|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-330 |
0e+00 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 518.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:COG1135 1 MIELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKF 237
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 238 IETLPQFE----DYDELPVADYKGCILRLGFTKETTTKPIISELIRQKNLDINIISGNIDKIKEGKVGHLIVEIF-EKDR 312
Cdd:COG1135 241 LPTVLNDElpeeLLARLREAAGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEgDDAA 320
|
330
....*....|....*...
gi 343398708 313 VDEIKNFLEDKKVLVEEV 330
Cdd:COG1135 321 IDAALAYLREQGVVVEVL 338
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-331 |
2.55e-166 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 466.59 E-value: 2.55e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:PRK11153 1 MIELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKF 237
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 238 I-ETLPQF--EDYDELPVADYKGC---ILRLGFTKETTTKPIISELIRQKNLDINIISGNIDKIKEGKVGHLIVEIF-EK 310
Cdd:PRK11153 241 IqSTLHLDlpEDYLARLQAEPTTGsgpLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTgDP 320
|
330 340
....*....|....*....|.
gi 343398708 311 DRVDEIKNFLEDKKVLVEEVN 331
Cdd:PRK11153 321 GDIQAAIAYLQEHGVKVEVLG 341
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-230 |
1.33e-133 |
|
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: 379.23 E-value: 1.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:cd03258 1 MIELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
1-328 |
1.33e-116 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 340.32 E-value: 1.33e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFK---AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:TIGR02314 81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKF 237
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 238 IET-----LPqfEDYDE-LPVADYKGC--ILRLGFTKETTTKPIISELIRQKNLDINIISGNIDKIKEGKVGHLIVEIFE 309
Cdd:TIGR02314 241 IRStlhlsIP--EDYQErLQATPFADSvpMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHG 318
|
330 340
....*....|....*....|
gi 343398708 310 KDRVDE-IKNFLEDKKVLVE 328
Cdd:TIGR02314 319 TQQDTQaAIAYLQEHNVKVE 338
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-245 |
5.90e-98 |
|
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: 298.74 E-value: 5.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYD----NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKE 76
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQ----SFNlfYQKNVFENIAYPLRINKW-KKKDIEERVNTLLEYVNLKEKIYE-YPANLSGGQKQRVAIAR 150
Cdd:COG1123 340 LRRRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
250
....*....|....*
gi 343398708 231 TATTKKFIETLPQFE 245
Cdd:COG1123 498 HPYTRALLAAVPSLD 512
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-241 |
7.87e-98 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 288.82 E-value: 7.87e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVkMNSKELKEARKN 80
Cdd:COG1126 1 MIEIENLHKSFGD-LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAY-PLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIE 239
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLS 237
|
..
gi 343398708 240 TL 241
Cdd:COG1126 238 KV 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-229 |
1.44e-89 |
|
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: 268.00 E-value: 1.44e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKN 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRIN-KWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-245 |
5.11e-87 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 261.66 E-value: 5.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnsKELKEA 77
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---RRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQ----SFNLFyqKNVFENIAYPLRINKwkKKDIEERVNTLLEYVNLKEKI-YEYPANLSGGQKQRVAIARAL 152
Cdd:COG1124 78 RRRVQMVFQdpyaSLHPR--HTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 153 AVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTA 232
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
250
....*....|...
gi 343398708 233 TTKKFIETLPQFE 245
Cdd:COG1124 234 YTRELLAASLAFE 246
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
1.04e-84 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 254.97 E-value: 1.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 R-KNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQP 156
Cdd:COG1136 84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 157 KILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEvVKAICDRAAVIENGEIIEQ 219
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-219 |
2.92e-84 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 253.97 E-value: 2.92e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQ----SFNlfYQKNVFENIAYPLRINK--WKKKDIEERVNTLLEYVNLKEKIYE-YPANLSGGQKQRVAIAR 150
Cdd:cd03257 81 RKEIQMVFQdpmsSLN--PRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGLPEEVLNrYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
3.99e-84 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 254.21 E-value: 3.99e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKN 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENI-----AY--PLR--INKWKKKDIEeRVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARA 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlGRtsTWRslLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-229 |
6.94e-84 |
|
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: 253.19 E-value: 6.94e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKNM 81
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRIN-KWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-216 |
8.24e-82 |
|
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: 247.40 E-value: 8.24e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEAR 78
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 -KNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKaICDRAAVIENGEI 216
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-218 |
1.06e-81 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 247.27 E-value: 1.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKN 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-230 |
2.97e-81 |
|
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: 249.59 E-value: 2.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEP---TQGNIFIDGKDIVKMNSKEL 74
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 75 KEAR-KNMAMIFQ----SFNLFYqkNVFENIAYPLRI-NKWKKKDIEERVNTLLEYVNL---KEKIYEYPANLSGGQKQR 145
Cdd:COG0444 81 RKIRgREIQMIFQdpmtSLNPVM--TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 146 VAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKL 225
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 343398708 226 FTSPK 230
Cdd:COG0444 239 FENPR 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-217 |
1.65e-80 |
|
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: 244.78 E-value: 1.65e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKNM 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPL--RINKWK-------KKDIeERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARAL 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgRRSTWRslfglfpKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 153 AVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-238 |
8.89e-80 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 246.93 E-value: 8.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVkmnskELKEARKN 80
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITH-QMEVVkAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdQEEAL-ALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFI 236
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-220 |
1.32e-79 |
|
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: 241.65 E-value: 1.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskeLKEARKNM 81
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQD 220
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-216 |
2.21e-79 |
|
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: 240.89 E-value: 2.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmNSKELKEARKNM 81
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAY-PLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-217 |
4.38e-79 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 241.43 E-value: 4.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKN 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENI---------AYPLRINKWKKKDIEERVNtLLEYVNLKEKIYEYPANLSGGQKQRVAIARA 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEEDKERALS-ALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-242 |
2.62e-78 |
|
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: 240.24 E-value: 2.62e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEAR-KNMAMIFQSFNLFYQKN 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 96 VFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKS 175
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 176 ILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIETLP 242
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-227 |
2.17e-77 |
|
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: 236.46 E-value: 2.17e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnsKELKEARKNM 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQ-SFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:COG1122 78 GLVFQnPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFT 227
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-238 |
6.97e-76 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 233.39 E-value: 6.97e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRL--EEP---TQGNIFIDGKDI--VKMNSKEL 74
Cdd:COG1117 12 IEVRNL-NVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 75 keaRKNMAMIFQSFNLFyQKNVFENIAYPLRINKWK-KKDIEERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIA 149
Cdd:COG1117 91 ---RRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKsKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFnlTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:COG1117 167 RALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
....*....
