|
Name |
Accession |
Description |
Interval |
E-value |
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-256 |
4.30e-177 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 487.19 E-value: 4.30e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR 81
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTFQNIRLFKQLTVLENLMVAQHLKVNRNMLSGLFATPAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQR 161
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|....*
gi 1787163341 242 VRNDPRVIKAYLGED 256
Cdd:PRK11300 241 IRNNPDVIKAYLGEA 255
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-256 |
2.04e-141 |
|
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: 396.72 E-value: 2.04e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRG 82
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVRTFQNIRLFKQLTVLENLMVAQHLKVNRNMLSGLFATPAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRR 162
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
250
....*....|....
gi 1787163341 243 RNDPRVIKAYLGED 256
Cdd:COG0411 241 RADPRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-248 |
2.86e-113 |
|
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: 324.78 E-value: 2.86e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRT 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLMVAQHLKVNRNMLSGLFAtpayrRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARAR-----REEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRnEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
..
gi 1787163341 247 RV 248
Cdd:cd03219 235 RV 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-255 |
3.31e-68 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 210.74 E-value: 3.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR 81
Cdd:COG4674 6 MHGPILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTFQNIRLFKQLTVLENLMVAqhLKVNRNMLSGLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQR 161
Cdd:COG4674 86 GIGRKFQKPTVFEELTVFENLELA--LKGDRGVFASLFARLTAEERDRIEEV-----LETIGLTDKADRLAGLLSHGQKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFgiSVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:COG4674 159 WLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDE 236
|
250
....*....|....
gi 1787163341 242 VRNDPRVIKAYLGE 255
Cdd:COG4674 237 VQADPRVIEVYLGR 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-254 |
7.99e-64 |
|
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: 199.05 E-value: 7.99e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV 84
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQLTVLENLMVaqhlkvnrnmlsGLFATPAYRRAERAaleraaywLERVG-----LKQVANREAGTLSYGH 159
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLL------------GAYARRDRAEVRAD--------LERVYelfprLKERRRQRAGTLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 160 QRRLEIARCMITDPRLLMLDEPAAGLNPqeKVeLQQMVDGLR--NEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAP--LI-VEEIFEIIRrlNREGVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
|
250
....*....|....*..
gi 1787163341 238 KPDEVRNDPRVIKAYLG 254
Cdd:COG0410 219 TAAELLADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-245 |
3.03e-60 |
|
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: 189.57 E-value: 3.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRT 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLMVAqhlkvnrnmlsglfatpAYRRAERAALERaaywLERV-----GLKQVANREAGTLSYGHQR 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLG-----------------AYARRRAKRKAR----LERVyelfpRLKERRKQLAGTLSGGEQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRnEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
....
gi 1787163341 242 VRND 245
Cdd:cd03224 219 LLAD 222
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-256 |
3.26e-59 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 187.54 E-value: 3.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV 84
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQLTVLENLM-VAQHLKVNR----NMLSGLfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGH 159
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILaVLELRKLSKkereERLEEL--------------------LEEFGITHLRKSKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 160 QRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKP 239
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTP 220
|
250
....*....|....*..
gi 1787163341 240 DEVRNDPRVIKAYLGED 256
Cdd:COG1137 221 EEILNNPLVRKVYLGED 237
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-244 |
6.51e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 186.81 E-value: 6.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVrt 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLmvaqhlkvnrNMLSGLFATPAyrraeRAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:COG1131 79 PQEPALYPDLTVRENL----------RFFARLYGLPR-----KEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN 244
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-254 |
1.82e-56 |
|
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: 180.43 E-value: 1.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRT 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLM-VAQHLKVNRnmlsglfatpayrraeRAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEI 165
Cdd:cd03218 81 PQEASIFRKLTVEENILaVLEIRGLSK----------------KEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRnEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRND 245
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
....*....
gi 1787163341 246 PRVIKAYLG 254
Cdd:cd03218 224 ELVRKVYLG 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
7-256 |
4.27e-54 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 174.38 E-value: 4.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRT 86
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLMVAQHLKvnrnmlsglfatpaYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIR--------------KDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRnEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:TIGR04406 148 RALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLK-ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
250
....*....|
gi 1787163341 247 RVIKAYLGED 256
Cdd:TIGR04406 227 KVRRVYLGEQ 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-247 |
6.82e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 177.60 E-value: 6.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQvaRR- 81
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVrtFQNIRLFKQLTVLENlmVAQHLKVnRNMlsglfatPAyrraeRAALERAAYWLERVGLKQVANREAGTLSYGHQR 161
Cdd:COG3842 80 GMV--FQDYALFPHLTVAEN--VAFGLRM-RGV-------PK-----AEIRARVAELLELVGLEGLADRYPHQLSGGQQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEE 222
|
....*.
gi 1787163341 242 VRNDPR 247
Cdd:COG3842 223 IYERPA 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-248 |
2.61e-53 |
|
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: 172.47 E-value: 2.61e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQ---V 78
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 ARR-GLVrtFQNIRLFKQLTVLENLMVA--QHLKVNRNMLSGLfatpayrraeraalerAAYWLERVGLKQVANREAGTL 155
Cdd:COG1127 81 RRRiGML--FQGGALFDSLTVFENVAFPlrEHTDLSEAEIREL----------------VLEKLELVGLPGAADKMPSEL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 156 SYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIM 235
Cdd:COG1127 143 SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|....*
gi 1787163341 236 IGKPDEVRN--DPRV 248
Cdd:COG1127 223 EGTPEELLAsdDPWV 237
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-237 |
2.67e-49 |
|
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: 161.15 E-value: 2.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQvaRR-GLVr 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNiGMV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 tFQNIRLFKQLTVLENlmVAQHLKVNRnmlsglfaTPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQRRLEI 165
Cdd:cd03259 78 -FQDYALFPHLTVAEN--IAFGLKLRG--------VPKAEIRARVREL-----LELVGLEGLLNRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-248 |
1.72e-48 |
|
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: 159.97 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 9 VAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITG--QPSHQVARR--GLV 84
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRrmGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 rtFQNIRLFKQLTVLENLMVA--QHLKVNRNMLSGLFAtpayrraeraaleraaYWLERVGLKQVANREAGTLSYGHQRR 162
Cdd:cd03261 83 --FQSGALFDSLTVFENVAFPlrEHTRLSEEEIREIVL----------------EKLEAVGLRGAEDLYPAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
....*...
gi 1787163341 243 RN--DPRV 248
Cdd:cd03261 225 RAsdDPLV 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-243 |
6.69e-48 |
|
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: 158.87 E-value: 6.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHqvARRGLVR 85
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 TFQNIRLFKQLTVLENLmvaqhlkvnrnmlsGLFATpAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEI 165
Cdd:COG4555 79 LPDERGLYDRLTVRENI--------------RYFAE-LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVR 243
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-251 |
8.27e-48 |
|
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: 157.88 E-value: 8.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNIR--LF 93
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGLV--FQNPDdqLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KQlTVLENLMVA-QHLKVNRNMLsglfatpayrraeraaLERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITD 172
Cdd:COG1122 90 AP-TVEEDVAFGpENLGLPREEI----------------RERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPRVIKA 251
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-243 |
2.21e-47 |
|
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: 156.76 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 9 VAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVrtFQ 88
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV--FQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 89 NIRLFKQLTVLENLMvaqhlkvnrnMLSGLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQRRLEIARC 168
Cdd:cd03265 81 DLSVDDELTGWENLY----------IHARLYGVPGAERRERIDEL-----LDFVGLLEAADRLVKTYSGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 169 MITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVR 243
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-253 |
5.15e-47 |
|
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: 156.15 E-value: 5.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRT 86
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLMVaqhlkvnrnmlsGLFATPAyrraERAALERAAYWLERVgLKQVANREAGTLSYGHQRRLEIA 166
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLT------------GLAALPR----RSRKIPDEIYELFPV-LKEMLGRRGGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVrnDP 246
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL--DE 221
|
....*..
gi 1787163341 247 RVIKAYL 253
Cdd:TIGR03410 222 DKVRRYL 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-246 |
1.32e-46 |
|
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: 155.09 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHqvaRRGLVRT 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENlmVAQHLKVNRnmlsglfatpayrRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:cd03300 78 FQNYALFPHLTVFEN--IAFGLRLKK-------------LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-231 |
4.44e-46 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.48 E-value: 4.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MS-AQALLKVAGLQMRF----GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPs 75
Cdd:COG1116 1 MSaAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 76 hqvARRGLVrtFQNIRLFKQLTVLENLMVAqhLKVNRnmlsglfatpayrRAERAALERAAYWLERVGLKQVANREAGTL 155
Cdd:COG1116 80 ---PDRGVV--FQEPALLPWLTVLDNVALG--LELRG-------------VPKAERRERARELLELVGLAGFEDAYPHQL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 156 SYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMS--LVMgvSDRILVMEHG 231
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeaVFL--ADRVVVLSAR 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-243 |
6.69e-46 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 152.66 E-value: 6.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGL--LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHqvARRGLV 84
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQLTVLENLMVAQHLKvnrnmlsGLFATPAYRRAERAaleraaywLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLK-------GLPKSEIKEEVELL--------LRVLGLTDKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVR 243
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-232 |
7.72e-46 |
|
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: 151.01 E-value: 7.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVrt 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLMvaqhlkvnrnmlsglfatpayrraeraaleraaywlervglkqvanreagtLSYGHQRRLEIA 166
Cdd:cd03230 79 PEEPSLYENLTVRENLK---------------------------------------------------LSGGMKQRLALA 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03230 108 QALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-232 |
1.29e-45 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 159.42 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAIT-GQPSHqvAR 80
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRD--AI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 R---GLVrtFQNIRLFKQLTVLENLMVAQ----HLKVNRNMLSGLFATPAyrraeraaleraaywlERVGLKQVANREAG 153
Cdd:COG3845 79 AlgiGMV--HQHFMLVPNLTVAENIVLGLeptkGGRLDRKAARARIRELS----------------ERYGLDVDPDAKVE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 154 TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:COG3845 141 DLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-232 |
6.27e-45 |
|
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: 149.92 E-value: 6.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNIR--LFKqLT 97
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV--FQNPDdqFFG-PT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 V-------LENLMVAQHLKVNRnmlsglfatpayrraeraalerAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMI 170
Cdd:cd03225 93 VeeevafgLENLGLPEEEIEER----------------------VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 171 TDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-247 |
9.92e-45 |
|
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: 156.99 E-value: 9.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRF-----GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSH 76
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 77 QVARR----GLVrtFQNIR--LFKQLTVLENLMVAQHlkvNRNMLSGlfatpayrraeRAALERAAYWLERVGL-KQVAN 149
Cdd:COG1123 336 SLRELrrrvQMV--FQDPYssLNPRMTVGDIIAEPLR---LHGLLSR-----------AERRERVAELLERVGLpPDLAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 150 REAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVME 229
Cdd:COG1123 400 RYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMY 479
|
250
....*....|....*...
gi 1787163341 230 HGKPIMIGKPDEVRNDPR 247
Cdd:COG1123 480 DGRIVEDGPTEEVFANPQ 497
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-247 |
2.57e-44 |
|
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: 149.41 E-value: 2.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPshqVARRGLVRT 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENlmVAQHLKVNRNmlsglfatpAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:cd03296 80 FQHYALFRHMTVFDN--VAFGLRVKPR---------SERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
.
gi 1787163341 247 R 247
Cdd:cd03296 229 A 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-242 |
3.33e-44 |
|
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: 149.42 E-value: 3.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLV 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRiAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 rtFQNIRLFKQLTVLEnlMVAQ----HLkvnrnmlsGLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQ 160
Cdd:COG1120 81 --PQEPPAPFGLTVRE--LVALgrypHL--------GLFGRPSAEDREAVEEA-----LERTGLEHLADRPVDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPD 240
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
..
gi 1787163341 241 EV 242
Cdd:COG1120 224 EV 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-252 |
6.80e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 148.31 E-value: 6.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItGQPSHQVA- 79
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-RRARRRIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 ---RRGLVRTFqnirlfkQLTVLEnlMVAQHLKVNRNMLSGLFATpayrraeraALERAAYWLERVGLKQVANREAGTLS 156
Cdd:COG1121 80 vpqRAEVDWDF-------PITVRD--VVLMGRYGRRGLFRRPSRA---------DREAVDEALERVGLEDLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 157 YGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKpIMI 236
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGL-VAH 219
|
250
....*....|....*.
gi 1787163341 237 GKPDEVRNDPRVIKAY 252
Cdd:COG1121 220 GPPEEVLTPENLSRAY 235
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-247 |
9.16e-44 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 147.83 E-value: 9.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR---G 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRrkvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVrtFQNIRLFKQLTVLENLMVAQ--HLKVNRNmlsglfatpayrraerAALERAAYWLERVGLKQVANREAGTLSYGHQ 160
Cdd:COG1126 81 MV--FQQFNLFPHLTVLENVTLAPikVKKMSKA----------------EAEERAMELLERVGLADKADAYPAQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPqEKVE--LQQMVDgLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGK 238
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDP-ELVGevLDVMRD-LAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
....*....
gi 1787163341 239 PDEVRNDPR 247
Cdd:COG1126 220 PEEFFENPQ 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-228 |
1.78e-43 |
|
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: 146.46 E-value: 1.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGG----LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPshqvARRG 82
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVrtFQNIRLFKQLTVLENLMVAqhLKVNRnmlsglfatpayrRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRR 162
Cdd:cd03293 77 YV--FQQDALLPWLTVLDNVALG--LELQG-------------VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVM 228
Cdd:cd03293 140 VALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-232 |
3.69e-43 |
|
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: 145.71 E-value: 3.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGG----LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA--R 80
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 R---GLVrtFQNIRLFKQLTVLENLMVAQhlkvnrnMLSGLFATPAyrraeraaLERAAYWLERVGLKQVANREAGTLSY 157
Cdd:cd03255 81 RrhiGFV--FQSFNLLPDLTALENVELPL-------LLAGVPKKER--------RERAEELLERVGLGDRLNHYPSELSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 158 GHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHGK 232
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-256 |
4.75e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 149.78 E-value: 4.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRG 82
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVRTFQNIRLFKQLTVLENLMVAQHLK----VNRNMLSGLFATpayrraeraaleraayWLERVGLKQVANREAGTLSYG 158
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRrgglIDWRAMRRRARE----------------LLARLGLDIDPDTPVGDLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 159 HQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGK 238
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGP 223
|
250
....*....|....*...
gi 1787163341 239 PDEVrNDPRVIKAYLGED 256
Cdd:COG1129 224 VAEL-TEDELVRLMVGRE 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-246 |
9.90e-42 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 142.47 E-value: 9.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQmRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHqvaRRGLVRT 86
Cdd:cd03299 1 LKVENLS-KDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE---KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLmvAQHLKVNRNMlsglfatpayrraERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:cd03299 77 PQNYALFPHMTVYKNI--AYGLKKRKVD-------------KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-232 |
6.99e-41 |
|
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: 138.47 E-value: 6.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRT 86
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 -FQNIRLFKQLTVLENLMVAqhlkvnrnmLSGlfatpayrraeraaleraaywlervglkqvanreagtlsyGHQRRLEI 165
Cdd:cd03229 81 vFQDFALFPHLTVLENIALG---------LSG----------------------------------------GQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-252 |
1.01e-40 |
|
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: 140.01 E-value: 1.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFG-GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQV--ARRGL 83
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VRTFQNIRLFKQLTVLENLMVAqhlKVNR-NMLSGLFA--TPAyrraeraALERAAYWLERVGLKQVANREAGTLSYGHQ 160
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG---RLGRrSTWRSLFGlfPKE-------EKQRALAALERVGLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPD 240
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
250
....*....|..
gi 1787163341 241 EVrNDPRVIKAY 252
Cdd:cd03256 231 EL-TDEVLDEIY 241
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-232 |
1.08e-40 |
|
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: 139.20 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPS--HQVARR-GL 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VrtFQNIRLFKQLTVLENLMVAQhLKVnRNMlsglfatpayrrAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRL 163
Cdd:cd03262 81 V--FQQFNLFPHLTVLENITLAP-IKV-KGM------------SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 164 EIARCMITDPRLLMLDEPAAGLNPqEKVE--LQQMVDgLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDP-ELVGevLDVMKD-LAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-232 |
2.10e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 139.02 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFG----GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA 79
Cdd:COG1136 2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 --RR---GLVrtFQNIRLFKQLTVLENLMVAQhlkvnrnMLSGLFATPAyrraeraaLERAAYWLERVGLKQVANREAGT 154
Cdd:COG1136 82 rlRRrhiGFV--FQFFNLLPELTALENVALPL-------LLAGVSRKER--------RERARELLERVGLGDRLDHRPSQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 155 LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLvMGVSDRILVMEHGK 232
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPEL-AARADRVIRLRDGR 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-245 |
3.93e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 140.24 E-value: 3.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA----RRG 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGylpeERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 lvrtfqnirLFKQLTVLENLM-VAQhlkvnrnmLSGLFATPAyrraeraaLERAAYWLERVGLKQVANREAGTLSYGHQR 161
Cdd:COG4152 82 ---------LYPKMKVGEQLVyLAR--------LKGLSKAEA--------KRRADEWLERLGLGDRANKKVEELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPqekVELQQMVDGLR--NEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKP 239
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDP---VNVELLKDVIRelAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSV 213
|
....*.
gi 1787163341 240 DEVRND 245
Cdd:COG4152 214 DEIRRQ 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-256 |
2.34e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.73 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRF-GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQV--ARR 81
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 --GLVrtFQNIRLFKQLTVLENLMVAQ--HLKVNRNMLsGLFATPAYRRAERAaleraaywLERVGLKQVANREAGTLSY 157
Cdd:COG3638 81 riGMI--FQQFNLVPRLSVLTNVLAGRlgRTSTWRSLL-GLFPPEDRERALEA--------LERVGLADKAYQRADQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 158 GHQRRLEIARCMITDPRLLMLDEPAAGLNPQ--EKVeLQQMVDgLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIM 235
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKtaRQV-MDLLRR-IAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVF 227
|
250 260
....*....|....*....|..
gi 1787163341 236 IGKPDEVrnDPRVIKA-YLGED 256
Cdd:COG3638 228 DGPPAEL--TDAVLREiYGGEA 247
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-183 |
1.01e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.00 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVARRGLVRTFQNIRLFKQLTVLEN 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 LMVAQHLKVNRNMLSGlfatpayrraeraalERAAYWLERVGL----KQVANREAGTLSYGHQRRLEIARCMITDPRLLM 177
Cdd:pfam00005 80 LRLGLLLKGLSKREKD---------------ARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLL 144
|
....*.
