |
|
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: 63.39 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTL----VRLVNHLEaassGQVIVDGHDItdySEKAMREIKKDIGMIFQHfNLLNS 96
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDI---SKLPLHTLRSRLSIILQD-PILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 97 ATVFKNVamplilsKKSKKEITQRVTEMLEFVGLSDKKDQFP-----------DELSGGQKQRVAIARALVTNPKILLCD 165
Cdd:cd03288 109 GSIRFNL-------DPECKCTDDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 166 EATSALDPATTAsilALLKNVNQTFG-ITIMIITHEMCVIKDiCNRVAVMEKGQVVETGTVTDVFSHpKTTIAQNFVST 243
Cdd:cd03288 182 EATASIDMATEN---ILQKVVMTAFAdRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ-EDGVFASLVRT 255
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-173 |
2.01e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 17 KIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDysEKAMREIKKDIGMIFQHF--NLL 94
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRAVCPRIAYMPQGLgkNLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 95 NSATVFKNVAMPLILSKKSKKEITQRVTEMLEFVGLsdkkDQFPD----ELSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:NF033858 91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 166
|
...
gi 1109734267 171 LDP 173
Cdd:NF033858 167 VDP 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-215 |
2.32e-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: 62.81 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 28 VNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdySEKAmREIKKDIGMIFQHFnllnsatvfknvampl 107
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV---SYKP-QYIKADYEGTVRDL---------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 108 iLSKKSKKEIT--QRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDP----ATTASILA 181
Cdd:cd03237 82 -LSSITKDFYThpYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|....
gi 1109734267 182 LLKNVNQtfgiTIMIITHEMCVIKDICNRVAVME 215
Cdd:cd03237 161 FAENNEK----TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-199 |
5.08e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 7 VSKTFNKKKQkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRlvnhleaassgqvIVDGHDiTDYSEKAMREIKKDIGM 86
Cdd:PRK11819 12 VSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVD-KEFEGEARPAPGIKVGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 87 IFQHFNLLNSATVFKNVAMPLilskKSKKEITQRVTE-MLEFVGLSDKKDQFPDE------------------------- 140
Cdd:PRK11819 75 LPQEPQLDPEKTVRENVEEGV----AEVKAALDRFNEiYAAYAEPDADFDALAAEqgelqeiidaadawdldsqleiamd 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 141 -------------LSGGQKQRVAIARALVTNPKILLCDEATSALDpattASILALLKNVNQTFGITIMIITH 199
Cdd:PRK11819 151 alrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AESVAWLEQFLHDYPGTVVAVTH 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-226 |
2.99e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAAS--SGQVIVDGHDITDYsEKAMR 78
Cdd:CHL00131 7 ILEIKNLHASVNENE----ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDL-EPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EiKKDIGMIFQH-----------FNLL--NSATVFKNvampliLSKKSKKEITQRVTEMLEFVGLSDK------KDQFpd 139
Cdd:CHL00131 82 A-HLGIFLAFQYpieipgvsnadFLRLayNSKRKFQG------LPELDPLEFLEIINEKLKLVGMDPSflsrnvNEGF-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 140 elSGGQKQRVAIARALVTNPKILLCDEATSALDP---ATTASILALLKNVNQtfgiTIMIITHEMCVIKDIC-NRVAVME 215
Cdd:CHL00131 153 --SGGEKKRNEILQMALLDSELAILDETDSGLDIdalKIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQ 226
|
250
....*....|.
gi 1109734267 216 KGQVVETGTVT 226
Cdd:CHL00131 227 NGKIIKTGDAE 237
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-200 |
3.03e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 33 IFGVIGYSGAGKSTLVR-LVNHLEAAS-SGQVIVDGHDITdysekamREIKKDIGMIFQHFNLLNSATVFKNVA------ 104
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNRKPT-------KQILKRTGFVTQDDILYPHLTVRETLVfcsllr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 105 MPLILSKKSKKEITQRVTEMLefvGLSDKKD-----QFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISEL---GLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180
....*....|....*....|.