gi 1787163341 178 LDEPAA 183
Cdd:pfam00005 145 LDEPTA 150
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-252 |
2.03e-37 |
|
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: 131.75 E-value: 2.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAG-DIVLEGHAITGQPSHQVARR- 81
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTFQNIRLFKQLTVLEnlMVaqhlkvnrnmLSGLFATPA-YRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQ 160
Cdd:COG1119 81 GLVSPALQLRFPRDETVLD--VV----------LSGFFDSIGlYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPD 240
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
250
....*....|..
gi 1787163341 241 EVRNDPRVIKAY 252
Cdd:COG1119 229 EVLTSENLSEAF 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-256 |
2.37e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 131.55 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV 84
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQLTVLENLMVAqhLKVNRNMLSGLFATPAYRRaeraaleraaywLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAV--LQIRDDLSAEQREDRANEL------------MEEFHIEHLRDSMGQSLSGGERRRVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRnEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN 244
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
250
....*....|..
gi 1787163341 245 DPRVIKAYLGED 256
Cdd:PRK10895 227 DEHVKRVYLGED 238
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-237 |
2.73e-37 |
|
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: 129.48 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 8 KVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVRT 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKiAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 fqnirlfkqltvlenlmvaqhlkvnrnmlsglfatpayrraeraaleraayWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:cd03214 81 ---------------------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLA 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03214 110 RALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-231 |
2.28e-36 |
|
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: 128.03 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 8 KVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGdivleghaitgqpshqvarrglvrtf 87
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSG-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 88 qNIRLFKQLTVLENLMVA---QHLKVNRNM-LSG--LFATPAYRRAERAALERAAYW------LERVGLKQVANREAGTL 155
Cdd:cd03235 55 -SIRVFGKPLEKERKRIGyvpQRRSIDRDFpISVrdVVLMGLYGHKGLFRRLSKADKakvdeaLERVGLSELADRQIGEL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 156 SYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHG 231
Cdd:cd03235 134 SGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-247 |
2.31e-36 |
|
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: 128.47 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQV--ARR--GLVrtFQNIRLFKQL 96
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRriGMI--FQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENlmVAQHLKVNRnmlsglfatpayrRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:cd03258 98 TVFEN--VALPLEIAG-------------VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 177 MLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-246 |
2.32e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 131.77 E-value: 2.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGhaITGQPSHQ-----VARRGLVRTFQNIRLFKqltvl 99
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG--RTLFDSRKgiflpPEKRRIGYVFQEARLFP----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 enlmvaqHLKVNRNMLSGL-FATPAYRRAERAALeraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLML 178
Cdd:TIGR02142 89 -------HLSVRGNLRYGMkRARPSERRISFERV------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 179 DEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-234 |
2.47e-36 |
|
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: 126.39 E-value: 2.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVrt 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 fqnirlfkqltvlenlMVAQhlkvnrnmlsglfatpayrraeraaleraaywlervglkqvanreagtLSYGHQRRLEIA 166
Cdd:cd03216 79 ----------------MVYQ------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-214 |
4.15e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 127.21 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV 84
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 rtFQNIRLFKQLTVLENLMVAQHLKvnrnmlsGLFATPAYRRAeraaleraayWLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:COG4133 81 --GHADGLKPELTVRENLRFWAALY-------GLRADREAIDE----------ALEAVGLAGLADLPVRQLSAGQKRRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGIsVLLIEHD 214
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-246 |
5.44e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.22 E-value: 5.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQvar 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 RGLVRTFQNIRLFKQLTVLENlmVAQHLKVNRnmlsglfaTPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQ 160
Cdd:PRK09452 86 RHVNTVFQSYALFPHMTVFEN--VAFGLRMQK--------TPAAEITPRVMEA-----LRMVQLEEFAQRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPD 240
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
....*.
gi 1787163341 241 EVRNDP 246
Cdd:PRK09452 231 EIYEEP 236
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-247 |
5.50e-36 |
|
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: 128.00 E-value: 5.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFG----GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQpshqvARR 81
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR-----RRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTFQnirlfkqltvlenlMVAQH--LKVN-RNMLSGLFATPAYRRAERAALERAAYWLERVGL-KQVANREAGTLSY 157
Cdd:COG1124 76 AFRRRVQ--------------MVFQDpyASLHpRHTVDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 158 GHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEEL 221
|
250
....*....|
gi 1787163341 238 KPDEVRNDPR 247
Cdd:COG1124 222 TVADLLAGPK 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-251 |
5.55e-36 |
|
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: 133.49 E-value: 5.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRF--GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTA---GDIVLEGHAITGQPSHQV 78
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 ARR-GLVrtFQNIRL-FKQLTVLENLMvaqhlkvnrnmlsglFATPAYRRAERAALERAAYWLERVGLKQVANREAGTLS 156
Cdd:COG1123 82 GRRiGMV--FQDPMTqLNPVTVGDQIA---------------EALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 157 YGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMI 236
Cdd:COG1123 145 GGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
250
....*....|....*
gi 1787163341 237 GKPDEVRNDPRVIKA 251
Cdd:COG1123 225 GPPEEILAAPQALAA 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-247 |
7.53e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.19 E-value: 7.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPshqVARRGLV 84
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP---PKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQLTVLENLmvAQHLKVNRnmlsglfaTPAyrraeRAALERAAYWLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:COG3839 79 MVFQSYALYPHMTVYENI--AFPLKLRK--------VPK-----AEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN 244
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYD 223
|
...
gi 1787163341 245 DPR 247
Cdd:COG3839 224 RPA 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-237 |
7.55e-36 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 126.63 E-value: 7.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA----RRG 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylpeERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 lvrtfqnirLFKQLTVLENLMVAQHLKvnrnmlsGLFATPAyrraeraaLERAAYWLERVGLKQVANREAGTLSYGHQRR 162
Cdd:cd03269 81 ---------LYPKMKVIDQLVYLAQLK-------GLKKEEA--------RRRIDEWLERLELSEYANKRVEELSKGNQQK 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-246 |
9.73e-36 |
|
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: 128.14 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 15 RFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPS---HQVARRGLVRTFQNIR 91
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelRELRRKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 92 LFKQLTVLENlmVAQHLKVnrnmlSGLFATPAYRRAERAaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMIT 171
Cdd:cd03294 113 LLPHRTVLEN--VAFGLEV-----QGVPRAEREERAAEA--------LELVGLEGWEHKYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 172 DPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:cd03294 178 DPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-232 |
2.22e-35 |
|
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: 126.08 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRF----GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR 81
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 G----LVrtFQNIR--LFKQLTVLENLM-VAQHLKVNRNmlsglfatpayrraERAALERAAYWLERVGL-KQVANREAG 153
Cdd:cd03257 81 RkeiqMV--FQDPMssLNPRMTIGEQIAePLRIHGKLSK--------------KEARKEAVLLLLVGVGLpEEVLNRYPH 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 154 TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03257 145 ELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-232 |
2.36e-35 |
|
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: 123.51 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 8 KVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVaRRGLVRTF 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 88 QnirlfkqltvlenlmvaqhlkvnrnmlsglfatpayrraeraaleraaywlervglkqvanreagtLSYGHQRRLEIAR 167
Cdd:cd00267 80 Q------------------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 168 CMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-252 |
3.36e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.38 E-value: 3.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVAR-RGLV 84
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARrRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RtfQNIRLFKQLTVLEnlMVAqhlkvnrnMlsGLFATPAYRRAERAALERAaywLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:COG4559 81 P--QHSSLAFPFTVEE--VVA--------L--GRAPHGSSAAQDRQIVREA---LALVGLAHLAGRSYQTLSGGEQQRVQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMI-------TDPRLLMLDEPAAGLNPQEkvelQQMVDGLRNEF---GISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:COG4559 144 LARVLAqlwepvdGGPRWLFLDEPTSALDLAH----QHAVLRLARQLarrGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
250
....*....|....*...
gi 1787163341 235 MIGKPDEVRNDPRVIKAY 252
Cdd:COG4559 220 AQGTPEEVLTDELLERVY 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-252 |
4.64e-35 |
|
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: 126.41 E-value: 4.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPS---HQVARR-GLVrtFQN--IRLFk 94
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklKDLRKKvGLV--FQFpeHQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 95 QLTVLENLMVAQhlkvnRNMlsGLFATPAyrraeraaLERAAYWLERVGL-KQVANREAGTLSYGHQRRLEIARCMITDP 173
Cdd:TIGR04521 97 EETVYKDIAFGP-----KNL--GLSEEEA--------EERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 174 RLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPRVIKAY 252
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDELEKI 240
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-234 |
7.22e-35 |
|
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: 123.87 E-value: 7.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGhAITGQPSHQVARRGLVRT 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG-KSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNirLFKQLTVLENLMVAQHLKVNRNmlsglfatpayrraeraalERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:cd03268 80 APG--FYPNLTARENLRLLARLLGIRK-------------------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-255 |
9.60e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.48 E-value: 9.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAvdGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQvarRGLVRT 86
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLMVAQH--LKVNRNMLSGLFATpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRpgLKLTAEQRAQVEQA-----------------LERVGLAGLLDRLPGQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV-- 242
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALld 219
|
250
....*....|...
gi 1787163341 243 RNDPRVIKAYLGE 255
Cdd:COG3840 220 GEPPPALAAYLGI 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-242 |
1.37e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 126.07 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV 84
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNirLFKQLTVLENLMVaqhlkvnrnmLSGLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:PRK13537 86 PQFDN--LDPDFTVRENLLV----------FGRYFGLSAAAARALVPPL-----LEFAKLENKADAKVGELSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKvelQQMVDGLRNEF--GISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQAR---HLMWERLRSLLarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-255 |
1.93e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 125.33 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-----GLVRTFQNIRLFKQl 96
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKlrkkvSLVFQFPEAQLFEN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENLMvaqhlkvnrnmlsglFATPAYRRAERAALERAAYWLERVGLK-QVANREAGTLSYGHQRRLEIARCMITDPRL 175
Cdd:PRK13641 102 TVLKDVE---------------FGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 176 LMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPR-VIKAYLG 254
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYLD 245
|
.
gi 1787163341 255 E 255
Cdd:PRK13641 246 E 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-247 |
2.79e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 125.61 E-value: 2.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRF---GGLL--------AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHA 69
Cdd:COG4608 2 AMAEPLLEVRDLKKHFpvrGGLFgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 70 ITGQPSHQVA--RRGLVRTFQ------NIRLfkqlTVLEnlMVAQHLKVNRnMLSGlfatpayrraeRAALERAAYWLER 141
Cdd:COG4608 82 ITGLSGRELRplRRRMQMVFQdpyaslNPRM----TVGD--IIAEPLRIHG-LASK-----------AERRERVAELLEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 142 VGLK-QVANREAGTLSyGHQR-RLEIARCMITDPRLLMLDEPAAGLNpqekVELQ-Q----MVDgLRNEFGISVLLIEHD 214
Cdd:COG4608 144 VGLRpEHADRYPHEFS-GGQRqRIGIARALALNPKLIVCDEPVSALD----VSIQaQvlnlLED-LQDELGLTYLFISHD 217
|
250 260 270
....*....|....*....|....*....|...
gi 1787163341 215 MSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:COG4608 218 LSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-237 |
4.34e-34 |
|
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: 122.02 E-value: 4.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVrPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAI--TGQ----PSHQvaRR-GLVrtFQNIRLFKQLT 97
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKkinlPPQQ--RKiGLV--FQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 VLENLMVAqhLKVNRNMLSGLFATPAyrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLM 177
Cdd:cd03297 92 VRENLAFG--LKRKRNREDRISVDEL---------------LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 178 LDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-228 |
1.19e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 122.28 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGG----LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGqPShqvAR 80
Cdd:COG4525 2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PG---AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 RGLVrtFQNIRLFKQLTVLENlmVAQHLKvnrnmLSGLfatpayrrAERAALERAAYWLERVGLKQVANREAGTLSYGHQ 160
Cdd:COG4525 78 RGVV--FQKDALLPWLNVLDN--VAFGLR-----LRGV--------PKAERRARAEELLALVGLADFARRRIWQLSGGMR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDM--SLVMGVsdRILVM 228
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVeeALFLAT--RLVVM 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-245 |
2.67e-33 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 126.05 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRG 82
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVRTFQNIRLFKQLTVLENLMVAQHL--KVnrnmlsglFATPAYRRAERAALERAAywLERVGLKQVANREAGTLSYGHQ 160
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIGRHLtkKV--------CGVNIIDWREMRVRAAMM--LLRVGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPD 240
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
....*
gi 1787163341 241 EVRND 245
Cdd:PRK09700 231 DVSND 235
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
17-246 |
3.40e-33 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 123.42 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQ---VARRGLVRTFQNIRLF 93
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVElreVRRKKIGMVFQQFALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KQLTVLENL-MVAQHLKVNRNmlsglfatpayrraerAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITD 172
Cdd:TIGR01186 84 PHMTILQNTsLGPELLGWPEQ----------------ERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:TIGR01186 148 PDILLMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNP 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-232 |
7.76e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.00 E-value: 7.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDE-VFaIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA--RR--GLVrtFQNIR 91
Cdd:COG2884 13 GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylRRriGVV--FQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 92 LFKQLTVLENLMVAqhLKVNRnmlsglfATPAyrraerAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMIT 171
Cdd:COG2884 90 LLPDRTVYENVALP--LRVTG-------KSRK------EIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 172 DPRLLMLDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-246 |
1.31e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 122.25 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQvarR 81
Cdd:PRK11607 15 ALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---R 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTFQNIRLFKQLTVLENlmVAQHLKVNRnmlsglfatpayrRAERAALERAAYWLERVGLKQVANREAGTLSYGHQR 161
Cdd:PRK11607 92 PINMMFQSYALFPHMTVEQN--IAFGLKQDK-------------LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEE 236
|
....*
gi 1787163341 242 VRNDP 246
Cdd:PRK11607 237 IYEHP 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-247 |
1.88e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 119.26 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA- 79
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 --RRGLVRT-----FQNIR--LFKQLT----VLENLMVaqhlkVNRNMLSGLFATPAyrraeraaleraaYWLERVGLKq 146
Cdd:PRK11701 81 aeRRRLLRTewgfvHQHPRdgLRMQVSaggnIGERLMA-----VGARHYGDIRATAG-------------DWLERVEID- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 147 vANR---EAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSD 223
Cdd:PRK11701 142 -AARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAH 220
|
250 260
....*....|....*....|....
gi 1787163341 224 RILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK11701 221 RLLVMKQGRVVESGLTDQVLDDPQ 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-242 |
3.13e-32 |
|
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: 117.67 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYK-----PTAGDIVLEGHAITGQPSHQVARR 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 ---GLVrtFQNIRLFKqLTVLENlmVAQHLKVNRNMLSGLFATPAYRRaeraaleraaywLERVGL-KQVANR-EAGTLS 156
Cdd:cd03260 81 rrvGMV--FQKPNPFP-GSIYDN--VAYGLRLHGIKLKEELDERVEEA------------LRKAALwDEVKDRlHALGLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 157 YGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfgISVLLIEHDMSLVMGVSDRILVMEHGKPIMI 236
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
....*.
gi 1787163341 237 GKPDEV 242
Cdd:cd03260 222 GPTEQI 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
15-246 |
9.69e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.73 E-value: 9.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 15 RFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGqPSHQV--ARR--GLVrtFQNI 90
Cdd:PRK09493 10 HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDErlIRQeaGMV--FQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 91 RLFKQLTVLENLMVAQhLKVNRnmlsglfATPAYRRAERAALeraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMI 170
Cdd:PRK09493 87 YLFPHLTALENVMFGP-LRVRG-------ASKEEAEKQAREL------LAKVGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 171 TDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
12-256 |
1.70e-31 |
|
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: 119.05 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 12 LQMRFGGL-LAVDgidFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGH------AITGQPSHQvaRR-GL 83
Cdd:COG4148 7 FRLRRGGFtLDVD---FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsaRGIFLPPHR--RRiGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VrtFQNIRLFKQLTVLENLMVAQHLKVNRNMLSGLfatpayrraeraaleraAYWLERVGLKQVANREAGTLSYGHQRRL 163
Cdd:COG4148 82 V--FQEARLFPHLSVRGNLLYGRKRAPRAERRISF-----------------DEVVELLGIGHLLDRRPATLSGGERQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 164 EIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVR 243
Cdd:COG4148 143 AIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
250
....*....|...
gi 1787163341 244 NDPRVIKAYLGED 256
Cdd:COG4148 223 SRPDLLPLAGGEE 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-246 |
2.19e-31 |
|
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: 115.86 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNIRLFKQ 95
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKiGYV--IQQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENL-MVAQHLKVNRNMLsglfATPAYRRaeraaleraaywLERVGL--KQVANREAGTLSYGHQRRLEIARCMITD 172
Cdd:cd03295 90 MTVEENIaLVPKLLKWPKEKI----RERADEL------------LALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-255 |
3.81e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.62 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRT 86
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLfkQLTVLENLMV-AQHLKVNRNMLSGLFATpayrraeraaleraayWLERVGLKQVANREAGTLSYGHQRRLEI 165
Cdd:PRK13536 122 FDNLDL--EFTVRENLLVfGRYFGMSTREIEAVIPS----------------LLEFARLESKADARVSDLSGGMKRRLTL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRND 245
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
250
....*....|...
gi 1787163341 246 P---RVIKAYLGE 255
Cdd:PRK13536 263 HigcQVIEIYGGD 275
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-232 |
4.50e-31 |
|
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: 112.86 E-value: 4.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNIRLFKQlTVL 99
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNiAYV--PQDPFLFSG-TIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENLmvaqhlkvnrnmLSGlfatpayrraeraaleraaywlervglkqvanreagtlsyGHQRRLEIARCMITDPRLLMLD 179
Cdd:cd03228 94 ENI------------LSG----------------------------------------GQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 180 EPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGVsDRILVMEHGK 232
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-244 |
1.24e-30 |
|
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: 119.55 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNIRLFKQlTV 98
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQiGVV--LQDVFLFSG-TI 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 99 LENLmvaqhlkvnrnMLSGLFATPAyrraeraaleRAAYWLERVGLKQVANR----------EAGT-LSYGHQRRLEIAR 167
Cdd:COG2274 566 RENI-----------TLGDPDATDE----------EIIEAARLAGLHDFIEAlpmgydtvvgEGGSnLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 168 CMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGVsDRILVMEHGKPIMIGKPDEVRN 244
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLA-DRIIVLDKGRIVEDGTHEELLA 698
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-252 |
2.73e-30 |
|
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: 118.33 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRF--GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA 79
Cdd:COG4987 329 PGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 RR-GLVrtFQNIRLFKQlTVLENLMVAqhlkvNRNmlsglfATPAYRRAEraaleraaywLERVGLKQVANR-------- 150
Cdd:COG4987 409 RRiAVV--PQRPHLFDT-TLRENLRLA-----RPD------ATDEELWAA----------LERVGLGDWLAAlpdgldtw 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 151 --EAG-TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKvelQQMVDGLRNEF-GISVLLIEHDMSLvMGVSDRIL 226
Cdd:COG4987 465 lgEGGrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE---QALLADLLEALaGRTVLLITHRLAG-LERMDRIL 540
|
250 260
....*....|....*....|....*..
gi 1787163341 227 VMEHGKPIMIGKPDE-VRNDPRVIKAY 252
Cdd:COG4987 541 VLEDGRIVEQGTHEElLAQNGRYRQLY 567
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-242 |
2.76e-30 |
|
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: 112.94 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQ-PSHQVarrglvrTFQNIRLFKQLTVLE 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRMV-------VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHlKVNRNMLSGlfatpayrraerAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDE 180
Cdd:TIGR01184 74 NIALAVD-RVLPDLSKS------------ERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDE 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 181 PAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:TIGR01184 141 PFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-232 |
3.00e-30 |
|
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: 111.90 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVrPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRt 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 fQNIRLFKQLTVLENLmvaQHLKVNRNMLSGlfatpayrraerAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:cd03264 79 -QEFGVYPNFTVREFL---DYIAWLKGIPSK------------EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfgISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-241 |
3.58e-30 |
|
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: 117.94 E-value: 3.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVRtfQNIRLFKQ 95
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQiAWVP--QNPYLFAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 lTVLENLMVAQHLkvnrnmlsglfATPAyrraeraaleRAAYWLERVGLKQVANR----------EAGT-LSYGHQRRLE 164
Cdd:COG4988 426 -TIRENLRLGRPD-----------ASDE----------ELEAALEAAGLDEFVAAlpdgldtplgEGGRgLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMgVSDRILVMEHGKPIMIGKPDE 241
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEE 557
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
17-232 |
7.85e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.02 E-value: 7.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQV--ARR--GLVrtFQNIRL 92
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARRkiGMI--FQHFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 93 FKQLTVLENlmVA---QHLKVNR-------NMLsglfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRR 162
Cdd:COG1135 94 LSSRTVAEN--VAlplEIAGVPKaeirkrvAEL-----------------------LELVGLSDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-237 |
1.72e-29 |
|
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: 110.15 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRF----GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPshQVARR 81
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTFQNIRLFKQLTVLENLMVAQHLK-VNRNMLSGLFATPAyrraeraaleraaywlERVGLKQVANREAGTLSYGHQ 160
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYgLKGDELTARLEELA----------------DRLGMEELLDRRVGGFSTGMR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03266 143 QKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-247 |
2.42e-29 |
|
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: 112.45 E-value: 2.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRF----GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKP---TAGDIVLEGHAITGQPSHQV 78
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 AR-RG----LVrtFQN--------IRLFKQLTvlENLMVaqHLKVNRNmlsglfatpayrraerAALERAAYWLERVGL- 144
Cdd:COG0444 81 RKiRGreiqMI--FQDpmtslnpvMTVGDQIA--EPLRI--HGGLSKA----------------EARERAIELLERVGLp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 145 --KQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNP--QEKVeLQQMVDgLRNEFGISVLLIEHDMSLVMG 220
Cdd:COG0444 139 dpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAQI-LNLLKD-LQRELGLAILFITHDLGVVAE 216
|
250 260
....*....|....*....|....*..
gi 1787163341 221 VSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:COG0444 217 IADRVAVMYAGRIVEEGPVEELFENPR 243
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-255 |
2.64e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.87 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 16 FGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQpsHQVARR-GLVrtFQNIRLFK 94
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRKvGFV--FQHYALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 95 QLTVLENlmVAQHLKV--NRNMLSGlfatpayrraeRAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITD 172
Cdd:PRK10851 88 HMTVFDN--IAFGLTVlpRRERPNA-----------AAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP--RVIK 250
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPatRFVL 234
|
....*
gi 1787163341 251 AYLGE 255
Cdd:PRK10851 235 EFMGE 239
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-252 |
3.10e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA-RRGL 83
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELArRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VRtfQNIRLFKQLTVLEnlMVAqhlkvnrnmlsgLFATPaYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRL 163
Cdd:PRK13548 81 LP--QHSSLSFPFTVEE--VVA------------MGRAP-HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 164 EIAR--CMIT----DPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:PRK13548 144 QLARvlAQLWepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
250
....*....|....*
gi 1787163341 238 KPDEVRNDPRVIKAY 252
Cdd:PRK13548 224 TPAEVLTPETLRRVY 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-232 |
1.12e-28 |
|
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: 107.96 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 33 EVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPshqVARRGLVRTFQNIRLFKQLTVLEN--LMVAQHLKV 110
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRPVSMLFQENNLFAHLTVEQNvgLGLSPGLKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 111 N---RNMLSGLFAtpayrraeraaleraaywleRVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNP 187
Cdd:cd03298 102 TaedRQAIEVALA--------------------RVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1787163341 188 QEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03298 162 ALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-237 |
1.21e-28 |
|
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: 108.11 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPShqvARRGLVRT 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLmvAQHLKVNRnmlsglFATPAYRraeraaleraaywlERV-------GLKQVANREAGTLSYGH 159
Cdd:cd03301 78 FQNYALYPHMTVYDNI--AFGLKLRK------VPKDEID--------------ERVrevaellQIEHLLDRKPKQLSGGQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 160 QRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03301 136 RQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-248 |
1.78e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.08 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQV-- 78
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 ARRGLVRTFQNIRLFKQLTVLENlmVAQHLKVNRNMLSGLFATPAYRRaeraaleraaywLERVGLKQVANREAGTLSYG 158
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDN--VAYPLREHTQLPAPLLHSTVMMK------------LEAVGLRGAAKLMPSELSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 159 HQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGK 238
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|..
gi 1787163341 239 PDEVRN--DPRV 248
Cdd:PRK11831 228 AQALQAnpDPRV 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-242 |
2.62e-28 |
|
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: 112.20 E-value: 2.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRF-----GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDI-VLEGHAITGQPSHQVA 79
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 RRGLVRT-----FQNIRLFKQLTVLENLMVAQHLKvnrnmLSGLFAtpayrraeraaLERAAYWLERVGL-----KQVAN 149
Cdd:TIGR03269 359 GRGRAKRyigilHQEYDLYPHRTVLDNLTEAIGLE-----LPDELA-----------RMKAVITLKMVGFdeekaEEILD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 150 REAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVME 229
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|...
gi 1787163341 230 HGKPIMIGKPDEV 242
Cdd:TIGR03269 503 DGKIVKIGDPEEI 515
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-232 |
6.50e-28 |
|
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: 106.36 E-value: 6.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGG----LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQ 77
Cdd:COG4181 4 SSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 78 VARR-----GLVrtFQNIRLFKQLTVLENLMVAQHLKVNRNmlsgLFATPAYrraeraaleraayWLERVGLKQVANREA 152
Cdd:COG4181 84 RARLrarhvGFV--FQSFQLLPTLTALENVMLPLELAGRRD----ARARARA-------------LLERVGLGHRLDHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 153 GTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKvelQQMVD---GLRNEFGISVLLIEHDMSLVmGVSDRILVME 229
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATG---EQIIDllfELNRERGTTLVLVTHDPALA-ARCDRVLRLR 220
|
...
gi 1787163341 230 HGK 232
Cdd:COG4181 221 AGR 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-232 |
7.79e-28 |
|
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: 105.95 E-value: 7.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA--RRGLVRTFQNIRLFK 94
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 95 QLTVLENLMVAQHL-----KVNRNMLSGLfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCM 169
Cdd:cd03292 92 DRNVYENVAFALEVtgvppREIRKRVPAA--------------------LELVGLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 170 ITDPRLLMLDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-255 |
9.78e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.65 E-value: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQvar 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 RGLVRTFQNIRLFKQLTVLENlmVAQHLKvnrnMLSglfatpayrRAERAALERAAYWLERVGLKQVANREAGTLSYGHQ 160
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGEN--VGYGLK----MLG---------VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNP------QEKV-ELQQmvdglrnEFGISVLLIEHDMSLVMGVSDRILVMEHGKP 233
Cdd:PRK11432 143 QRVALARALILKPKVLLFDEPLSNLDAnlrrsmREKIrELQQ-------QFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
250 260
....*....|....*....|....
gi 1787163341 234 IMIGKPDEVRNDP--RVIKAYLGE 255
Cdd:PRK11432 216 MQIGSPQELYRQPasRFMASFMGD 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-254 |
1.20e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 106.12 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGL 83
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VRTFQNIRLFKQLTVLENLmvaqhlkvnrnMLSGLFAT-PAYRRAERAALERAAYWLERvglkqvANREAGTLSYGHQRR 162
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENL-----------AMGGFFAErDQFQERIKWVYELFPRLHER------RIQRAGTMSGGEQQM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK11614 146 LAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
250
....*....|..
gi 1787163341 243 RNDPRVIKAYLG 254
Cdd:PRK11614 225 LANEAVRSAYLG 236
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-232 |
1.34e-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: 104.44 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRfgglLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRG 82
Cdd:cd03215 1 GEPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LV-----RtfQNIRLFKQLTVLENLMVAQHLkvnrnmlSGlfatpayrraeraaleraaywlervglkqvanreagtlsy 157
Cdd:cd03215 77 IAyvpedR--KREGLVLDLSVAENIALSSLL-------SG---------------------------------------- 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 158 GHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-238 |
1.92e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 104.94 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 26 DFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQvarRGLVRTFQNIRLFKQLTVLENLMVA 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ---RPVSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 106 QH--LKVNRNMLSGLFATPayrraeraaleraaywlERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAA 183
Cdd:TIGR01277 95 LHpgLKLNAEQQEKVVDAA-----------------QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 184 GLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGK 238
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-235 |
2.33e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 109.63 E-value: 2.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYkPTA---GDIVLEGHAITGQPSHQVA 79
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 RRGLVRTFQNIRLFKQLTVLENLMVAQHLkvnrnmlsglfaTPAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGH 159
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEI------------TPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 160 QRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIM 235
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-242 |
2.70e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.29 E-value: 2.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQP---SHQVARRGLVRTFQNIRLFKQlT 97
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 V-------LENLMVAQ---HLKVNRNMlsglfatpayrraeraaleraaywlERVGLK--QVANREAGTLSYGHQRRLEI 165
Cdd:PRK13637 101 IekdiafgPINLGLSEeeiENRVKRAM-------------------------NIVGLDyeDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-250 |
3.57e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.54 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 18 GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR---GLVrtFQNI--RL 92
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRktvGIV--FQNPddQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 93 FKQlTVLE-------NLMVAQHLKVNRNMLSglfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEI 165
Cdd:PRK13639 92 FAP-TVEEdvafgplNLGLSKEEVEKRVKEA----------------------LKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRND 245
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
....*
gi 1787163341 246 PRVIK 250
Cdd:PRK13639 228 IETIR 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-232 |
4.78e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 104.76 E-value: 4.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIvLEGHAitgqPSHQvARRGLVRT 86
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA----PLAE-AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 FQNIRLFKQLTVLENLMVAqhlkvnrnmLSGLFATPAYRRaeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLG---------LKGQWRDAALQA------------LAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-235 |
7.88e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.40 E-value: 7.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRgLVRTFQNIRL--FKQLTV 98
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 99 LENLMVAQHLKVNRNMLSGLfaTPAYRRAERAAleraaywLERVGLkQVANR---EAGTLSyGHQRR-LEIARCMITDPR 174
Cdd:COG1101 100 EENLALAYRRGKRRGLRRGL--TKKRRELFREL-------LATLGL-GLENRldtKVGLLS-GGQRQaLSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 175 LLMLDEPAAGLNPQ--EKV-EL-QQMVdglrNEFGISVLLIEHDMS--LVMGvsDRILVMEHGKPIM 235
Cdd:COG1101 169 LLLLDEHTAALDPKtaALVlELtEKIV----EENNLTTLMVTHNMEqaLDYG--NRLIMMHEGRIIL 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-247 |
1.27e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.68 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAqalLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDI-VLEGHAITGQPSHQva 79
Cdd:PRK11264 1 MSA---IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrVGDITIDTARSLSQ-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 RRGLVR--------TFQNIRLFKQLTVLENLM----------VAQHLKVNRNMLSglfatpayrraeraaleraaywleR 141
Cdd:PRK11264 76 QKGLIRqlrqhvgfVFQNFNLFPHRTVLENIIegpvivkgepKEEATARARELLA------------------------K 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 142 VGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGV 221
Cdd:PRK11264 132 VGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDV 210
|
250 260
....*....|....*....|....*.
gi 1787163341 222 SDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK11264 211 ADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-249 |
1.42e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.92 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGG--LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVARR 81
Cdd:PRK13632 5 SVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS-KENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTFQNI-RLFKQLTV-------LENLMVaqhlkvNRNMLSGLFATPAyrraeraaleraaywlERVGLKQVANREAG 153
Cdd:PRK13632 84 KIGIIFQNPdNQFIGATVeddiafgLENKKV------PPKKMKDIIDDLA----------------KKVGMEDYLDKEPQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 154 TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMgVSDRILVMEHGKP 233
Cdd:PRK13632 142 NLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
250
....*....|....*.
gi 1787163341 234 IMIGKPDEVRNDPRVI 249
Cdd:PRK13632 221 IAQGKPKEILNNKEIL 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-249 |
3.58e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.16 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGG-----LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLE----GHAIT 71
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 72 GQPSHQVARRGLVRTFQNIR-------------LFKQlTVLENLMvaqhlkvnrnmlsglFATPAYRRAERAALERAAYW 138
Cdd:PRK13631 96 NHELITNPYSKKIKNFKELRrrvsmvfqfpeyqLFKD-TIEKDIM---------------FGPVALGVKKSEAKKLAKFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 LERVGLKQ-VANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSL 217
Cdd:PRK13631 160 LNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEH 238
|
250 260 270
....*....|....*....|....*....|..
gi 1787163341 218 VMGVSDRILVMEHGKPIMIGKPDEVRNDPRVI 249
Cdd:PRK13631 239 VLEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-250 |
5.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.00 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFG-GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItgqpshQVARRGLV 84
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI------DYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQLTVLENLMVAQHLKVNrnmlsglFATPAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLE 164
Cdd:PRK13636 79 KLRESVGMVFQDPDNQLFSASVYQDVS-------FGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN 244
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
....*.
gi 1787163341 245 DPRVIK 250
Cdd:PRK13636 232 EKEMLR 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-215 |
5.33e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.09 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGqPShqvARRGLVr 85
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PG---AERGVV- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 tFQNIRLFKQLTVLENLMV---------AQHLKVNRNMLSglfatpayrraeraaleraaywleRVGLKQVANREAGTLS 156
Cdd:PRK11248 76 -FQNEGLLPWRNVQDNVAFglqlagvekMQRLEIAHQMLK------------------------KVGLEGAEKRYIWQLS 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 157 YGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDM 215
Cdd:PRK11248 131 GGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-256 |
7.21e-26 |
|
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: 105.29 E-value: 7.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYK--PTAGDIVLEGHAITGQPSHQVARRGL 83
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VRTFQNIRLFKQLTVLENLMVAQHLKVNrnmlSGLFATPAYRRAERAAleraaywLERVGLKQVAN-REAGTLSYGHQRR 162
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLP----GGRMAYNAMYLRAKNL-------LRELQLDADNVtRPVGDYGGGQQQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIgKPDEV 242
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMST 227
|
250
....*....|....
gi 1787163341 243 RNDPRVIKAYLGED 256
Cdd:TIGR02633 228 MSEDDIITMMVGRE 241
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-242 |
1.49e-25 |
|
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: 100.38 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVaRRGLVRTFQNIRLFkQL 96
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-RSMIGVVLQDTFLF-SG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENlmvaqhLKVNRNMlsglfaTPAYRRAERAALERAAYWLERV--GLKQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:cd03254 92 TIMEN------IRLGRPN------ATDEEVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDEV 242
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-247 |
1.56e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 100.81 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAIT------GQ------P 74
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdGQlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 75 SHQVARRGLVRTFQNIRLFKQLTVLENLMVA--QHLkvnrnmlsGLFATPAyrraeraaLERAAYWLERVGLKQVAN-RE 151
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEApiQVL--------GLSKQEA--------RERAVKYLAKVGIDERAQgKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 152 AGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHG 231
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
250
....*....|....*.
gi 1787163341 232 KPIMIGKPDEVRNDPR 247
Cdd:PRK10619 229 KIEEEGAPEQLFGNPQ 244
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-234 |
2.14e-25 |
|
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: 104.41 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGG--LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVAR 80
Cdd:TIGR02203 327 ARGDVEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA-DYTLASLR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 RGLVRTFQNIRLFKQlTVLENLMVAqhlkvnrnmlsglfATPAYRRAERAALERAAYWLERV-----GLKQVANREAGTL 155
Cdd:TIGR02203 406 RQVALVSQDVVLFND-TIANNIAYG--------------RTEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLL 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 156 SYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGvSDRILVMEHGKPI 234
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIV 546
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-247 |
2.69e-25 |
|
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: 104.00 E-value: 2.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRF---GGLL--------AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYkPTAGDIVLEGHAI 70
Cdd:COG4172 271 DAPPLLEARDLKVWFpikRGLFrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 71 TGQPSHqvARRGLVRTFQ----------NIRLfkqlTVLEnlMVAQHLKVNRNMLSGlfatpayrraeRAALERAAYWLE 140
Cdd:COG4172 350 DGLSRR--ALRPLRRRMQvvfqdpfgslSPRM----TVGQ--IIAEGLRVHGPGLSA-----------AERRARVAEALE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 141 RVGLK-QVANReagtlsYGH-----QR-RLEIARCMITDPRLLMLDEPAAGLNpqekVELQ-QMVDGLRN---EFGISVL 209
Cdd:COG4172 411 EVGLDpAARHR------YPHefsggQRqRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDLLRDlqrEHGLAYL 480
|
250 260 270
....*....|....*....|....*....|....*...