gi 1109734267 180 LALLKNVNQTfGITIMIITHE 200
Cdd:PLN03211 246 VLTLGSLAQK-GKTIVTSMHQ 265
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-223 |
3.48e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.28 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 9 KTFNKKKQKIHA-LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLV----NHLEAASSGQVIVDGHDITDYsekaMREIKKD 83
Cdd:TIGR00956 64 KLKKFRDTKTFDiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI----KKHYRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 84 IGMIFQ---HFNLLNSATVFKNVAM-------PLILSKKSKKEITQRVTemLEFVGLSDKKD-----QFPDELSGGQKQR 148
Cdd:TIGR00956 140 VVYNAEtdvHFPHLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVY--MATYGLSHTRNtkvgnDFVRGVSGGERKR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 149 VAIARALVTNPKILLCDEATSALDPATTASILALLKN----VNQTFGITIMIITHEmcvIKDICNRVAVMEKGQVVETG 223
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTsaniLDTTPLVAIYQCSQD---AYELFDKVIVLYEGYQIYFG 293
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-236 |
4.47e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 3 EFRQVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVrlvNHLEAASSGQVIVDGHDITDYSEKAmREIKK 82
Cdd:TIGR00956 761 HWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRLVNGRPLD-SSFQR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMIFQHFNLLNSATVFKNVA------MPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFPDE-LSGGQKQRVAIARAL 155
Cdd:TIGR00956 837 SIGYVQQQDLHLPTSTVRESLRfsaylrQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVEL 916
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 156 VTNPKILL-CDEATSALDPATTASILALLKNVNQTfGITIMIITHE-MCVIKDICNRVAVMEKG-QVVETGtvtDVFSHP 232
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQpSAILFEEFDRLLLLQKGgQTVYFG---DLGENS 992
|
....
gi 1109734267 233 KTTI 236
Cdd:TIGR00956 993 HTII 996
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
113-228 |
5.27e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 113 SKKEITQRVTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTfGI 192
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GA 195
|
90 100 110
....*....|....*....|....*....|....*.
gi 1109734267 193 TIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDV 228
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-173 |
8.79e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 20 ALKDVSFKVNRNAIFG-------------VIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDySEKA--------MR 78
Cdd:PRK13543 13 AAHALAFSRNEEPVFGpldfhvdageallVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR-GDRSrfmaylghLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 79 EIKKDIGMIfQHFNLLNSATVFKNVAMPlilskkskkeitqrvTEMLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTN 158
Cdd:PRK13543 92 GLKADLSTL-ENLHFLCGLHGRRAKQMP---------------GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....*
gi 1109734267 159 PKILLCDEATSALDP 173
Cdd:PRK13543 156 APLWLLDEPYANLDL 170
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-306 |
2.89e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 8 SKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAassgqviVDGHditdysekamREIKKDIGM 86
Cdd:TIGR00957 641 NATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-------VEGH----------VHMKGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 87 IFQHFNLLNSaTVFKNVAMPLILSKKSKKEITQRVTEM--LEFVGLSDKKD--QFPDELSGGQKQRVAIARALVTNPKIL 162
Cdd:TIGR00957 704 VPQQAWIQND-SLRENILFGKALNEKYYQQVLEACALLpdLEILPSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 163 LCDEATSALDPATTASIL-------ALLKNVnqtfgiTIMIITHEMCVIKDIcNRVAVMEKGQVVETGTVTDVFShpKTT 235
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFehvigpeGVLKNK------TRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ--RDG 853
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 236 IAQNFVSTVIQTEPSSQLLQNLNDKQVGDYRDYKLfIEETQLphpiVNDLIQIN-QGQVKILfSSMSEIQGK 306
Cdd:TIGR00957 854 AFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKL-IENGML----VTDVVGKQlQRQLSAS-SSDSGDQSR 919
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-206 |
4.39e-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: 54.69 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 30 RNAIFGVIGYSGAGKSTLVR-LVNHLEAASSGQVIVDGHDITDYSEKAMREIKKDIGMIfqhfnllnsatvfknvampli 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 109 lskkskkeitqrvtemlefvglsdkkdqfpdELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILAL-----L 183
Cdd:smart00382 60 -------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180
....*....|....*....|...
gi 1109734267 184 KNVNQTFGITIMIITHEMCVIKD 206
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-173 |
6.95e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKqkihALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLV--NHLEAAS-----------SGQVIVDghd 68
Cdd:PRK10938 261 IVLNNGVVSYNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgDHPQGYSndltlfgrrrgSGETIWD--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 69 itdysekamreIKKDIGMIFQ--HFNLLNSATVfKNVamplILS---------KKSKKEITQRVTEMLEFVGLSDKKDQF 137
Cdd:PRK10938 334 -----------IKKHIGYVSSslHLDYRVSTSV-RNV----ILSgffdsigiyQAVSDRQQKLAQQWLDILGIDKRTADA 397
|
170 180 190
....*....|....*....|....*....|....*..