gi 1787163341 210 LIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:COG4172 481 FISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-232 |
2.71e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.56 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRfgglLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR 81
Cdd:COG1129 252 PGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLV-----RTFQNirLFKQLTVLENLMVAQHLKVNRNmlsGLFATPAyrraeraALERAAYWLERVGLKqVANRE--AGT 154
Cdd:COG1129 328 GIAyvpedRKGEG--LVLDLSIRENITLASLDRLSRG---GLLDRRR-------ERALAEEYIKRLRIK-TPSPEqpVGN 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 155 LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:COG1129 395 LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
12-241 |
4.07e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 99.27 E-value: 4.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 12 LQMRFggllavdgiDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPShqvARRGLVRTFQNIR 91
Cdd:PRK10771 14 LPMRF---------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRPVSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 92 LFKQLTVLENLMVAQH--LKVNRNMLSGLFATpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCM 169
Cdd:PRK10771 82 LFSHLTVAQNIGLGLNpgLKLNAAQREKLHAI-----------------ARQMGIEDLLARLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 170 ITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-255 |
7.20e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRglvrt 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 fqnIRLFKQLTVLE-NLMVAQHLKVNRNMLSGLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQRRLEI 165
Cdd:PRK09536 79 ---VASVPQDTSLSfEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERA-----MERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRND 245
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
250
....*....|
gi 1787163341 246 PRVIKAYLGE 255
Cdd:PRK09536 230 DTLRAAFDAR 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-242 |
1.37e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.72 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNI--RLFKQlt 97
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFvGLV--FQNPddQIFSP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 vlenlMVAQHLKVNRNMLSGLFATPAYRRAERaaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLM 177
Cdd:PRK13652 95 -----TVEQDIAFGPINLGLDEETVAHRVSSA---------LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 178 LDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-247 |
2.45e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.68 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTT---VFNCVGGFYKP--TAGDIVLEGHAITGQPSHQV 78
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTllrVFNRLIELYPEarVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 ARRgLVRTFQNIRLFKQLTVLENlmVAQHLKVNRNMLSglfatpayrraERAALERAAYWLERVGL-KQVANR---EAGT 154
Cdd:PRK14247 81 RRR-VQMVFQIPNPIPNLSIFEN--VALGLKLNRLVKS-----------KKELQERVRWALEKAQLwDEVKDRldaPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 155 LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfgISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
250
....*....|...
gi 1787163341 235 MIGKPDEVRNDPR 247
Cdd:PRK14247 225 EWGPTREVFTNPR 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-247 |
3.48e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.10 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQV--ARRGLVRTFQNIRLFK 94
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkARRQIGMIFQHFNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 95 QLTVLENlmVAQHLKvnrnmLSGlfaTPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:PRK11153 96 SRTVFDN--VALPLE-----LAG---TPKAEIKARVTEL-----LELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 175 LLMLDEPAAGLNPQEKvelQQMVDGLRN---EFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK11153 161 VLLCDEATSALDPATT---RSILELLKDinrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-246 |
6.30e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.95 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQmrfgglLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEG---HAITGQPSHQ 77
Cdd:PRK10070 29 LSKEQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 78 VARRGLVRTFQNIRLFKQLTVLENLMVAQHLkvnrnmlSGLFATPAYRRAERAaleraaywLERVGLKQVANREAGTLSY 157
Cdd:PRK10070 103 VRRKKIAMVFQSFALMPHMTVLDNTAFGMEL-------AGINAEERREKALDA--------LRQVGLENYAHSYPDELSG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 158 GHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:PRK10070 168 GMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
....*....
gi 1787163341 238 KPDEVRNDP 246
Cdd:PRK10070 248 TPDEILNNP 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-251 |
6.76e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 99.74 E-value: 6.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVAR 80
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 RGLVRTFQNIRLFKQLTVLENLmvaqhlkvnrnmlsgLFATPAYRRAERAALERaaywLERVGLKQVANREAGTLSYGHQ 160
Cdd:PRK15439 86 LGIYLVPQEPLLFPNLSVKENI---------------LFGLPKRQASMQKMKQL----LAALGCQLDLDSSAGSLEVADR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPD 240
Cdd:PRK15439 147 QIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTA 225
|
250
....*....|.
gi 1787163341 241 EVrNDPRVIKA 251
Cdd:PRK15439 226 DL-STDDIIQA 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-242 |
1.08e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.62 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGL--LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVAR 80
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 R-GLVrtFQNI-RLFKQLTV-------LENLMVAQHLKVNRnmlsglfatpayrraeraalerAAYWLERVGLKQVANRE 151
Cdd:PRK13635 82 QvGMV--FQNPdNQFVGATVqddvafgLENIGVPREEMVER----------------------VDQALRQVGMEDFLNRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 152 AGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHG 231
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
250
....*....|.
gi 1787163341 232 KPIMIGKPDEV 242
Cdd:PRK13635 217 EILEEGTPEEI 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-242 |
1.20e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNI-RLFKQLTV- 98
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKiGMV--FQNPdNQFVGATVe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 99 ------LENLMVAQHLKVNRnmlsglfatpayrraeraalerAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITD 172
Cdd:PRK13650 101 ddvafgLENKGIPHEEMKER----------------------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVmGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
17-232 |
1.32e-23 |
|
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: 94.63 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEghaitGQPSHQVARRGLVrtfqnirlfkql 96
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN-----GKPIKAKERRKSI------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 tvlenLMVAQHLK-------VNRNMLSGLFATPAYRRAERAAleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCM 169
Cdd:cd03226 74 -----GYVMQDVDyqlftdsVREELLLGLKELDAGNEQAETV-------LKDLDLYALKERHPLSLSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 170 ITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-232 |
2.09e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.44 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRG 82
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVRTFQNIRLFKQLTVLENLMVAQ----HLKVNRNMLsglfatpayrraeraaLERAAYWLERVGLKQVANREAGTLSYG 158
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENLYLGQlphkGGIVNRRLL----------------NYEAREQLEHLGVDIDPDTPLKYLSIG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 159 HQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
7-228 |
5.19e-23 |
|
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: 97.36 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGG-LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVaRRGLVR 85
Cdd:TIGR02857 322 LEFSGVSVAYPGrRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 TFQNIRLFKQlTVLENLMVAQhlkvnrnmlsgLFATPAYRRAEraaleraaywLERVGLKQ-VANREAGT---------- 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR-----------PDASDAEIREA----------LERAGLDEfVAALPQGLdtpigeggag 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 155 LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLvMGVSDRILVM 228
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLAL-AALADRIVVL 529
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-247 |
9.86e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.77 E-value: 9.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFG-------------GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAI 70
Cdd:PRK15079 6 KVLLEVADLKVHFDikdgkqwfwqppkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 71 TGQPSHQ--VARRGLVRTFQN--IRLFKQLTVLEnlMVAQHLKVNRNMLSglfatpayrraERAALERAAYWLERVGL-K 145
Cdd:PRK15079 86 LGMKDDEwrAVRSDIQMIFQDplASLNPRMTIGE--IIAEPLRTYHPKLS-----------RQEVKDRVKAMMLKVGLlP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 146 QVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNpqekVELQ-QMVDGLRN---EFGISVLLIEHDMSLVMGV 221
Cdd:PRK15079 153 NLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD----VSIQaQVVNLLQQlqrEMGLSLIFIAHDLAVVKHI 228
|
250 260
....*....|....*....|....*.
gi 1787163341 222 SDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK15079 229 SDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-256 |
1.27e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.38 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHaitgQPSHQvaRRGLVRTF-----QNIRLFKQ 95
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----VPFKR--RKEFARRIgvvfgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENLMVAQHL--------KVNRNMLSGLFatpayrraeraaleraaywlervGLKQVANREAGTLSYGhQR-RLEIA 166
Cdd:COG4586 111 LPAIDSFRLLKAIyripdaeyKKRLDELVELL-----------------------DLGELLDTPVRQLSLG-QRmRCELA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN-- 244
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKErf 246
|
250
....*....|...
gi 1787163341 245 -DPRVIKAYLGED 256
Cdd:COG4586 247 gPYKTIVLELAEP 259
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-242 |
1.44e-22 |
|
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: 92.55 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 18 GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAI-TGQPSHQVARRGLVrtFQNIRLFKQl 96
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVV--LQENVLFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENLMVAQHLKVNRNMLSGLFATPAYRRAERAaleraaywleRVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGAHDFISEL----------PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 177 MLDEPAAGLNPQ-EKVELQQMVDGLRnefGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDEV 242
Cdd:cd03252 161 IFDEATSALDYEsEHAIMRNMHDICA---GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-241 |
1.44e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.00 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNIRLFkQLTVL 99
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQiGVV--PQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENLmvaqhlkvnrnmlsgLFATPAYRraeraaleraaywLERV------------------GLKQVANREAGTLSYGhQR 161
Cdd:COG1132 432 ENI---------------RYGRPDAT-------------DEEVeeaakaaqahefiealpdGYDTVVGERGVNLSGG-QR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 -RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGVsDRILVMEHGKPIMIGKPD 240
Cdd:COG1132 483 qRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNA-DRILVLDDGRIVEQGTHE 559
|
.
gi 1787163341 241 E 241
Cdd:COG1132 560 E 560
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-214 |
1.61e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKP---TAGDIVLEGHAITGQPSHQvaRR-G 82
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ--RRiG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVrtFQNIRLFKQLTVLENLmvaqhlkvnrnmlsgLFATPAYRRAERAALERAAYwLERVGLKQVANREAGTLSYGHQRR 162
Cdd:COG4136 80 IL--FQDDLLFPHLSVGENL---------------AFALPPTIGRAQRRARVEQA-LEEAGLAGFADRDPATLSGGQRAR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHD 214
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
36-251 |
2.72e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 36 AIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-----GLVRTFQNIRLFKQlTVLENLMvaqhlkv 110
Cdd:PRK13634 37 AIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPlrkkvGIVFQFPEHQLFEE-TVEKDIC------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 111 nrnmlsglFATPAYRRAERAALERAAYWLERVGL-KQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQE 189
Cdd:PRK13634 109 --------FGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 190 KVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPRVIKA 251
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-252 |
3.17e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPT-----AGDIVLEGHAITGQPSHQVARRGLVRTFQNIRLFKQlTVL 99
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkvtVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEE-TVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENLMVA-QHLKVNRNMLSGLFATPayrraeraaleraaywLERVGL-KQVANREAGTLSYGHQRRLEIARCMITDPRLLM 177
Cdd:PRK13643 104 KDVAFGpQNFGIPKEKAEKIAAEK----------------LEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 178 LDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPRVIKAY 252
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAH 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-243 |
4.86e-22 |
|
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: 90.28 E-value: 4.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGF--YKPTAGDIVLEGHAITGQPSHQVARRGLV 84
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQLTVLENLmvaqhlkvnRNMLSGlfatpayrraeraaleraaywlervglkqvanreagtLSYGHQRRLE 164
Cdd:cd03217 81 LAFQYPPEIPGVKNADFL---------RYVNEG-------------------------------------FSGGEKKRNE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEH-DMSLVMGVSDRILVMEHGKPIMIGKPDEVR 243
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-232 |
4.89e-22 |
|
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: 90.99 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVARRGLVRTFQNIRLFKQlTVL 99
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENlmVAQHLKvNRNMLSGLFATPAYRRAERAALERAAYWLErvglkqvANREAGTLSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:cd03248 106 DN--IAYGLQ-SCSFECVKEAAQKAHAHSFISELASGYDTE-------VGEKGSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 180 EPAAGLNPQEKVELQQMV-DGLRNEfgiSVLLIEHDMSLVMGvSDRILVMEHGK 232
Cdd:cd03248 176 EATSALDAESEQQVQQALyDWPERR---TVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-256 |
1.01e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 93.70 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 12 LQMR-----FGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYkPTA---GDIVLEGHAITGQPSHQVARRGL 83
Cdd:NF040905 2 LEMRgitktFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VRTFQNIRLFKQLTVLENLM----VAQHLKVNRNmlsglfatpayrraerAALERAAYWLERVGLKQVANREAGTLSYGH 159
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFlgneRAKRGVIDWN----------------ETNRRARELLAKVGLDESPDTLVTDIGVGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 160 QRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPI--MIG 237
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIetLDC 223
|
250
....*....|....*....
gi 1787163341 238 KPDEVRNDpRVIKAYLGED 256
Cdd:NF040905 224 RADEVTED-RIIRGMVGRD 241
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-231 |
1.21e-21 |
|
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: 89.80 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRF-----GG--LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVL--EGHAI--TG 72
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 73 QPSHQVA--RR---GLVRTFqnIRLFKQLTVLEnlMVAQHLkvnrnmlsglfatpayrraeraaleraaywLERVGLKQV 147
Cdd:COG4778 82 ASPREILalRRrtiGYVSQF--LRVIPRVSALD--VVAEPL------------------------------LERGVDREE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 148 ANREAGTL------------------SYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVL 209
Cdd:COG4778 128 ARARARELlarlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAII 206
|
250 260
....*....|....*....|..
gi 1787163341 210 LIEHDMSLVMGVSDRILVMEHG 231
Cdd:COG4778 207 GIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-185 |
1.30e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAIT----GQPSHQVARRG 82
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdpdvAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 LVRTFqnirlfkqLTVLENLMVAQHLKVNRNmlsgLFATPAyrraeraaleraaywLERVGLKQVANREAGTLSYGHQRR 162
Cdd:PRK13539 83 AMKPA--------LTVAENLEFWAAFLGGEE----LDIAAA---------------LEAVGLAPLAHLPFGYLSAGQKRR 135
|
170 180
....*....|....*....|...
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGL 185
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAAL 158
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-237 |
1.58e-21 |
|
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: 89.19 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVARRGLVRTFQNIRLFKQlTVLE 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIR-QLDPADLRRNIGYVPQDVTLFYG-TLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHLKVNRNMLSGlfatpayrraeraaleraaywLERVGLKQVANR----------EAG-TLSYGHQRRLEIARCM 169
Cdd:cd03245 97 NITLGAPLADDERILRA---------------------AELAGVTDFVNKhpngldlqigERGrGLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 170 ITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGVsDRILVMEHGKPIMIG 237
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLV-DRIIVMDSGRIVADG 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
30-241 |
2.77e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.42 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 30 RPDEVFAIIGPNGAGKTTVFNCVGgFYKPT----AGDIVLEGHAITGQPSHqvARRGLVRtfQNIRLFKQLTVLENLMVA 105
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMR--AISAYVQ--QDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 106 QHLKVNRNMLSglfatpayrraeRAALERAAYWLERVGLKQVANREAGT------LSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:TIGR00955 124 AHLRMPRRVTK------------KEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 180 EPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-251 |
3.21e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.48 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 24 GIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVARRGLVRTFQNIRLFKQltvlenlm 103
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHHYLHRQVALVGQEPVLFSG-------- 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 104 vaqhlKVNRNMLSGLFATPAYRRAERAALERAAYWLErvGLKQVANREAGT----LSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:TIGR00958 570 -----SVRENIAYGLTDTPDEEIMAAAKAANAHDFIM--EFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 180 EPAAGLNpqekVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDEVRNDPRVIKA 251
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-232 |
3.33e-21 |
|
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: 88.93 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRTfQNIRLFKQLTVLE 100
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFG-QKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHL--------KVNRNMLSGLFAtpayrraeraaleraaywLERVgLKQVANReagtLSYGHQRRLEIARCMITD 172
Cdd:cd03267 115 SFYLLAAIydlpparfKKRLDELSELLD------------------LEEL-LDTPVRQ----LSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-232 |
4.17e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 16 FGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA--RRGLVRTFQNIRLF 93
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KQLTVLENLMV------AQHLKVNRNMLSGlfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIAR 167
Cdd:PRK10908 92 MDRTVYDNVAIpliiagASGDDIRRRVSAA---------------------LDKVGLLDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 168 CMITDPRLLMLDEPAAGLNPqekvELQQMVDGLRNEF---GISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDD----ALSEGILRLFEEFnrvGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-244 |
6.29e-21 |
|
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: 92.00 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 18 GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItgQPSHQVARRGLVRTFQNIRLFKQLT 97
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 VLENLMVAQHLKvNRNMLSGLFATPAYrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLM 177
Cdd:TIGR01257 1020 VAEHILFYAQLK-GRSWEEAQLEMEAM--------------LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 178 LDEPAAGLNPQEKVELQQMVdgLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN 244
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-241 |
6.98e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.18 E-value: 6.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGqpshqVARRGLVRT----FQNIRLFKQl 96
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT-----VTRASLRRNiavvFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENLMVAQHLKVNRNMLSGLFATPAYRraeraaleraayWLER--VGLKQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:PRK13657 424 SIEDNIRVGRPDATDEEMRAAAERAQAHD------------FIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDE 241
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDE 555
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-242 |
8.80e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 8.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItgqpshQVARRGLVR 85
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL------DYSKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 TFQNIRLFKQ---------------LTVLENLMVAQHlKVNRNMLSGLFATPAyrraeraaleraaywlervglKQVANR 150
Cdd:PRK13638 75 LRQQVATVFQdpeqqifytdidsdiAFSLRNLGVPEA-EITRRVDEALTLVDA---------------------QHFRHQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 151 EAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEH 230
Cdd:PRK13638 133 PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQ 211
|
250
....*....|..
gi 1787163341 231 GKPIMIGKPDEV 242
Cdd:PRK13638 212 GQILTHGAPGEV 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-231 |
9.27e-21 |
|
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: 91.23 E-value: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHqvarrglvrTFQNIRLFKQLTVLE 100
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---------VHQNMGYCPQFDAID 2024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVA-QHLKvnrnMLSGLFATPAyrraeRAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:TIGR01257 2025 DLLTGrEHLY----LYARLRGVPA-----EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLD 2095
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 180 EPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHG 231
Cdd:TIGR01257 2096 EPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-242 |
1.05e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 87.59 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDG----IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYkPTAGDIVLEGHAITGQPSHQVARRglvRTF--QNIRLF 93
Cdd:COG4138 6 VAVAGrlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARH---RAYlsQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KQLTVLENLMVAQHLKVNRNMLSGLFAtpayrraeraaleraaYWLERVGLKQVANREAGTLSYGHQRRLEIARCMIT-- 171
Cdd:COG4138 82 FAMPVFQYLALHQPAGASSEAVEQLLA----------------QLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvw 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 172 -----DPRLLMLDEPAAGLNpqekVELQQMVDGLRNEF---GISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:COG4138 146 ptinpEGQLLLLDEPMNSLD----VAQQAALDRLLRELcqqGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-218 |
1.06e-20 |
|
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: 86.64 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAI---TGQPSHQVARRGL 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 84 VRTFQNirlfkQLTVLENLMVAQHL-KVNRNMLSGLfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRR 162
Cdd:TIGR01189 81 LPGLKP-----ELSALENLHFWAAIhGGAQRTIEDA--------------------LAAVGLTGFEDLPAAQLSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLV 218
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-242 |
1.35e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 8 KVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRglvrtf 87
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 88 qnIRLFKQ-------LTVLE------------NLMVAQHLKVNRnmlsglfAtpayrraeraaleraaywLERVGLKQVA 148
Cdd:COG4604 77 --LAILRQenhinsrLTVRElvafgrfpyskgRLTAEDREIIDE-------A------------------IAYLDLEDLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 149 NREAGTLSyGHQR-RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILV 227
Cdd:COG4604 130 DRYLDELS-GGQRqRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVA 208
|
250
....*....|....*
gi 1787163341 228 MEHGKPIMIGKPDEV 242
Cdd:COG4604 209 MKDGRVVAQGTPEEI 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-241 |
1.43e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 87.29 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVRtfQNIRLFKQlTVL 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQiGLVS--QDVFLFND-TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENLMvaqhlkvnrnmlsglFATPAYRRAERAALERAAYWLERV-----GLKQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:cd03251 94 ENIA---------------YGRPGATREEVEEAARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDE 241
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-245 |
1.92e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFykpTAGDIVLEGH----AITGQPSHQVA 79
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHiellGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 ---RRGLVRT---FQNIRLFKQLTVLENLMVAqhlkvnrnmlsGLFATPAYRR----AERAALERAAYWLERVGLKQVAN 149
Cdd:PRK09984 79 rdiRKSRANTgyiFQQFNLVNRLSVLENVLIG-----------ALGSTPFWRTcfswFTREQKQRALQALTRVGMVHFAH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 150 REAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVME 229
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALR 227
|
250
....*....|....*.
gi 1787163341 230 HGKPIMIGKPDEVRND 245
Cdd:PRK09984 228 QGHVFYDGSSQQFDNE 243
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-251 |
2.19e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.48 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 18 GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQNI--RLFK 94
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKvGLV--FQDPddQVFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 95 QlTVLENLMVAQhlkvnRNMlsGLFATPAYRRAERAaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:PRK13647 95 S-TVWDDVAFGP-----VNM--GLDKDEVERRVEEA--------LKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPdEVRNDPRVIKA 251
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIVEQ 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-214 |
2.59e-20 |
|
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: 89.73 E-value: 2.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRF-GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVr 85
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 TFQNIRLFKQlTVLENLMVAQHLKVNRNMLSGLFAtpayrraeraalERAAYWLERV--GLKQVANREAGTLSYGHQRRL 163
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLARPDATDEELWAALER------------VGLADWLRALpdGLDTVLGEGGARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 164 EIARCMITDPRLLMLDEPAAGLNPqeKVELQQMVDGLRNEFGISVLLIEHD 214
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDA--ETADELLEDLLAALSGRTVVLITHH 529
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-242 |
4.24e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.22 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRglvrt 86
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 fqnIRLFKQ-LTVLENLMVAQHLKVNRNMLSGLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQRRLEI 165
Cdd:PRK11231 78 ---LALLPQhHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQA-----MEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-247 |
1.43e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.17 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA--RRGLVRTFQN--IRLFKQL 96
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVFQNpyGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENLmvAQHLKVNRNMLSGLFATPAYRRaeraaleraaywLERVGLK-QVANREAGTLSYGHQRRLEIARCMITDPRL 175
Cdd:PRK11308 110 KVGQIL--EEPLLINTSLSAAERREKALAM------------MAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 176 LMLDEPAAGLNP--QEKVeLQQMVDgLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK11308 176 VVADEPVSALDVsvQAQV-LNLMMD-LQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-237 |
1.84e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHA--ITGQPSHQVARR--- 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 --GLVrtFQNIRLFKQLTVLENLMVA--QHLKVNRnmlsglfatpayrraeRAALERAAYWLERVGLKQVANREAGTLSY 157
Cdd:COG4161 83 kvGMV--FQQYNLWPHLTVMENLIEApcKVLGLSK----------------EQAREKAMKLLARLRLTDKADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 158 GHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-232 |
2.00e-19 |
|
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: 82.65 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGL--LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEghaitGQPSHQVARRGLV 84
Cdd:cd03246 1 LEVENVSFRYPGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-----GADISQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTF----QNIRLFKQlTVLENLmvaqhlkvnrnmLSGlfatpayrraeraaleraaywlervglkqvanreagtlsyGHQ 160
Cdd:cd03246 76 DHVgylpQDDELFSG-SIAENI------------LSG----------------------------------------GQR 102
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 161 RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRnEFGISVLLIEHDMSLVMGVsDRILVMEHGK 232
Cdd:cd03246 103 QRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLASA-DRILVLEDGR 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-232 |
3.09e-19 |
|
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: 86.28 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGG----LLAVDGIDFDVRPDEVFAIIGPNGAGKT----TVFNCVGGFYKPTAGDIVLEGHAITG 72
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 73 QPSHQVAR-RG----LVrtFQ------N--IRLFKQLTvlENLMVaqHLKVNRN-----MLSglfatpayrraeraaler 134
Cdd:COG4172 81 LSERELRRiRGnriaMI--FQepmtslNplHTIGKQIA--EVLRL--HRGLSGAaararALE------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 135 aayWLERVGLKQVANREAgtlSYGH-----QR-RLEIARCMITDPRLLMLDEPAAGLNpqekVELQ-QMVD---GLRNEF 204
Cdd:COG4172 137 ---LLERVGIPDPERRLD---AYPHqlsggQRqRVMIAMALANEPDLLIADEPTTALD----VTVQaQILDllkDLQREL 206
|
250 260
....*....|....*....|....*...
gi 1787163341 205 GISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:COG4172 207 GMALLLITHDLGVVRRFADRVAVMRQGE 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-242 |
3.89e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSH----QVARR-GLVRTFQNIRLFKQ 95
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQIRKKvGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 lTVLENlmVAqhlkvnrnmlsglFATPAYRRAERAALERAAYWLERVGL-KQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:PRK13649 102 -TVLKD--VA-------------FGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
16-234 |
4.29e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.94 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 16 FGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRTFQNIRLFKQ 95
Cdd:PRK10982 8 FPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENLMVAqhlkvnRNMLSGLFATPAYRRAERAALeraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRL 175
Cdd:PRK10982 88 RSVMDNMWLG------RYPTKGMFVDQDKMYRDTKAI------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 176 LMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-242 |
5.07e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITG--QPSHQVARR----GLVRTFQNIRLFk 94
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLrkeiGLVFQFPEYQLF- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 95 QLTVLENLMVAQ-HLKVNRNmlsglfatPAYRRAERAaleraaywLERVGL-KQVANREAGTLSYGHQRRLEIARCMITD 172
Cdd:PRK13645 105 QETIEKDIAFGPvNLGENKQ--------EAYKKVPEL--------LKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-232 |
8.10e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV---RTFQNIRLFKQLTVLEN 101
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpEDRQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 LMVaqhLKVNRNmlsGLFATPAYRRAEraaleraaywLER----VGLK-QVANREAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:PRK15439 362 VCA---LTHNRR---GFWIKPARENAV----------LERyrraLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 177 MLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-225 |
9.01e-19 |
|
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: 81.39 E-value: 9.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQP----------SH 76
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiargllylGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 77 QVARRGLVRTFQNIRLFKQLTVLENLMVAqhlkvnrnmlsglfatpayrraeraaleraaywLERVGLKQVANREAGTLS 156
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEA---------------------------------LARVGLNGFEDRPVAQLS 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 157 YGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRI 225
Cdd:cd03231 128 AGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-253 |
9.30e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 9.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGdivleghaitgqpshQVARRGLVRT-------FQNirlf 93
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG---------------RVEVNGRVSAllelgagFHP---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 kQLTVLENL-MVAQHLKVNRNMLSGL------FAtpayrraeraaleraaywlervGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:COG1134 102 -ELTGRENIyLNGRLLGLSRKEIDEKfdeiveFA----------------------ELGDFIDQPVKTYSSGMRARLAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEP-AAG-LNPQEKVE--LQQMVDGlrnefGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEv 242
Cdd:COG1134 159 VATAVDPDILLVDEVlAVGdAAFQKKCLarIRELRES-----GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE- 232
|
250
....*....|.
gi 1787163341 243 rndprVIKAYL 253
Cdd:COG1134 233 -----VIAAYE 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-247 |
1.51e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.52 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRF---GGLL--------AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQP 74
Cdd:PRK10261 313 ILQVRNLVTRFplrSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 75 SH--QVARRGLVRTFQN--IRLFKQLTVLENLMvaQHLKVNrNMLSGLFAtpayrraeraaLERAAYWLERVGLK-QVAN 149
Cdd:PRK10261 393 PGklQALRRDIQFIFQDpyASLDPRQTVGDSIM--EPLRVH-GLLPGKAA-----------AARVAWLLERVGLLpEHAW 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 150 REAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVME 229
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY 538
|
250
....*....|....*...
gi 1787163341 230 HGKPIMIGKPDEVRNDPR 247
Cdd:PRK10261 539 LGQIVEIGPRRAVFENPQ 556
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
34-242 |
1.69e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.39 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 34 VFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAI--TGQ----PSHQvaRR-GLVrtFQNIRLFKQLTVLENL---- 102
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKgiclPPEK--RRiGYV--FQDARLFPHYKVRGNLrygm 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 103 ---MVAQHLKVnrnmlsglfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:PRK11144 102 aksMVAQFDKI----------------------------VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 180 EPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-245 |
1.90e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.83 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 19 LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIV----------------LEGHAITGQPSH------ 76
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktkekeKVLEKLVIQKTRfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 77 --QVARR-GLVRTFQNIRLFKQlTVLENLMvaqhlkvnrnmlsglFATPAYRRAERAALERAAYWLERVGLKQ-VANREA 152
Cdd:PRK13651 100 ikEIRRRvGVVFQFAEYQLFEQ-TIEKDII---------------FGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 153 GTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKRTIFFKDGK 242
|
250
....*....|...
gi 1787163341 233 PIMIGKPDEVRND 245
Cdd:PRK13651 243 IIKDGDTYDILSD 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-242 |
2.43e-18 |
|
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: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMR-FGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV 84
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RtfqnI---R----LFKQLTVLENLMVaqhlkvnrnmlsGLFATPAYRRAEraaleraayWLERVGLKQVANR------- 150
Cdd:COG3845 337 Y----IpedRlgrgLVPDMSVAENLIL------------GRYRRPPFSRGG---------FLDRKAIRAFAEElieefdv 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 151 -------EAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNP--QEKVeLQQMVDgLRNEfGISVLLIEHDMSLVMGV 221
Cdd:COG3845 392 rtpgpdtPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVgaIEFI-HQRLLE-LRDA-GAAVLLISEDLDEILAL 468
|
250 260
....*....|....*....|.
gi 1787163341 222 SDRILVMEHGKPIMIGKPDEV 242
Cdd:COG3845 469 SDRIAVMYEGRIVGEVPAAEA 489
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-242 |
2.67e-18 |
|
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: 83.64 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGG--LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItgqpsHQVARR 81
Cdd:COG4618 328 KGRLSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL-----SQWDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRTF----QNIRLFKQlTVLEN------------LMVAQHLKVNRnMLSGL---FATpayrraeraaleraaywleRV 142
Cdd:COG4618 403 ELGRHIgylpQDVELFDG-TIAENiarfgdadpekvVAAAKLAGVHE-MILRLpdgYDT-------------------RI 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 143 GlkqvanrEAGT-LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLvMGV 221
Cdd:COG4618 462 G-------EGGArLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSL-LAA 532
|
250 260
....*....|....*....|.
gi 1787163341 222 SDRILVMEHGKPIMIGKPDEV 242
Cdd:COG4618 533 VDKLLVLRDGRVQAFGPRDEV 553
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-237 |
2.75e-18 |
|
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: 79.90 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGG--FYKPTAGDIvleghAITGQPSHQVARR---GLVRtfQNIRLFKQL 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEV-----LINGRPLDKRSFRkiiGYVP--QDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENLMVAQHLKVnrnmLSGlfatpayrraeraaleraaywlervglkqvanreagtlsyGHQRRLEIARCMITDPRLL 176
Cdd:cd03213 98 TVRETLMFAAKLRG----LSG----------------------------------------GERKRVSIALELVSNPSLL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 177 MLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMS-LVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-243 |
3.81e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.48 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAG--KTTVFNCVGGfykPTAGDIVLEGHAITGQpshqvaR 80
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCAN------R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 RGLVRTFQNIRLFK-----QLTVLENL-MVAQHLKVNRNmlsglfatpayrraerAALERAAYWLERVGLKQVANREAGT 154
Cdd:NF000106 81 RALRRTIG*HRPVR*grreSFSGRENLyMIGR*LDLSRK----------------DARARADELLERFSLTEAAGRAAAK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 155 LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:NF000106 145 YSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
....*....
gi 1787163341 235 MIGKPDEVR 243
Cdd:NF000106 224 ADGKVDELK 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-230 |
4.56e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 16 FGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIvleghaitgQPSHQVaRRGLVRTFQNIRLFKQ 95
Cdd:PRK09544 14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---------KRNGKL-RIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENLMVAQHLKVNRNMlsglfatPAyrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRL 175
Cdd:PRK09544 84 LTVNRFLRLRPGTKKEDIL-------PA---------------LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 176 LMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEH 230
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-232 |
6.35e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIvleghaitgqpshqvaRRGlvr 85
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------KLG--- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 tfQNIRL--FKQ--------LTVLENL------MVAQHLkvnRNMLSG-LFATpayrraeraaleraaywlERVgLKQVa 148
Cdd:COG0488 376 --ETVKIgyFDQhqeeldpdKTVLDELrdgapgGTEQEV---RGYLGRfLFSG------------------DDA-FKPV- 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 149 nreaGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNpqekVE-LQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILV 227
Cdd:COG0488 431 ----GVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----IEtLEALEEAL-DDFPGTVLLVSHDRYFLDRVATRILE 501
|
....*
gi 1787163341 228 MEHGK 232
Cdd:COG0488 502 FEDGG 506
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-234 |
6.36e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAIT--GQPSHQVARR 81
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 GLVRtfQNIRLFKQLTVLENLMVAQHLKvnrNMLSGLFATPAYRRAERAaleraaywLERVGLKQVANREAGTLSYGHQR 161
Cdd:PRK10762 82 GIIH--QELNLIPQLTIAENIFLGREFV---NRFGRIDWKKMYAEADKL--------LARLNLRFSSDKLVGELSIGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-246 |
6.47e-18 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 79.72 E-value: 6.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKP----TAGDIVLEGhaitgQPSHQVARRG--LVRTFQNIR-LF 93
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDG-----RPLLPLSIRGrhIATIMQNPRtAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KQLtvlenLMVAQHLKVNRNMLSGLFATPayrraeraaLERAAYWLERVGL---KQVANREAGTLSYGHQRRLEIARCMI 170
Cdd:TIGR02770 76 NPL-----FTMGNHAIETLRSLGKLSKQA---------RALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 171 TDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:TIGR02770 142 LEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNP 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-245 |
1.12e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.21 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-----GLVRTFQNIRLFKQ 95
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvrkriGMVFQFPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 ltvlenlmvaqhlKVNRNMLsglFATPAYRRAERAALERAAYWLERVGL-KQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:PRK13646 102 -------------TVEREII---FGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRND 245
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-251 |
1.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.13 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR--GLVrtFQNIRlfKQL- 96
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNkaGMV--FQNPD--NQIv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 -TVLE--------NLMVAQHLKVNRnmlsglfatpayrraeraalerAAYWLERVGLKQVANREAGTLSYGHQRRLEIAR 167
Cdd:PRK13633 100 aTIVEedvafgpeNLGIPPEEIRER----------------------VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 168 CMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
....
gi 1787163341 248 VIKA 251
Cdd:PRK13633 237 MMKK 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-245 |
1.80e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.41 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVrtFQN--------I 90
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHiGIV--FQNpdnqfvgsI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 91 RLFKQLTVLENLMVA---QHLKVNRNmlsglfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIAR 167
Cdd:PRK13648 101 VKYDVAFGLENHAVPydeMHRRVSEA-------------------------LKQVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 168 CMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDEVRND 245
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-232 |
2.00e-17 |
|
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: 81.02 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPT-AGDIVLEGHAITGQPSHQVARRGLVRTFQNirlFKQLTVLE 100
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPED---RKRHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHLKvnrnmLSGL--FATPAYRRAERAALERaaywleRVGLKQVANREA------GTLSYGHQRRLEIARCMITD 172
Cdd:TIGR02633 353 ILGVGKNIT-----LSVLksFCFKMRIDAAAELQII------GSAIQRLKVKTAspflpiGRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-232 |
2.56e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRTFQNiRLFKQLtVLEn 101
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISED-RKRDGL-VLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 lmvaqhLKVNRNM-LSGL--FATPAYRRAERAALERAAYWLERVGLKqVANREA--GTLSYGHQRRLEIARCMITDPRLL 176
Cdd:PRK10762 345 ------MSVKENMsLTALryFSRAGGSLKHADEQQAVSDFIRLFNIK-TPSMEQaiGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 177 MLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-246 |
2.78e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.66 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 4 QALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVG--GFYKP---TAGDIVLEGHAITGQPSHQV 78
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 ARR---GLVrtFQNIRLFKqLTVLENlmVAQHLKVNrnmlsGLFATPAYRRAERAALERAAYWLErvgLKQVANREAGTL 155
Cdd:PRK14239 83 DLRkeiGMV--FQQPNPFP-MSIYEN--VVYGLRLK-----GIKDKQVLDEAVEKSLKGASIWDE---VKDRLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 156 SYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFgiSVLLIEHDMSLVMGVSDRILVMEHGKPIM 235
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
250
....*....|.
gi 1787163341 236 IGKPDEVRNDP 246
Cdd:PRK14239 228 YNDTKQMFMNP 238
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
11-239 |
2.93e-17 |
|
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: 77.92 E-value: 2.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 11 GLQMRF--GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR------- 81
Cdd:cd03244 7 NVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRisiipqd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 -----GLVRtfQNIRLFKQLTVLEnLMVAqhlkvnrnmlsglfatpayrraeraaleraaywLERVGLKQVANREAGTL- 155
Cdd:cd03244 87 pvlfsGTIR--SNLDPFGEYSDEE-LWQA---------------------------------LERVGLKEFVESLPGGLd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 156 ----------SYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMvdgLRNEF-GISVLLIEHDMSLVMGvSDR 224
Cdd:cd03244 131 tvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDR 206
|
250
....*....|....*
gi 1787163341 225 ILVMEHGKPIMIGKP 239
Cdd:cd03244 207 ILVLDKGRVVEFDSP 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-237 |
3.68e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.13 E-value: 3.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQallkVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHA--ITGQPSHQV 78
Cdd:PRK11124 1 MSIQ----LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 ARR-----GLVrtFQNIRLFKQLTVLENLMVAQhLKVnrnmlSGLFATPAYRRAERAaleraaywLERVGLKQVANREAG 153
Cdd:PRK11124 77 IRElrrnvGMV--FQQYNLWPHLTVQQNLIEAP-CRV-----LGLSKDQALARAEKL--------LERLRLKPYADRFPL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 154 TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPqekvEL-QQMVDGLR--NEFGISVLLIEHDMSLVMGVSDRILVMEH 230
Cdd:PRK11124 141 HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP----EItAQIVSIIRelAETGITQVIVTHEVEVARKTASRVVYMEN 216
|
....*..