gi 1109734267 138 P-DELSGGQKQRVAIARALVTNPKILLCDEATSALDP 173
Cdd:PRK10938 398 PfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-199 |
8.51e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.81 E-value: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 23 DVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdyseKAMREIKKD----IGmifqHFNLLNSA- 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----RRQRDEYHQdllyLG----HQPGIKTEl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNVAMPLILSKKSKKEITQRVtemLEFVGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTA 177
Cdd:PRK13538 90 TALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|..
gi 1109734267 178 SILALLKNVNQTFGITIMiITH 199
Cdd:PRK13538 167 RLEALLAQHAEQGGMVIL-TTH 187
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-201 |
1.08e-08 |
|
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: 54.64 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 6 QVSKTFNKKKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREIKK-DI 84
Cdd:cd03290 2 QVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 85 GMIFQHFNLLNsATVFKNVAMPLILSKKSKKEIT-----QRVTEMLEFvGLSDKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:cd03290 82 AYAAQKPWLLN-ATVEENITFGSPFNKQRYKAVTdacslQPDIDLLPF-GDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1109734267 160 KILLCDEATSALDPATT-----ASILALLKNVNQtfgiTIMIITHEM 201
Cdd:cd03290 160 NIVFLDDPFSALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKL 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
15-172 |
2.49e-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: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 15 KQKIHALKDVSFKVNR------NAIFGVIGYSGAGKSTLVRLV---------NHLEAASSGQVI--VDGHDITDYSEKaM 77
Cdd:cd03236 4 DEPVHRYGPNSFKLHRlpvpreGQVLGLVGPNGIGKSTALKILagklkpnlgKFDDPPDWDEILdeFRGSELQNYFTK-L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 78 REIKKDIGMIFQHFNLLNSAtvFKNVAMpLILSKKSKKEITQRVTEMLEFVGLSDKKdqfPDELSGGQKQRVAIARALVT 157
Cdd:cd03236 83 LEGDVKVIVKPQYVDLIPKA--VKGKVG-ELLKKKDERGKLDELVDQLELRHVLDRN---IDQLSGGELQRVAIAAALAR 156
|
170
....*....|....*
gi 1109734267 158 NPKILLCDEATSALD 172
Cdd:cd03236 157 DADFYFFDEPSSYLD 171
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
139-205 |
2.57e-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: 2.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 139 DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNvnqtFGITIMIITHEMCVIK 205
Cdd:TIGR00954 581 DVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE----FGITLFSVSHRKSLWK 643
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-230 |
3.90e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 25 SFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLeAASSGQVIVDGHDITDYSekaMREIKKDIGMIFQHFN--LLNSATV-F 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARaLAGEL-PLLSGERQSQFSHITRLS---FEQLQKLVSDEWQRNNtdMLSPGEDdT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAMPLILSKKSKKEITQRVTEMLEFVGLSDKKDQFpdeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASIL 180
Cdd:PRK10938 99 GRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1109734267 181 ALLKNVNQTfGITIMIITHEMCVIKDICNRVAVMEKGQVVETGTVTDVFS 230
Cdd:PRK10938 176 ELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-215 |
5.34e-08 |
|
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: 54.41 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 2 IEFRQVSKTFNKKKQKIHAlkdvsFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDghdiTDYSEKAmREIK 81
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEG-----GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----LKISYKP-QYIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 82 KDIGMIFQhfnllnsaTVFKNVAMPLILSKKSKKEITQRVtemlefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKI 161
Cdd:COG1245 412 PDYDGTVE--------EFLRSANTDDFGSSYYKTEIIKPL-------GLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 162 LLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAVME 215
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
141-228 |
1.39e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.14 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 141 LSGGQKQRVAIARAL---------VTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRV 211
Cdd:PRK13547 146 LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI 225
|
90
....*....|....*..
gi 1109734267 212 AVMEKGQVVETGTVTDV 228
Cdd:PRK13547 226 AMLADGAIVAHGAPADV 242
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
14-205 |
2.71e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.01 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 14 KKQKIHALKDVSFKVNRNAIFGVIGYSGAGKSTLVrlvnhLEaassgqvivdghdiTDYSEKAMREIKkdigmifqhfnl 93
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NE--------------GLYASGKARLIS------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 94 lnsaTVFKNVAMPLILSKKskkeiTQRVTEM-LEFVGLsdkkDQFPDELSGGQKQRVAIARALVTNPK--ILLCDEATSA 170
Cdd:cd03238 53 ----FLPKFSRNKLIFIDQ-----LQFLIDVgLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190
....*....|....*....|....*....|....*
gi 1109734267 171 LDPATTASILALLKNVNQTfGITIMIITHEMCVIK 205
Cdd:cd03238 120 LHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLS 153
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
4.42e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDItdysEKAMREIKKDIGMIFQHFNLLNSATVF 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAMPLILSKKSKKeitqrVTEMLEFVGLSDKKDqFP-DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASI 179
Cdd:PRK13540 93 ENCLYDIHFSPGAVG-----ITELCRLFSLEHLID-YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|.