gi 1787163341 231 GKPIMIG 237
Cdd:PRK11124 217 GHIVEQG 223
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-242 |
3.95e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 33 EVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARrglvrtfQNIRLFKQLTVLENLMVAQHLKVNR 112
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-------KVAYLPQQLPAAEGMTVRELVAIGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 113 NMLSGlfatpAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVE 192
Cdd:PRK10575 111 YPWHG-----ALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1787163341 193 LQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-232 |
4.26e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 9 VAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHaitgqpshqvARRGLVRtfQ 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGYLP--Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 89 NIRLFKQLTVLENlmVAQHLKVNRNMLSGLFAtpAYRRAERAALERAAY------------W---------LERVGLKQV 147
Cdd:COG0488 69 EPPLDDDLTVLDT--VLDGDAELRALEAELEE--LEAKLAEPDEDLERLaelqeefealggWeaearaeeiLSGLGFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 148 -ANREAGTLSYGHQRRLEIARCMITDPRLLMLDEP-----AAGlnpqekVE-LQQMvdgLRNeFGISVLLIEHDMSLVMG 220
Cdd:COG0488 145 dLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPtnhldLES------IEwLEEF---LKN-YPGTVLVVSHDRYFLDR 214
|
250
....*....|..
gi 1787163341 221 VSDRILVMEHGK 232
Cdd:COG0488 215 VATRILELDRGK 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-247 |
5.56e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.77 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNC-------VGGFYkpTAGDIVLEGHAI--TG 72
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPGAR--VEGEILLDGEDIydPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 73 QPSHQVARR-GLVrtFQNIRLFkQLTVLENlmVAQHLKVN----RNMLSglfatpayrraeraaleraaywlERV--GLK 145
Cdd:COG1117 85 VDVVELRRRvGMV--FQKPNPF-PKSIYDN--VAYGLRLHgiksKSELD-----------------------EIVeeSLR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 146 QVA---------NREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQ--EKVElqQMVDGLRNEFgiSVLLIEHD 214
Cdd:COG1117 137 KAAlwdevkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIstAKIE--ELILELKKDY--TIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|...
gi 1787163341 215 MSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:COG1117 213 MQQAARVSDYTAFFYLGELVEFGPTEQIFTNPK 245
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-231 |
5.57e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.55 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVAR---RGLVRTFQNIRLFKQLTVLEN 101
Cdd:PRK11629 28 VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFIYQFHHLLPDFTALEN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 lmVAQHLKVNRnmlsglfATPAYRRAERAALeraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEP 181
Cdd:PRK11629 108 --VAMPLLIGK-------KKPAEINSRALEM------LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1787163341 182 AAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSdRILVMEHG 231
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-237 |
6.79e-17 |
|
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: 76.93 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 24 GIDFDVRPDEVFAIIGPNGAGKTTVFNCVGG---FYKPTAGDIVleghaITGQPS--HQVARR-GLVRtfQNIRLFKQLT 97
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQIL-----FNGQPRkpDQFQKCvAYVR--QDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 VLENLMVAQHLKVNRNMLSGlfatpayrraeRAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLM 177
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDA-----------IRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 178 LDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-252 |
7.76e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 7.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 27 FDVRPDEVFAIIGPNGAGKTTVFNCVGGFYkPTAGDIVLEGHAITGQPSHQVARRglvRTFqnirLFKQLTVLENLMVAQ 106
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARH---RAY----LSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 107 HLKVNRnmlsglfatPAyRRAERAALERAAYWLERVGLKQVANREAGTLSYGH-QR-RLeIARCMITDP------RLLML 178
Cdd:PRK03695 89 YLTLHQ---------PD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEwQRvRL-AAVVLQVWPdinpagQLLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 179 DEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDPRVIKAY 252
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
31-242 |
8.26e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.72 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 31 PDEVF-AIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVRtfQNIRLFKQLTVLEnlMVAQhl 108
Cdd:PRK10253 31 PDGHFtAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRiGLLA--QNATTPGDITVQE--LVAR-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 109 kvnrnmlsGLFA-TPAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNP 187
Cdd:PRK10253 105 --------GRYPhQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 188 QEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-237 |
9.13e-17 |
|
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: 76.42 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVleghaITGQPShqvARRGLVRTFQNirlfkQLTVLE 100
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-----VRGRVS---SLLGLGGGFNP-----ELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVaqhlkvnRNMLSGLfaTPAYRRAEraaleraaywLERV----GLKQVANREAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:cd03220 104 NIYL-------NGRLLGL--SRKEIDEK----------IDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 177 MLDEP-AAG-LNPQEKVE--LQQMVDGLRnefgiSVLLIEHDMSLVMGVSDRILVMEHGKPIMIG 237
Cdd:cd03220 165 LIDEVlAVGdAAFQEKCQrrLRELLKQGK-----TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-232 |
1.02e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYK-PTAGDIVLEGHAITGQPSHQVARRGLV-----RTFQNIRLfkQ 95
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAmvpedRKRDGIVP--V 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENLMVAQhlkVNRNMLSGLFATPAYRRAERAAleraaywLERVGLKQVANREA-GTLSYGHQRRLEIARCMITDPR 174
Cdd:PRK13549 356 MGVGKNITLAA---LDRFTGGSRIDDAAELKTILES-------IQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
20-233 |
1.52e-16 |
|
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: 76.29 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDGIDFdvRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPshqvarrglvrtfQNIRLFKQLTVL 99
Cdd:cd03237 15 LEVEGGSI--SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-------------QYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENLMvaqhlKVNRNMLSglfatpayrraeraalerAAYW----LERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRL 175
Cdd:cd03237 80 DLLS-----SITKDFYT------------------HPYFkteiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 176 LMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEhGKP 233
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEP 193
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-237 |
2.03e-16 |
|
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: 74.66 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgqpSHQVARRglvrtfqnirlfKQLTVL 99
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS---DLEKALS------------SLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 enlmvaqhlkvnrNMLSGLFATPAYrraeraaleraaywlERVGLKqvanreagtLSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:cd03247 81 -------------NQRPYLFDTTLR---------------NNLGRR---------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 180 EPAAGLNPQ-EKVELQQMVDGLRNEfgiSVLLIEHDMSLVMGVsDRILVMEHGKPIMIG 237
Cdd:cd03247 124 EPTVGLDPItERQLLSLIFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-241 |
2.08e-16 |
|
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: 76.04 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLV--------RTFQ-NIRL 92
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQiGLVsqepvlfdGTIAeNIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 93 FKQLTVLENLMVAQHLKVNRNMLSGL---FATpayrraeraaleraaywleRVGlkqvanrEAGT-LSYGHQRRLEIARC 168
Cdd:cd03249 100 GKPDATDEEVEEAAKKANIHDFIMSLpdgYDT-------------------LVG-------ERGSqLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 169 MITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDE 241
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-254 |
2.68e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 18 GLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGhAITGQPSHQVARRGLVR-TFQNIRL-FKQ 95
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-IDTGDFSKLQGIRKLVGiVFQNPETqFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENLMVAQHlkvnrnmlsGLFATPAYRRAERAALeraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRL 175
Cdd:PRK13644 93 RTVEEDLAFGPE---------NLCLPPIEIRKRVDRA------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 176 LMLDEPAAGLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSlVMGVSDRILVMEHGKPIMIGKPDEVRNDPRVikAYLG 254
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSL--QTLG 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-247 |
7.48e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 76.67 E-value: 7.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 3 AQALLKVAGLQMRF---GGLL--------AVDGIDFDVRPDEVFAIIGPNGAGKTTVfncvgGF----YKPTAGDIVLEG 67
Cdd:PRK15134 272 ASPLLDVEQLQVAFpirKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTT-----GLallrLINSQGEIWFDG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 68 haitgQPSHQVARRGL--VR-----TFQ--NIRLFKQLTVLEnlMVAQHLKVNRNMLSGLFATPAYRRAeraaleraayw 138
Cdd:PRK15134 347 -----QPLHNLNRRQLlpVRhriqvVFQdpNSSLNPRLNVLQ--IIEEGLRVHQPTLSAAQREQQVIAV----------- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 LERVGLKQVA-NREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSL 217
Cdd:PRK15134 409 MEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHV 488
|
250 260 270
....*....|....*....|....*....|
gi 1787163341 218 VMGVSDRILVMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK15134 489 VRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-250 |
8.90e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 8.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGD---IVLEGHAITGQPSHQVARR-GLVrtFQNI-RLFKQ 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREKvGIV--FQNPdNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTV-------LENLMVA--QHLKVNRNMLSglfatpayrraeraaleraaywleRVGLKQVANREAGTLSYGHQRRLEIA 166
Cdd:PRK13640 100 ATVgddvafgLENRAVPrpEMIKIVRDVLA------------------------DVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:PRK13640 156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKV 234
|
....
gi 1787163341 247 RVIK 250
Cdd:PRK13640 235 EMLK 238
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-223 |
8.96e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.69 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKpTAGDIVLEGHA-ITGQPSHQVA------ 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVeFFNQNIYERRvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 RRGLVRTFQNIRLFKqLTVLENL-----MVAQHLKVNrnmLSGLFATpayrraeraALERAAYWLErvgLKQVANREAGT 154
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVaygvkIVGWRPKLE---IDDIVES---------ALKDADLWDE---IKHKIHKSALD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 155 LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSD 223
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-247 |
9.63e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 9.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVARRGLVRTFQNIRLFKQlTVLE 100
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA-DYSEAALRQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHlKVNRNMLSGLfatpayrraeraaleraaywLERVGLKQVANREAG----------TLSYGHQRRLEIARCMI 170
Cdd:PRK11160 433 NLLLAAP-NASDEALIEV--------------------LQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 171 TDPRLLMLDEPAAGLNPQEKvelQQMVDGLRNEF-GISVLLIEHDMSLvMGVSDRILVMEHGKPIMIGKPDE-VRNDPR 247
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETE---RQILELLAEHAqNKTVLMITHRLTG-LEQFDRICVMDNGQIIEQGTHQElLAQQGR 566
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-242 |
1.04e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVaRRGLVRTFQNI-RLFKQLTV-- 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL-RRKIGMVFQNPdNQFVGATVed 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 99 -----LENLMVAQHLKVNRnMLSGLFAtpayrraeraaleraaywlerVGLKQVANREAGTLSYGHQRRLEIARCMITDP 173
Cdd:PRK13642 102 dvafgMENQGIPREEMIKR-VDEALLA---------------------VNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 174 RLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-241 |
1.09e-15 |
|
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: 73.80 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARR-GLVRtfQNIRLFKQlTVLEN 101
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAiGVVP--QDTVLFND-TIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 L----------------MVAQHLKVNRNMLSGlFATpayrraeraaleraaywleRVGlkqvanrEAGT-LSYGHQRRLE 164
Cdd:cd03253 95 IrygrpdatdeevieaaKAAQIHDKIMRFPDG-YDT-------------------IVG-------ERGLkLSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDE 241
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-246 |
1.18e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVaR 80
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 RGLVRTFQNIRLFKQlTVLENLMVAQHLKVNRNMLSGLFATpayrraeraaleraaywLERVGLKQ-VANREAGTLSYGH 159
Cdd:PRK10247 81 QQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDD-----------------LERFALPDtILTKNIAELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 160 QRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGkpimiGKP 239
Cdd:PRK10247 143 KQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA-----GEM 217
|
....*..
gi 1787163341 240 DEVRNDP 246
Cdd:PRK10247 218 QEARYEL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-242 |
1.74e-15 |
|
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: 75.61 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGF--YKPTAGDIV-----------LEGHAITGQ 73
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 74 P------------------SHQVARR-------GLVRTFQnirLFKQLTVLENLMVAQHLkvnrnmlSGLFATPAYRRAE 128
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlSDKLRRRirkriaiMLQRTFA---LYGDDTVLDNVLEALEE-------IGYEGKEAVGRAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 129 RAaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISV 208
Cdd:TIGR03269 151 DL--------IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISM 222
|
250 260 270
....*....|....*....|....*....|....
gi 1787163341 209 LLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:TIGR03269 223 VLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-247 |
2.53e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 12 LQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYK--PTA---GDIVLEGHAITGQPSHQV-ARRGLVR 85
Cdd:PRK14267 10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDPIeVRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 TFQNIRLFKQLTVLENlmVAQHLKVNRNMLSglfatpayrraERAALERAAYWLERVGL-KQVANR---EAGTLSYGHQR 161
Cdd:PRK14267 90 VFQYPNPFPHLTIYDN--VAIGVKLNGLVKS-----------KKELDERVEWALKKAALwDEVKDRlndYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFgiSVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDE 241
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
....*.
gi 1787163341 242 VRNDPR 247
Cdd:PRK14267 235 VFENPE 240
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
11-187 |
3.12e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.78 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 11 GLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgqPSHQVARRGLVRTFQNI 90
Cdd:NF033858 271 GLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD--AGDIATRRRVGYMSQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 91 RLFKQLTVLENLMVaqHLKvnrnmlsgLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMI 170
Cdd:NF033858 349 SLYGELTVRQNLEL--HAR--------LFHLPAAEIAARVAEM-----LERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170
....*....|....*..
gi 1787163341 171 TDPRLLMLDEPAAGLNP 187
Cdd:NF033858 414 HKPELLILDEPTSGVDP 430
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-238 |
3.19e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGfykptagdiVLEGHAITG-------QPSHQVARR-GLVRtfQNIRLF 93
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAG---------RIQGNNFTGtilannrKPTKQILKRtGFVT--QDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KQLTVLENLMVAQHLKVNRNMlsglfatpayrrAERAALERAAYWLERVGLKQVANREAGT-----LSYGHQRRLEIARC 168
Cdd:PLN03211 153 PHLTVRETLVFCSLLRLPKSL------------TKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHE 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 169 MITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGK 238
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-255 |
3.20e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.29 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAIT-GQPSHQVarrglvrtfQNIRLFKQ--LT 97
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRS---------QRIRMIFQdpST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 VLE-NLMVAQHLKVNRNMLSGLFATPAYRRAERAaleraaywLERVGLK-QVANREAGTLSYGHQRRLEIARCMITDPRL 175
Cdd:PRK15112 99 SLNpRQRISQILDFPLRLNTDLEPEQREKQIIET--------LRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 176 LMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP------RVI 249
Cdd:PRK15112 171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlheltkRLI 250
|
....*.
gi 1787163341 250 KAYLGE 255
Cdd:PRK15112 251 AGHFGE 256
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
16-254 |
3.61e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.91 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 16 FGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPShqvARRGLVRTFQNIRLFKQ 95
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERGVGMVFQSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENLMVAQHL-KVNRNMLSglfatpayrraeraaleraaywlERVglKQVA---------NREAGTLSYGHQRRLEI 165
Cdd:PRK11000 90 LSVAENMSFGLKLaGAKKEEIN-----------------------QRV--NQVAevlqlahllDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 166 ARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRND 245
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHY 224
|
250
....*....|.
gi 1787163341 246 P--RVIKAYLG 254
Cdd:PRK11000 225 PanRFVAGFIG 235
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-246 |
3.99e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.61 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRF----GGLLAVDGIDFDVRPDEVFAIIGPNGAGKT-TVFNCVGGFYKP--TAGDIVLEGHAITGQP 74
Cdd:PRK09473 8 QADALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 75 SHQVARrglVRT------FQN--------IRLFKQLTvlENLMVaqHLKVNRNmlsglfatpayrraeraaleraAYWLE 140
Cdd:PRK09473 88 EKELNK---LRAeqismiFQDpmtslnpyMRVGEQLM--EVLML--HKGMSKA----------------------EAFEE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 141 RVG-LKQVANREA--------GTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLI 211
Cdd:PRK09473 139 SVRmLDAVKMPEArkrmkmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMI 218
|
250 260 270
....*....|....*....|....*....|....*
gi 1787163341 212 EHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:PRK09473 219 THDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-213 |
4.54e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 74.28 E-value: 4.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFY-KPTAGDIVLEGHaitgqpshqvaRRGLVRTFQNIRlfKQLTVLEN 101
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTLFGR-----------RRGSGETIWDIK--KHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 LMvaqHL--KVN---RN-MLSGLF-ATPAYRRAERAALERAAYWLERVGL-KQVANREAGTLSYGHQRRLEIARCMITDP 173
Cdd:PRK10938 344 SL---HLdyRVStsvRNvILSGFFdSIGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHP 420
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1787163341 174 RLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEH 213
Cdd:PRK10938 421 TLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-232 |
4.68e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRF--GGLLA-------VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSH 76
Cdd:PRK10419 3 LLNVSGLSHHYahGGLSGkhqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 77 QVA--RRGLVRTFQ------NIR------LFKQLTVLENLMVAQHLKVNRNMLsglfatpayrraeraaleraaywlERV 142
Cdd:PRK10419 83 QRKafRRDIQMVFQdsisavNPRktvreiIREPLRHLLSLDKAERLARASEML------------------------RAV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 143 GLK-QVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGV 221
Cdd:PRK10419 139 DLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERF 218
|
250
....*....|.
gi 1787163341 222 SDRILVMEHGK 232
Cdd:PRK10419 219 CQRVMVMDNGQ 229
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-237 |
1.05e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGF--YKPTAGDIVLEGHAITGQPSHQV 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 ARRGLVRTFQNIRLFKQLTVLENLMVAQHLKVNRNMLSGLFATPAYRRAERAaleraaywLERVGLKQV-ANREAGT-LS 156
Cdd:CHL00131 82 AHLGIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEK--------LKLVGMDPSfLSRNVNEgFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 157 YGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVS-DRILVMEHGKPIM 235
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
..
gi 1787163341 236 IG 237
Cdd:CHL00131 233 TG 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-217 |
1.10e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPS----------HQVARRGLvrtfqnirl 92
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyhqdllylgHQPGIKTE--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 93 fkqLTVLENLMVAQHLkvnrNMLSGLFATPAYrraeraaleraaywLERVGLkqvANRE---AGTLSYGHQRRLEIARCM 169
Cdd:PRK13538 89 ---LTALENLRFYQRL----HGPGDDEALWEA--------------LAQVGL---AGFEdvpVRQLSAGQQRRVALARLW 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1787163341 170 ITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSL 217
Cdd:PRK13538 145 LTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPV 192
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-232 |
2.17e-14 |
|
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: 68.24 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGdIVLEGHAITgqpshqvarrglvrt 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVK--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 87 fqnIRLFKQltvlenlmvaqhlkvnrnmLSGlfatpayrraeraaleraaywlervglkqvanreagtlsyGHQRRLEIA 166
Cdd:cd03221 65 ---IGYFEQ-------------------LSG----------------------------------------GEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 167 RCMITDPRLLMLDEPAAGLNPQEKVELQQMVdglrNEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-232 |
2.38e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGG----LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSH 76
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 77 QVARR-----GLVrtFQNIRLFKQLTVLENLMVAQHLKVNRNMLSGLFATPAyrraeraaleraaywLERVGLKQVANRE 151
Cdd:PRK10584 81 ARAKLrakhvGFV--FQSFMLIPTLNALENVELPALLRGESSRQSRNGAKAL---------------LEQLGLGKRLDHL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 152 AGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVmGVSDRILVMEHG 231
Cdd:PRK10584 144 PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNG 222
|
.
gi 1787163341 232 K 232
Cdd:PRK10584 223 Q 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-242 |
2.61e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.63 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGG-FYKPTA-------GDIVLEGHAITGQPSHQVARRGLVRTFQNIRLF 93
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KqLTVLENLMVAQHLKVNR----NMLSGLFATPAyrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCM 169
Cdd:PRK13547 97 A-FSAREIVLLGRYPHARRagalTHRDGEIAWQA---------------LALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 170 ---------ITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPD 240
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
..
gi 1787163341 241 EV 242
Cdd:PRK13547 241 DV 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-232 |
2.75e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.68 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRTFQNIR---LFKQLTVLEN 101
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEERRstgIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 LMVAqhlkvnrNMLSglFATPAYRRAERAALERAAYWLERVGLKQVANREA-GTLSYGHQRRLEIARCMITDPRLLMLDE 180
Cdd:PRK10982 347 SLIS-------NIRN--YKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 181 PAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK10982 418 PTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
139-232 |
3.23e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 LERVGLKQVANREAG---TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDM 215
Cdd:PRK15134 138 LDRVGIRQAAKRLTDyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL 217
|
90
....*....|....*..
gi 1787163341 216 SLVMGVSDRILVMEHGK 232
Cdd:PRK15134 218 SIVRKLADRVAVMQNGR 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-247 |
3.59e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.08 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAIT-GQPSHQV-- 78
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfGKDIFQIda 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 79 --ARRGLVRTFQNIRLFKQLTVLENL---MVAQHLKVNRNMLSGLFATpayrraeraaleraaywLERVGL-KQVANR-- 150
Cdd:PRK14246 86 ikLRKEVGMVFQQPNPFPHLSIYDNIaypLKSHGIKEKREIKKIVEEC-----------------LRKVGLwKEVYDRln 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 151 -EAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfgISVLLIEHDMSLVMGVSDRILVME 229
Cdd:PRK14246 149 sPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLY 226
|
250
....*....|....*...
gi 1787163341 230 HGKPIMIGKPDEVRNDPR 247
Cdd:PRK14246 227 NGELVEWGSSNEIFTSPK 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-239 |
6.44e-14 |
|
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: 68.59 E-value: 6.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 7 LKVAGLQMRFGGLL--AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVaRRGLV 84
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL-RSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 85 RTFQNIRLFKQlTVLENLMVAQHLKvNRNMLSGLfatpayrraeraaleraaywleRVglkqvanREAG-TLSYGHQRRL 163
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLDPFDEYS-DEEIYGAL----------------------RV-------SEGGlNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 164 EIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVdglRNEF-GISVLLIEHDMSLVMGVsDRILVMEHGKPIMIGKP 239
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTI---REEFtNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-232 |
9.24e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 9.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLVRTFQNIR---LFKQLTV 98
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 99 LENLMVAQHLKVNR-NMLSGLFATPAYRRAERAALeraaywlERVGLK-QVANREAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:PRK09700 359 AQNMAISRSLKDGGyKGAMGLFHEVDEQRTAENQR-------ELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1787163341 177 MLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-247 |
1.18e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.97 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNC-------VGGFYkpTAGDIVLEGHAITGQP 74
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYR--YSGDVLLGGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 75 SHQVARRGLVRTFQNIRLFKqLTVLENLM--VAQHLKVNRNMLSGLFATPayrraeraaleraaywLERVGL-KQVANRE 151
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFP-MSIMDNVLagVRAHKLVPRKEFRGVAQAR----------------LTEVGLwDAVKDRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 152 AGT---LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfgISVLLIEHDMSLVMGVSDRILVM 228
Cdd:PRK14271 158 SDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALF 235
|
250
....*....|....*....
gi 1787163341 229 EHGKPIMIGKPDEVRNDPR 247
Cdd:PRK14271 236 FDGRLVEEGPTEQLFSSPK 254
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-255 |
2.63e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 69.10 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYkPTAGDIVLEGHAITgQPSHQVARRGLVRTFQNIRLFKQlTVLENLmv 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELR-ELDPESWRKHLSWVGQNPQLPHG-TLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 105 aqhlkvnrnmlsgLFATPAYRRAERAALERAAYWLERV-----GLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:PRK11174 444 -------------LLGNPDASDEQLQQALENAWVSEFLpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 180 EPAAGLNPQEKvelQQMVDGLRNE-FGISVLLIEHDMSLVMGVsDRILVMEHGKPIMIGKPDEVRNDPRVIKAYLGE 255
Cdd:PRK11174 511 EPTASLDAHSE---QLVMQALNAAsRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-232 |
2.96e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 20 LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAIT----GQPSHQVArrgLVRtfQNIRLFKQ 95
Cdd:PRK11176 357 PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytlASLRNQVA---LVS--QNVHLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 lTVLENLMVAQHLKVNRNMLSGLfATPAYRRAeraaleraayWLERV--GLKQVANREAGTLSYGHQRRLEIARCMITDP 173
Cdd:PRK11176 432 -TIANNIAYARTEQYSREQIEEA-ARMAYAMD----------FINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 174 RLLMLDEPAAGLNPQEKVELQQMVDGLRNEFgiSVLLIEHDMSLVMGvSDRILVMEHGK 232
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGE 555
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-223 |
3.84e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.11 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 2 SAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNC-------VGGFYkpTAGDIVLEGHAITGQ- 73
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndlIPGFR--VEGKVTFHGKNLYAPd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 74 --PSHQVARRGLVrtFQNIRLFKQlTVLENlmVAQHLKVN--RNMLSGLFATpayrraeraALERAAYWLErvgLKQVAN 149
Cdd:PRK14243 84 vdPVEVRRRIGMV--FQKPNPFPK-SIYDN--IAYGARINgyKGDMDELVER---------SLRQAALWDE---VKDKLK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 150 REAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGIsvLLIEHDMSLVMGVSD 223
Cdd:PRK14243 147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSD 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-233 |
6.44e-13 |
|
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: 67.89 E-value: 6.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 28 DVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDiVLEGHAITGQPshqvarrglvrtfQNIRLFKQLTVLENLMvaqh 107
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE-VDEDLKISYKP-------------QYISPDYDGTVEEFLR---- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 108 lKVNRNMLSGlfatpayrraeraaleraAYW----LERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAA 183
Cdd:COG1245 424 -SANTDDFGS------------------SYYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1787163341 184 GLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEhGKP 233
Cdd:COG1245 485 HLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEP 533
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
17-246 |
9.10e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.79 E-value: 9.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITG-QPshqvARRGLVRTFQNIRLFKQ 95
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEP----ADRDIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 96 LTVLENLmvAQHLKvNRNMLSGLFAtpayrraeraaleraaywlERV-------GLKQVANREAGTLSYGHQRRLEIARC 168
Cdd:PRK11650 91 MSVRENM--AYGLK-IRGMPKAEIE-------------------ERVaeaarilELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 169 MITDPRLLMLDEPA----AGLNPQEKVELQQmvdgLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN 244
Cdd:PRK11650 149 IVREPAVFLFDEPLsnldAKLRVQMRLEIQR----LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYE 224
|
..
gi 1787163341 245 DP 246
Cdd:PRK11650 225 KP 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-238 |
1.31e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.05 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 17 GGLLAVDGIDFDVRPDEV--------------FAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQpSHQVARRG 82
Cdd:PRK10790 338 SGRIDIDNVSFAYRDDNLvlqninlsvpsrgfVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 83 ----------LVRTF-QNIRLFKQLT---VLENLMVAQHLKVNRNMLSGLFAtpayrraeraaleraaywleRVGlkqva 148
Cdd:PRK10790 417 vamvqqdpvvLADTFlANVTLGRDISeeqVWQALETVQLAELARSLPDGLYT--------------------PLG----- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 149 nrEAG-TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfgISVLLIEHDMSLVMGvSDRILV 227
Cdd:PRK10790 472 --EQGnNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILV 546
|
250
....*....|.
gi 1787163341 228 MEHGKPIMIGK 238
Cdd:PRK10790 547 LHRGQAVEQGT 557
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
23-234 |
4.13e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVA--RR---GLVrtFQNIRLFKQLT 97
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlRRehfGFI--FQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 98 VLENLMV-AQHLKVNRNmlsglfatpayrraerAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:PRK10535 103 AAQNVEVpAVYAGLERK----------------QRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 177 MLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDmSLVMGVSDRILVMEHGKPI 234
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-223 |
5.68e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRF-GGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIvleghAITGQPSHQVA 79
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 RRGLVRTF-QNIRLFKQLTVLenlmVAQHLKVNRNMLSGLFATPAYRRAERAALEraaywLERVGLKQVANREAGTLSYG 158
Cdd:PRK15056 76 QKNLVAYVpQSEEVDWSFPVL----VEDVVMMGRYGHMGWLRRAKKRDRQIVTAA-----LARVDMVEFRHRQIGELSGG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1787163341 159 HQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSD 223
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-238 |
7.69e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 29 VRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEgHAITGQPshqvarrglvrtfQNIRLFKQLTVLENLMvaqhl 108
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP-------------QYIKPDYDGTVEDLLR----- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 109 KVNRNMLSGLFATPAyrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQ 188
Cdd:PRK13409 423 SITDDLGSSYYKSEI---------------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1787163341 189 EKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEhGKPIMIGK 238
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE-GEPGKHGH 536
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-197 |
1.05e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 1 MSAQALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGH-AITGQPSHQVA 79
Cdd:PRK13543 6 HTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 80 RRGLVRTfqnirLFKQLTVLENL--MVAQHLKVNRNMLSGLFATpayrraeraaleraaywlerVGLKQVANREAGTLSY 157
Cdd:PRK13543 86 YLGHLPG-----LKADLSTLENLhfLCGLHGRRAKQMPGSALAI--------------------VGLAGYEDTLVRQLSA 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1787163341 158 GHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMV 197
Cdd:PRK13543 141 GQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-232 |
7.33e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 7.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPSHQVARRGLV-----RTFQNIrlFKQLTVL 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKAEGI--IPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENLMVAQHLKVNRnmlSGLFATPAyrraeraaleraayWLERVGLKQVA-------NREA--GTLSYGHQRRLEIARCMI 170
Cdd:PRK11288 350 DNINISARRHHLR---AGCLINNR--------------WEAENADRFIRslniktpSREQliMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 171 TDPRLLMLDEPAAGLNPQEKVELQQMVDGLRnEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-232 |
7.87e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.53 E-value: 7.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGqpSHQVARRGLVRT-FQNIRLFKQLTVL 99
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA--EQPEDYRKLFSAvFTDFHLFDQLLGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 EnlmvaqhlkvnrnmlsGLFATPAyrraeraaleRAAYWLERVGLKQVANREAGT-----LSYGHQRRLEIARCMITDPR 174
Cdd:PRK10522 416 E----------------GKPANPA----------LVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 175 LLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILVMEHGK 232
Cdd:PRK10522 470 ILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQ 526
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-244 |
4.21e-10 |
|
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: 58.53 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 29 VRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIvleghaiTGQPSHQvarrGLVRTFQNIRLFKQLTVLEN-----LM 103
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-------DDPPDWD----EILDEFRGSELQNYFTKLLEgdvkvIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 104 VAQHLKVNRNMLSGlfaTPAYRRAERAALERAAYWLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAA 183
Cdd:cd03236 92 KPQYVDLIPKAVKG---KVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 184 GLNPQEKVELQQMVDGLrNEFGISVLLIEHDMSLVMGVSDRILVMeHGKPIMIG---KPDEVRN 244
Cdd:cd03236 169 YLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCL-YGEPGAYGvvtLPKSVRE 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
149-231 |
5.43e-10 |
|
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: 56.95 E-value: 5.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 149 NREAGTLSYGHQRRLEIARCMI--TDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSlVMGVSDRIL 226
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLD-VLSSADWII 159
|
....*
gi 1787163341 227 VMEHG 231
Cdd:cd03238 160 DFGPG 164
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-247 |
6.23e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGG----LLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFY----KPTAGDIVLEGHAITGQPSH 76
Cdd:PRK11022 2 ALLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 77 QvaRRGLVRT-----FQN--IRLFKQLTVLENLMVAqhLKVNRnmlSGLFATpayrraeraALERAAYWLERVGLKQVAN 149
Cdd:PRK11022 82 E--RRNLVGAevamiFQDpmTSLNPCYTVGFQIMEA--IKVHQ---GGNKKT---------RRQRAIDLLNQVGIPDPAS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 150 R---EAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRIL 226
Cdd:PRK11022 146 RldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
250 260
....*....|....*....|.
gi 1787163341 227 VMEHGKPIMIGKPDEVRNDPR 247
Cdd:PRK11022 226 VMYAGQVVETGKAHDIFRAPR 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
155-246 |
1.36e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 155 LSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
90
....*....|..
gi 1787163341 235 MIGKPDEVRNDP 246
Cdd:PRK10261 249 ETGSVEQIFHAP 260
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-253 |
1.77e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 30 RPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDI--------VLEGHAITG-QPSHQVARRGLVRTFQNI-------RLF 93
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKRFRGTElQDYFKKLANGEIKVAHKPqyvdlipKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 94 KqLTVLENLMvaqhlKVN-RNMLSGLfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITD 172
Cdd:COG1245 177 K-GTVRELLE-----KVDeRGKLDEL--------------------AEKLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 173 PRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMeHGKPI---MIGKPDEVRNDprvI 249
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHIL-YGEPGvygVVSKPKSVRVG---I 305
|
....
gi 1787163341 250 KAYL 253
Cdd:COG1245 306 NQYL 309
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-247 |
1.82e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.63 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTtvFNCVG--GFYKP----TAGDIVLEGhaitgQPSHQVARRG-LVRT-FQNIR-L 92
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAalGILPAgvrqTAGRVLLDG-----KPVAPCALRGrKIATiMQNPRsA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 93 FKQLT-----VLENLMVAQHLKVNRNMLSGLfatpayrraeraaleraaywlERVGL---KQVANREAGTLSYGHQRRLE 164
Cdd:PRK10418 92 FNPLHtmhthARETCLALGKPADDATLTAAL---------------------EAVGLenaARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 165 IARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRN 244
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
...
gi 1787163341 245 DPR 247
Cdd:PRK10418 231 APK 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-241 |
2.72e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 24 GIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItgqpshqvARRGLVRTFQNIRLFKQLTVLENLM 103
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDI--------SKFGLMDLRKVLGIIPQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 104 VAQHLK-VNRNMLSGLFATpayrraeraaleraaywLERVGLKQVANR----------EAG-TLSYGHQRRLEIARCMIT 171
Cdd:PLN03130 1329 VRFNLDpFNEHNDADLWES-----------------LERAHLKDVIRRnslgldaevsEAGeNFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 172 DPRLLMLDEPAAGLNPQEKVELQQMVdglRNEF-GISVLLIEHDMSLVMGvSDRILVMEHGKPIMIGKPDE 241
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTI---REEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPEN 1458
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-242 |
7.61e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.14 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 24 GIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGhaitgqpsHQVARRGLVRTFQNIRLFKQLTVLenlm 103
Cdd:PLN03232 1254 GLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--------CDVAKFGLTDLRRVLSIIPQSPVL---- 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 104 vaqhlkvnrnmLSGlfaTPAYRRAERAALERAAYW--LERVGLKQVANR----------EAG-TLSYGHQRRLEIARCMI 170
Cdd:PLN03232 1322 -----------FSG---TVRFNIDPFSEHNDADLWeaLERAHIKDVIDRnpfgldaevsEGGeNFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 171 TDPRLLMLDEPAAGLNPQEKVELQQMVdglRNEF-GISVLLIEHDMSLVMGVsDRILVMEHGKPIMIGKPDEV 242
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTI---REEFkSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQEL 1456
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-232 |
7.94e-09 |
|
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: 55.60 E-value: 7.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITgQPSHQVARR--GLVRtfQNIRLFKQlTVLE 100
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR-DVTQASLRAaiGIVP--QDTVLFND-TIAY 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLM-------------VAQ--HLkvnRNMLSGL---FATPAYrraeraaleraaywlERvGLKqvanreagtLSYGHQRR 162
Cdd:COG5265 451 NIAygrpdaseeeveaAARaaQI---HDFIESLpdgYDTRVG---------------ER-GLK---------LSGGEKQR 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 163 LEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGvSDRILVMEHGK 232
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGR 569
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-65 |
8.52e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.71 E-value: 8.52e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVL 65
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-244 |
1.70e-08 |
|
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: 52.96 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 28 DVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQPshqvarrglvrtfqnirlfkqltvlenlmvaQH 107
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-------------------------------QY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 108 LKvnrnmlsglfatpayrraeraaleraaywlervglkqvanreagtLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNP 187
Cdd:cd03222 70 ID---------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDI 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 188 QEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEhGKPIMIG---KPDEVRN 244
Cdd:cd03222 105 EQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE-GEPGVYGiasQPKGTRE 163
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-237 |
1.71e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.04 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 15 RFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNC----VGGFYKPTaGDIVLEGHaiTGQPSHQVARRGLVRTFQNI 90
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanrTEGNVSVE-GDIHYNGI--PYKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 91 RLFKQLTVLENLMVAQHLKVNRnMLSGlfatpayrraeraaleraaywlervglkqvanreagtLSYGHQRRLEIARCMI 170
Cdd:cd03233 93 VHFPTLTVRETLDFALRCKGNE-FVRG-------------------------------------ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 171 TDPRLLMLDEPAAGLNPQEKVE----LQQMVDGLRnefgisvlliehdMSLVMGVS----------DRILVMEHGKPIMI 236
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEilkcIRTMADVLK-------------TTTFVSLYqasdeiydlfDKVLVLYEGRQIYY 201
|
.
gi 1787163341 237 G 237
Cdd:cd03233 202 G 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-239 |
2.10e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYK--PTAGDIVLEGHAITgqpshqvarrglvrtfqnirlfkqltvlE 100
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG----------------------------R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHLKVNRNMLSGLfatpayrraeraaleraaYWLERVGLKQVAN--REAGTLSYGHQRRLEIARCMITDPRLLML 178
Cdd:COG2401 99 EASLIDAIGRKGDFKDAV------------------ELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 179 DEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKP 239
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVGYGGVPEEKR 221
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
149-226 |
2.80e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 149 NREAGTLSYGHQRRLEIARCM------ITdprlLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVmGVS 222
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLgaeligIT----YILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMI-SLA 544
|
....