gi 1109734267 180 LALLKNvNQTFGITIMIITHE 200
Cdd:PRK13540 167 ITKIQE-HRAKGGAVLLTSHQ 186
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-229 |
5.29e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAASSGQVIVDGHdiTDYSEKamreikkdIGMIFqhfnllnSATV 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS--VAYVPQ--------VSWIF-------NATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNVAMplilskKSKKEiTQRVTEMLEFVGLSDKKDQFPDE-----------LSGGQKQRVAIARALVTNPKILLCDEAT 168
Cdd:PLN03232 696 RENILF------GSDFE-SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109734267 169 SALDPATTASIL-ALLKNVNQtfGITIMIITHEMCVIKDIcNRVAVMEKGQVVETGTVTDVF 229
Cdd:PLN03232 769 SALDAHVAHQVFdSCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-220 |
6.62e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLvrlvnhleAAS----------SGQVIVDGHDI-TDYSEKAMR-------EIKK 82
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTEL--------AMSvfgrsygrniSGTVFKDGKEVdVSTVSDAIDaglayvtEDRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 83 DIGMifqhfNLLNsaTVFKNVAMPlILSKKSKKEITQRVTEMLEFVGLSDKK-------DQFPDELSGGQKQRVAIARAL 155
Cdd:NF040905 348 GYGL-----NLID--DIKRNITLA-NLGKVSRRGVIDENEEIKVAEEYRKKMniktpsvFQKVGNLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 156 VTNPKILLCDEATSALDPATTASILALlknVNQ--TFGITIMIITHEMCVIKDICNRVAVMEKGQVV 220
Cdd:NF040905 420 FTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-215 |
1.94e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 28 VNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDghdiTDYSEKAmREIKKDIGMIFQHFnlLNSATvfknvamPL 107
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----LKISYKP-QYIKPDYDGTVEDL--LRSIT-------DD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 108 ILSKKSKKEITQRVtemlefvGLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD---PATTASIlalLK 184
Cdd:PRK13409 428 LGSSYYKSEIIKPL-------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKA---IR 497
|
170 180 190
....*....|....*....|....*....|.
gi 1109734267 185 NVNQTFGITIMIITHEMCVIKDICNRVAVME 215
Cdd:PRK13409 498 RIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-227 |
3.18e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 21 LKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAaSSGQVivdghditdYSEKAmreikkdIGMIFQHFNLLNsATV 99
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEGRV---------WAERS-------IAYVPQQAWIMN-ATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNVampLILSKKSKKEITQ--RVTEMLEFV-----GLSDKKDQFPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PTZ00243 738 RGNI---LFFDEEDAARLADavRVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 173 PATTASIlallknVNQTF-----GITIMIITHEMCVIKdICNRVAVMEKGQVVETGTVTD 227
Cdd:PTZ00243 815 AHVGERV------VEECFlgalaGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSSAD 867
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
264-340 |
5.80e-06 |
|
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: 43.65 E-value: 5.80e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109734267 264 DYRDYKLFIEETQLPHPIVNDLIQINQGQVKILFSSMSEIQGKTVCYLWLRFDANQHfNDTKIKHYFEMNDIQFEEV 340
Cdd:smart00930 1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEE-DIEAALAYLREQGVEVEVL 76
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
134-235 |
8.22e-06 |
|
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: 45.64 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 134 KDQFPDeLSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQTFGITIMIITHEMCVIKDICNRVAV 213
Cdd:cd03222 66 KPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
90 100
....*....|....*....|..
gi 1109734267 214 MEkGQVVETGTvtdvFSHPKTT 235
Cdd:cd03222 145 FE-GEPGVYGI----ASQPKGT 161
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
22-219 |
1.63e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 22 KDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVivdghditdysekaMREIKKDIGMIFQH----FNLLNSA 97
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHhvdgLDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNVAMPLILSkkskkeitQRVTEMLEFVGLSDKKDQFPD-ELSGGQKQRVAIARALVTNPKILLCDEATSALD-PAT 175
Cdd:PLN03073 592 LLYMMRCFPGVPE--------QKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAV 663
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1109734267 176 TASILALLknvnqTFGITIMIITHEMCVIKDICNRVAVMEKGQV 219
Cdd:PLN03073 664 EALIQGLV-----LFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-172 |
2.51e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 35 GVIGYSGAGKSTLVR---------LVNHLEAASSGQVI--VDGHDITDY----SEKAMREIKKDigmifQHFNLLnsATV 99
Cdd:PRK13409 103 GILGPNGIGKTTAVKilsgelipnLGDYEEEPSWDEVLkrFRGTELQNYfkklYNGEIKVVHKP-----QYVDLI--PKV 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109734267 100 FK-NVAMplILSKKSKKEITQRVTEMLEFVGLSDKKdqfPDELSGGQKQRVAIARALVTNPKILLCDEATSALD 172
Cdd:PRK13409 176 FKgKVRE--LLKKVDERGKLDEVVERLGLENILDRD---ISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
14-172 |
2.99e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 14 KKQKIHALKDVSFK------VNRNAIFGVIGYSGAGKSTLVRLVnhleaasSGQVIvdgHDITDYSEKAMRE--IKKDIG 85
Cdd:COG1245 76 EEDPVHRYGENGFRlyglpvPKKGKVTGILGPNGIGKSTALKIL-------SGELK---PNLGDYDEEPSWDevLKRFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 86 M-IFQHFNLLNSATVfkNVAM--------PLILSKKSK---KEITQR--VTEMLEFVGLSDKKDQFPDELSGGQKQRVAI 151
Cdd:COG1245 146 TeLQDYFKKLANGEI--KVAHkpqyvdliPKVFKGTVRellEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAI 223
|
170 180
....*....|....*....|.
gi 1109734267 152 ARALVTNPKILLCDEATSALD 172
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLD 244
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-172 |
6.85e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 6.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 19 HALKDVSFKVNRNAIFGVIGYSGAGKSTLVR-LVNHLEAASSGQVIVDGHdiTDYSEKamreikkdIGMIFqhfnllnSA 97
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT--VAYVPQ--------VSWIF-------NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 98 TVFKNVAMPLILsKKSKKEITQRVTEMLEFVGLSDKKDQfpDE-------LSGGQKQRVAIARALVTNPKILLCDEATSA 170
Cdd:PLN03130 694 TVRDNILFGSPF-DPERYERAIDVTALQHDLDLLPGGDL--TEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
..
gi 1109734267 171 LD 172
Cdd:PLN03130 771 LD 772
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
62-238 |
9.67e-05 |
|
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: 44.23 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 62 VIVDGHDITDYSEKAMREIkkdigMIFqhFNLLNSATVFKNVAMPLIlskkskKEITQRVTEMLEfVGLSD-KKDQFPDE 140
Cdd:TIGR00630 423 VTVGGKSIADVSELSIREA-----HEF--FNQLTLTPEEKKIAEEVL------KEIRERLGFLID-VGLDYlSLSRAAGT 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 141 LSGGQKQRVAIAR----ALVTNPKILlcDEATSALDPATTASILALLKNVnQTFGITIMIITHEMCVIK------DICNR 210
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRaadyviDIGPG 565
|
170 180
....*....|....*....|....*...