gi 1787163341 223 DRIL 226
Cdd:PRK00635 545 DRII 548
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
232-256 |
4.96e-08 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 47.63 E-value: 4.96e-08
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-231 |
6.61e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 6.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCV-----GGFYkpTAGDIVLEGHAItgQPSHQvaRR-GLVRTfQNIRLfKQL 96
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPL--DSSFQ--RSiGYVQQ-QDLHL-PTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 97 TVLENLMVAQHLKvnrnmlsglfaTPAyRRAERAALERAAYWLERVGLKQVANREAGT----LSYGHQRRLEIARCMITD 172
Cdd:TIGR00956 852 TVRESLRFSAYLR-----------QPK-SVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAK 919
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1787163341 173 PRLLM-LDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMS-LVMGVSDRILVMEHG 231
Cdd:TIGR00956 920 PKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQPSaILFEEFDRLLLLQKG 979
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
151-232 |
1.12e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.10 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 151 EAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGVSDRILVMEH 230
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNE 479
|
..
gi 1787163341 231 GK 232
Cdd:NF040905 480 GR 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-243 |
1.21e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 9 VAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDI-VLEGHaiTGQPSH--QVARR---- 81
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGD--MADARHrrAVCPRiaym 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 82 --GLVRtfqNirLFKQLTVLENLmvaqhlkvnrNMLSGLFATPAyrraeraaleraaywLER----------VGLKQVAN 149
Cdd:NF033858 82 pqGLGK---N--LYPTLSVFENL----------DFFGRLFGQDA---------------AERrrridellraTGLAPFAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 150 REAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEF-GISVLliehdmslvmgVS------ 222
Cdd:NF033858 132 RPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVL-----------VAtaymee 200
|
250 260
....*....|....*....|....*
gi 1787163341 223 ----DRILVMEHGKPIMIGKPDEVR 243
Cdd:NF033858 201 aerfDWLVAMDAGRVLATGTPAELL 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-253 |
1.45e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 29 VRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDI--------VLEGHAITG-QPSHQVARRGLVRTFQNI-------RL 92
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKRFRGTElQNYFKKLYNGEIKVVHKPqyvdlipKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 93 FKQlTVLENLMvaqhlKVN-RNMLSGLfatpayrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMIT 171
Cdd:PRK13409 176 FKG-KVRELLK-----KVDeRGKLDEV--------------------VERLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 172 DPRLLMLDEPAAGLNPQEKVELQQMVDGLRNefGISVLLIEHDMSLVMGVSDRILVMeHGKPIMIG---KPDEVRNDprv 248
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA-YGEPGAYGvvsKPKGVRVG--- 303
|
....*
gi 1787163341 249 IKAYL 253
Cdd:PRK13409 304 INEYL 308
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-217 |
1.50e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItgQPSHQVARRGLVR 85
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI--KKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 86 TFQNIRLFKQLTVLENLMVAQHLKvNRNM----LSGLFAtpayrraeraaleraaywlervgLKQVANREAGTLSYGHQR 161
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFS-PGAVgiteLCRLFS-----------------------LEHLIDYPCGLLSSGQKR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 162 RLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGiSVLLIEH-DMSL 217
Cdd:PRK13540 135 QVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGG-AVLLTSHqDLPL 190
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
139-246 |
1.70e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 LERVGLK---QVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDM 215
Cdd:PRK15093 140 LHRVGIKdhkDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDL 219
|
90 100 110
....*....|....*....|....*....|.
gi 1787163341 216 SLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:PRK15093 220 QMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-65 |
1.80e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.80e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVL 65
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-88 |
4.30e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 6 LLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGF--YKPTAGDIVLEGHAITGQPSHQVARRGL 83
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
....*
gi 1787163341 84 VRTFQ 88
Cdd:PRK09580 81 FMAFQ 85
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
138-246 |
7.18e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.52 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 138 WLERVGLKqvaNREAGTLSYGHQ------RRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLI 211
Cdd:COG4170 139 LLHRVGIK---DHKDIMNSYPHEltegecQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLI 215
|
90 100 110
....*....|....*....|....*....|....*
gi 1787163341 212 EHDMSLVMGVSDRILVMEHGKPIMIGKPDEVRNDP 246
Cdd:COG4170 216 SHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
140-232 |
7.57e-07 |
|
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: 49.08 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 140 ERVGLKQVANREAG-----------TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPqekVELQQMVDGLRNEF-GIS 207
Cdd:cd03289 113 EEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP---ITYQVIRKTLKQAFaDCT 189
|
90 100
....*....|....*....|....*
gi 1787163341 208 VLLIEHDMSLVMGVSdRILVMEHGK 232
Cdd:cd03289 190 VILSEHRIEAMLECQ-RFLVIEENK 213
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-231 |
1.40e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 47.62 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 23 DGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGfyKPTAGDIvlEGH-AITGQPSHQVARR--GLVRtfQNIRLFKQLTVL 99
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--TGEiLINGRPLDKNFQRstGYVE--QQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 100 ENLMVAQHLKvnrnmlsglfatpayrraeraaleraaywlervglkqvanreagTLSYGHQRRLEIARCMITDPRLLMLD 179
Cdd:cd03232 98 EALRFSALLR--------------------------------------------GLSVEQRKRLTIGVELAAKPSILFLD 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1787163341 180 EPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMS-LVMGVSDRILVMEHG 231
Cdd:cd03232 134 EPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSaSIFEKFDRLLLLKRG 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-232 |
1.84e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 5 ALLKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFncvggfyKPTAGDIVLEGHAITGQPSHQVAR---- 80
Cdd:PRK11147 2 SLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLM-------KILNGEVLLDDGRIIYEQDLIVARlqqd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 81 -----RGLVRTFqnirlfkqltVLENLM-VAQHLKV---------------NRNMLSGLFATPAYRRAeraaleraayW- 138
Cdd:PRK11147 75 pprnvEGTVYDF----------VAEGIEeQAEYLKRyhdishlvetdpsekNLNELAKLQEQLDHHNL----------Wq 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 --------LERVGLKqvANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNpqekVELQQMVDGLRNEFGISVLL 210
Cdd:PRK11147 135 lenrinevLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIF 208
|
250 260
....*....|....*....|..
gi 1787163341 211 IEHDMSLVMGVSDRILVMEHGK 232
Cdd:PRK11147 209 ISHDRSFIRNMATRIVDLDRGK 230
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
139-235 |
2.23e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 47.25 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 LERVGLKQVA-NREAGTLSYGHQRRLEIAR---CMITDPrLLMLDEPAAGLNPQEKVELQQMVDGLRNeFGISVLLIEHD 214
Cdd:cd03270 121 LVDVGLGYLTlSRSAPTLSGGEAQRIRLATqigSGLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHD 198
|
90 100
....*....|....*....|....*.
gi 1787163341 215 MSlVMGVSDRILVM-----EHGKPIM 235
Cdd:cd03270 199 ED-TIRAADHVIDIgpgagVHGGEIV 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-63 |
3.07e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 3.07e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 7 LKVAGLQMRFGGLLAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDI 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
139-254 |
3.63e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 47.70 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 LERVGLKQVA-NREAGTLSYGHQRRLEIARCM---ITDPrLLMLDEPAAGLNPQEKVELQQMVDGLRNeFGISVLLIEHD 214
Cdd:TIGR00630 472 LIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHD 549
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1787163341 215 mSLVMGVSDRILVM-----EHGKPIMI-GKPDEVRNDPRVIK-AYLG 254
Cdd:TIGR00630 550 -EDTIRAADYVIDIgpgagEHGGEVVAsGTPEEILANPDSLTgQYLS 595
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-232 |
4.78e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 24 GIDFDVRpdevFAIIGPNGAGKTTVFNCVGGFYKPTAGdivleghaitgqpshQVARRGLVRtfqnIRLFKQLTVlenlm 103
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSG---------------TVFRSAKVR----MAVFSQHHV----- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 104 vaQHLKVNRNMLsgLFATPAYRRAERAALERAaywLERVGLK-QVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPA 182
Cdd:PLN03073 583 --DGLDLSSNPL--LYMMRCFPGVPEQKLRAH---LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1787163341 183 AGLNpQEKVElqQMVDGLRnEFGISVLLIEHDMSLVMGVSDRILVMEHGK 232
Cdd:PLN03073 656 NHLD-LDAVE--ALIQGLV-LFQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
25-218 |
6.71e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 6.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 25 IDFDvrpDEVFAIIGPNGAGKTTVFNCVggFYkptagdiVLEGHAIT----GQPSHQVARRGLVRTfqNIRLFKQLTVLE 100
Cdd:cd03240 18 IEFF---SPLTLIVGQNGAGKTTIIEAL--KY-------ALTGELPPnskgGAHDPKLIREGEVRA--QVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHLKVNRNML---SGLFATPAYrraeraaleraaywlervglkqvanREAGTLSYGhQR-------RLEIARCMI 170
Cdd:cd03240 84 KYTITRSLAILENVIfchQGESNWPLL-------------------------DMRGRCSGG-EKvlasliiRLALAETFG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1787163341 171 TDPRLLMLDEPAAGLNPqEKVE--LQQMVDGLRNEFGISVLLIEHDMSLV 218
Cdd:cd03240 138 SNCGILALDEPTTNLDE-ENIEesLAEIIEERKSQKNFQLIVITHDEELV 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-218 |
1.01e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 1.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 152 AGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLR-NEFGISVlLIEHDMSLV 218
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI-IIAHRLSTI 643
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-73 |
1.10e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 45.94 E-value: 1.10e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1787163341 25 IDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGQ 73
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD 399
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-213 |
3.02e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 31 PDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAItgqpsHQVARRGLVRTFQNIRLFKQLTVLENLMVAQHLkv 110
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI-----NNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEI-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 111 nRNMLSGLFATPAYRRaeraaleraaywlervgLKQVANREAGTLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEK 190
Cdd:PRK13541 98 -YNSAETLYAAIHYFK-----------------LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
170 180
....*....|....*....|...
gi 1787163341 191 VELQQMVDGLRNEFGIsVLLIEH 213
Cdd:PRK13541 160 DLLNNLIVMKANSGGI-VLLSSH 181
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
140-213 |
3.57e-05 |
|
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: 44.90 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 140 ERVGLKQVANREAG-----------TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPqekVELQQMVDGLRNEFG-IS 207
Cdd:TIGR01271 1328 EEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP---VTLQIIRKTLKQSFSnCT 1404
|
....*.
gi 1787163341 208 VLLIEH 213
Cdd:TIGR01271 1405 VILSEH 1410
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
16-71 |
3.72e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 3.72e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1787163341 16 FGGLLAVDGIDFDvrpDEVFAIIGPNGAGKTTVFNCVG-GFYKPTAGDIVLEGHAIT 71
Cdd:COG0419 10 FRSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRyALYGKARSRSKLRSDLIN 63
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
139-231 |
4.41e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.41 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 139 LERVGLKQVANR---EAG---TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMvdgLRNEF-GISVLLI 211
Cdd:COG4178 464 LEAVGLGHLAERldeEADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL---LREELpGTTVISV 540
|
90 100
....*....|....*....|
gi 1787163341 212 EHDMSLvMGVSDRILVMEHG 231
Cdd:COG4178 541 GHRSTL-AAFHDRVLELTGD 559
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-217 |
5.49e-05 |
|
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: 42.53 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAitgqpshqvarrglvrtfqnirlfkqltvlEN 101
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE------------------------------DL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 102 LMVAQHLKVNRNMLSGLFATPayrraeraaleraayWLErvglkqvanreagTLSYGHQRRLEIARCMITDPRLLMLDEP 181
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIYP---------------WDD-------------VLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|....*.
gi 1787163341 182 AAGLNPQEKVELQQMVdglrNEFGISVLLIEHDMSL 217
Cdd:cd03223 119 TSALDEESEDRLYQLL----KELGITVISVGHRPSL 150
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-249 |
6.56e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 11 GLQMRF-GGL-LAVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAITGqpshqVARRGLVRTFQ 88
Cdd:PTZ00243 1313 GVQMRYrEGLpLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA-----YGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 89 NIrlfKQLTVLENLMVAQhlkvnrNMLSGLFATPAyrraeraaleraAYW--LERVGLKQ-VANREAG----------TL 155
Cdd:PTZ00243 1388 MI---PQDPVLFDGTVRQ------NVDPFLEASSA------------EVWaaLELVGLRErVASESEGidsrvleggsNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 156 SYGHQRRLEIARCMIT-DPRLLMLDEPAAGLNPQEKVELQQMVdglRNEF-GISVLLIEHDMSLVmGVSDRILVMEHGKP 233
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATV---MSAFsAYTVITIAHRLHTV-AQYDKIIVMDHGAV 1522
|
250
....*....|....*.
gi 1787163341 234 IMIGKPDEVRNDPRVI 249
Cdd:PTZ00243 1523 AEMGSPRELVMNRQSI 1538
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-242 |
8.88e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEGHAitgqpshqvarrGLVRTFQNirLFKQLTVLE 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA------------ALIAISSG--LNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVaqhlkvnRNMLSGLFA------TPAYrraeraaleraaywLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPR 174
Cdd:PRK13545 105 NIEL-------KGLMMGLTKekikeiIPEI--------------IEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1787163341 175 LLMLDEP-AAGLNPQEKVELQQMvdglrNEF---GISVLLIEHDMSLVMGVSDRILVMEHGKPIMIGKPDEV 242
Cdd:PRK13545 164 ILVIDEAlSVGDQTFTKKCLDKM-----NEFkeqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-242 |
1.69e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 142 VGLKQVA-NREAGTLSYGHQRRLEIARCM---ITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSl 217
Cdd:TIGR00630 816 VGLGYIRlGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK-GNTVVVIEHNLD- 893
|
90 100 110
....*....|....*....|....*....|.
gi 1787163341 218 VMGVSDRILVM------EHGKPIMIGKPDEV 242
Cdd:TIGR00630 894 VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
154-227 |
2.05e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 2.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1787163341 154 TLSYGHQRRLEIARCMITDPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEFGISVLLIEHDMSLVMGvSDRILV 227
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1430
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
25-52 |
2.26e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.94 E-value: 2.26e-04
10 20
....*....|....*....|....*...
gi 1787163341 25 IDFDvrpDEVFAIIGPNGAGKTTVFNCV 52
Cdd:pfam13476 14 IDFS---KGLTLITGPNGSGKTTILDAI 38
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-226 |
4.40e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 150 REAGTLSYGHQRRLEIARCMIT---DPRLLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMgVSDRIL 226
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVK-VADYVL 882
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
154-231 |
5.35e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 154 TLSYGHQRRLEIARCMITDPR---LLMLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLIEHDMSLVMGvSDRILVMEH 230
Cdd:PRK00635 1699 SLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSL-GHSVIYIDHDPALLKQ-ADYLIEMGP 1776
|
.
gi 1787163341 231 G 231
Cdd:PRK00635 1777 G 1777
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-234 |
6.75e-04 |
|
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: 40.69 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 37 IIGPNGAGKTTVFNCVGGFYKPTAGDIVLeghaitgQPSHQVarrGLVRtfQNIRLFKQLTVLENLMVA-QHLK--VNR- 112
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARP-------QPGIKV---GYLP--QEPQLDPTKTVRENVEEGvAEIKdaLDRf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 113 NMLSGLFATP-AYRRAERAALERAAYWLERVGLKQVANR---------------EAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:TIGR03719 104 NEISAKYAEPdADFDKLAAEQAELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKPDML 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1787163341 177 MLDEPAAGLNpQEKVE-LQQMVdglrNEFGISVLLIEHDMSLVMGVSDRILVMEHGKPI 234
Cdd:TIGR03719 184 LLDEPTNHLD-AESVAwLERHL----QEYPGTVVAVTHDRYFLDNVAGWILELDRGRGI 237
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-252 |
7.04e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.60 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 30 RPDEVFAIIGPNGAGKTTVFNCVGGfyKPTAGDIvlEGHA-ITGQPSHQvarrglvRTFQNIRLF--------KQLTVLE 100
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDIrISGFPKKQ-------ETFARISGYceqndihsPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 101 NLMVAQHLKVNRNMlsglfatpayrrAERAALERAAYWLERVGLKQVANREAGT-----LSYGHQRRLEIARCMITDPRL 175
Cdd:PLN03140 973 SLIYSAFLRLPKEV------------SKEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSI 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 176 LMLDEPAAGLNPQEKVELQQMVdglRN--EFGISVLLIEHDMSL-VMGVSDRILVMEHGKPIMIGKPDEvRNDPRVIKAY 252
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTV---RNtvDTGRTVVCTIHQPSIdIFEAFDELLLMKRGGQVIYSGPLG-RNSHKIIEYF 1116
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-67 |
9.53e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.80 E-value: 9.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1787163341 21 AVDGIDFDVRPDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVLEG 67
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-211 |
1.47e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 26 DFDVRPDEVFAIIGPNGAGKTTvfncvggFYKPTAGDIVLEghaiTGQPSHQvarrglvrtFQNI-RL-FKQLTVLenlm 103
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA-------LARALAGELPLL----SGERQSQ---------FSHItRLsFEQLQKL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 104 VAQHLKVNRN-MLS------GLFATPAYRRAERAALERAAYwLERVGLKQVANREAGTLSYGHQRRLEIARCMITDPRLL 176
Cdd:PRK10938 79 VSDEWQRNNTdMLSpgeddtGRTTAEIIQDEVKDPARCEQL-AQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1787163341 177 MLDEPAAGLNPQEKVELQQMVDGLRNEfGISVLLI 211
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
12-49 |
1.51e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 1.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1787163341 12 LQMR-FGGLLAVDGIDF-DVRPDEVFAIIGPNGAGKTTVF 49
Cdd:cd03279 6 LELKnFGPFREEQVIDFtGLDNNGLFLICGPTGAGKSTIL 45
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
25-52 |
2.40e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 2.40e-03
10 20
....*....|....*....|....*...
gi 1787163341 25 IDFDvRPDEVFAIIGPNGAGKTTVFNCV 52
Cdd:COG3950 19 IDFD-NPPRLTVLVGENGSGKTTLLEAI 45
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
23-49 |
2.54e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 2.54e-03
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-65 |
3.51e-03 |
|
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: 36.97 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|....*
gi 1787163341 31 PDEVFAIIGPNGAGKTTVFNCVGGFYKPTAGDIVL 65
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
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| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-243 |
4.40e-03 |
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Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.17 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 22 VDGIdfdVRPDEVFAIIGPNGAGKTTVFNCVG----GFYKPTAGDIVLEGHaitgqPSHQVAR--RG-LVRTFQNIRLFK 94
Cdd:TIGR00956 80 MDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGI-----TPEEIKKhyRGdVVYNAETDVHFP 151
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1787163341 95 QLTVLENLMVAQHLKVNRNMLSGLfatpayrRAERAALERAAYWLERVGLKQVANREAGT-----LSYGHQRRLEIARCM 169
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQNRPDGV-------SREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1787163341 170 ITDPRLLMLDEPAAGLNPQEKVE----LQQMVDGLRNEFGISVLLIEHDmslVMGVSDRILVMEHGKPIMIGKPDEVR 243
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEfiraLKTSANILDTTPLVAIYQCSQD---AYELFDKVIVLYEGYQIYFGPADKAK 299
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