gi 1109734267 211 vAVMEKGQVVETGTVTDVFSHPKTTIAQ 238
Cdd:TIGR00630 566 -AGEHGGEVVASGTPEEILANPDSLTGQ 592
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
73-223 |
1.30e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 73 SEKAMREikKDIGmIF--QHFNLLNSATVFKNVAMPLIlskkskkeitqrVTEMLEFVGLSDKKDQF-PDEL----SGGQ 145
Cdd:PLN03140 277 SELARRE--KDAG-IFpeAEVDLFMKATAMEGVKSSLI------------TDYTLKILGLDICKDTIvGDEMirgiSGGQ 341
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 146 KQRVAIARALVTNPKILLCDEATSALDPATTASILALLKN-VNQTFGITIMIITHEMCVIKDICNRVAVMEKGQVVETG 223
Cdd:PLN03140 342 KKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQiVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQIVYQG 420
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-172 |
2.08e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 1 MIEFRQVSKTFNKKKqkihaLKDVSFKVNRNAIFGVIGYSGAGKSTLVRLVNHLEAASSGQVIVDGHDITDYSEKAMREI 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKN-----LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 81 KKDIGMIFQhfnllnsATVFKNVAMplilskksKKEITQRVTEM---LEFVGLSDKKDQFPDELSGGQKQRVAIARALVT 157
Cdd:PRK13541 76 GHNLGLKLE-------MTVFENLKF--------WSEIYNSAETLyaaIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIAC 140
|
170
....*....|....*
gi 1109734267 158 NPKILLCDEATSALD 172
Cdd:PRK13541 141 QSDLWLLDEVETNLS 155
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
140-185 |
4.81e-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: 38.76 E-value: 4.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1109734267 140 ELSGGQKQR---VAIARALV----------TNPKILLCDEATSALDPATTASILALLKN 185
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
140-217 |
8.25e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 8.25e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109734267 140 ELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfgiTIMIITHEMCVIKDICNRVAVMEKG 217
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHDRHFLNSVCTHMADLDYG 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-200 |
1.09e-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: 39.51 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 33 IFGVIGYSGAGKSTLvrlvnhLEA---ASSGQVIVDG----HDITDYSEKamrEIKKDIGMIFQHFN-----LLNSATVF 100
Cdd:cd03240 24 LTLIVGQNGAGKTTI------IEAlkyALTGELPPNSkggaHDPKLIREG---EVRAQVKLAFENANgkkytITRSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 101 KNVAMplilskKSKKEITQRVTEMLEFvglsdkkdqfpdeLSGGQKQ------RVAIARALVTNPKILLCDEATSALDPA 174
Cdd:cd03240 95 ENVIF------CHQGESNWPLLDMRGR-------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155
|
170 180
....*....|....*....|....*..
gi 1109734267 175 T-TASILALLKNVNQTFGITIMIITHE 200
Cdd:cd03240 156 NiEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-172 |
1.19e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 34 FGVIGYSGAGKSTLVRL--------------VNHLEAASSGQVIVDGHDITDYSEKAMREIKKDIGMIFQHFNLlNSATV 99
Cdd:PLN03073 206 YGLVGRNGTGKTTFLRYmamhaidgipkncqILHVEQEVVGDDTTALQCVLNTDIERTQLLEEEAQLVAQQREL-EFETE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 100 FKNVAMPLILSKKsKKEITQRVTEM---LEFV--------------GLS---DKKDQFPDELSGGQKQRVAIARALVTNP 159
Cdd:PLN03073 285 TGKGKGANKDGVD-KDAVSQRLEEIykrLELIdaytaearaasilaGLSftpEMQVKATKTFSGGWRMRIALARALFIEP 363
|
170
....*....|...
gi 1109734267 160 KILLCDEATSALD 172
Cdd:PLN03073 364 DLLLLDEPTNHLD 376
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
117-238 |
1.33e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 117 ITQRVTEMLEFVGLSDKKDQFP-DELSGGQKQRVAIARALVTNPKILLCDEATSALDPATTASILALLKNVNQtfgiTIM 195
Cdd:PRK10636 125 IRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLI 200
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1109734267 196 IITHEMCVIKDICNRVAVMEKGQVVE-TGTVTDVFSHPKTTIAQ 238
Cdd:PRK10636 201 LISHDRDFLDPIVDKIIHIEQQSLFEyTGNYSSFEVQRATRLAQ 244
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-205 |
1.40e-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: 40.38 E-value: 1.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109734267 141 LSGGQKQRVAIARAL---VTNPKILLCDEATSALDpatTASILALLkNVNQTF---GITIMIITHEMCVIK 205
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLH---FDDIKKLL-EVLQRLvdkGNTVVVIEHNLDVIK 896
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
140-224 |
4.26e-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: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 140 ELSGGQKQRVAIARAL---VTNPKILLCDEATSALDPATTASILALLKN-VNQtfGITIMIITHEMCVIKdICNRVAVM- 214
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDK--GNTVVVIEHNLDVIK-CADWIIDLg 245
|
90
....*....|....*
gi 1109734267 215 -----EKGQVVETGT 224
Cdd:cd03271 246 peggdGGGQVVASGT 260
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
280-339 |
9.23e-03 |
|
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: 34.35 E-value: 9.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109734267 280 PIVNDLIQINQGQVKILFSSMSEIQGKTVCYLWLRFDANQHfNDTKIKHYFEMNDIQFEE 339
Cdd:pfam09383 15 PVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPE-QIEAALAYLREQGVEVEV 73
|
|
| |