gi 343398708 230 KTATTKKFI 238
Cdd:COG1117 245 KDKRTEDYI 253
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-239 |
2.84e-75 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 236.54 E-value: 2.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIY-----------DNG------FK------AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQG 57
Cdd:COG4175 3 KIEVRNLYKIFgkrperalkllDQGkskdeiLEktgqtvGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 58 NIFIDGKDIVKMNSKELKEAR-KNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPA 136
Cdd:COG4175 83 EVLIDGEDITKLSKKELRELRrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 137 NLSGGQKQRVAIARALAVQPKILLCDEATSALDP------QstksilELLLKIRDEFNLTIVLITHQM-EVVKaICDRAA 209
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirremQ------DELLELQAKLKKTIVFITHDLdEALR-LGDRIA 235
|
250 260 270
....*....|....*....|....*....|
gi 343398708 210 VIENGEIIEQDTVLKLFTSPKTATTKKFIE 239
Cdd:COG4175 236 IMKDGRIVQIGTPEEILTNPANDYVADFVE 265
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-215 |
2.60e-74 |
|
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: 226.68 E-value: 2.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNsKELKEARKNM 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLrinkwkkkdieervntlleyvnlkekiyeypanlSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGE 215
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-238 |
1.91e-73 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 230.42 E-value: 1.91e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDI-VKMNSKElkearKN 80
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE-----RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-218 |
3.28e-73 |
|
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: 225.52 E-value: 3.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEE-----PTQGNIFIDGKDIVKMNSKELkE 76
Cdd:cd03260 1 IELRDL-NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVL-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQSFNLFyQKNVFENIAYPLRIN-KWKKKDIEERVNTLLEYVNLKEKIYE--YPANLSGGQKQRVAIARALA 153
Cdd:cd03260 79 LRRRVGMVFQKPNPF-PGSIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 154 VQPKILLCDEATSALDPQSTKSILELLLKIRDEfnLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-230 |
6.26e-73 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 228.46 E-value: 6.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYD--NGF--------KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNS 71
Cdd:COG4608 8 LEVRDLKKHFPvrGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 72 KELKEARKNMAMIFQ----SFNLfyQKNVFENIAYPLRINK-WKKKDIEERVNTLLEYVNLK-EKIYEYPANLSGGQKQR 145
Cdd:COG4608 88 RELRPLRRRMQMVFQdpyaSLNP--RMTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 146 VAIARALAVQPKILLCDEATSALDpqstKSI----LELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALD----VSIqaqvLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
....*....
gi 343398708 222 VLKLFTSPK 230
Cdd:COG4608 242 RDELYARPL 250
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-225 |
1.03e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 224.56 E-value: 1.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskELKEARKNM 81
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR----DPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKL 225
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-238 |
2.18e-72 |
|
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: 224.10 E-value: 2.18e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIY--EYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFadRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-215 |
5.47e-71 |
|
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: 219.26 E-value: 5.47e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 3 KIENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKNM 81
Cdd:cd03225 1 ELKNLSFSYPDGARPAlDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNL-FYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGE 215
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-238 |
2.12e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 222.64 E-value: 2.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnsKELKEARKN 80
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITH-QMEVVkAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHdQVEAM-TLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFI 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
3.71e-70 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 218.81 E-value: 3.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIY---DNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnskelKEA 77
Cdd:COG1116 7 ALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV--------TGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQsTKSIL-ELLLKIRDEFNLTIVLITHQMEvvKAI--CDRAAVIEN--GEIIEQDTV 222
Cdd:COG1116 159 VLLMDEPFGALDAL-TRERLqDELLRLWQETGKTVLFVTHDVD--EAVflADRVVVLSArpGRIVEEIDV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-222 |
2.56e-69 |
|
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: 215.41 E-value: 2.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnskelKEAR 78
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV--------TGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKI 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 159 LLCDEATSALDPQsTKSIL-ELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIEN--GEIIEQDTV 222
Cdd:cd03293 153 LLLDEPFSALDAL-TREQLqEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEVEV 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-230 |
1.59e-68 |
|
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: 215.39 E-value: 1.59e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG----FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQsF---NLFyQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEY-PANLSGGQKQRVAIARALA 153
Cdd:TIGR04521 81 RKKVGLVFQ-FpehQLF-EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 154 VQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-245 |
1.66e-68 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 223.02 E-value: 1.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEePTQGNIFIDGKDIVKMNSKELKEARKNMAMIFQ----SFN- 89
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQdpfgSLSp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 90 -LfyqkNVFENIAYPLRIN--KWKKKDIEERVNTLLEYVNLKEKIYE-YPANLSGGQKQRVAIARALAVQPKILLCDEAT 165
Cdd:COG4172 378 rM----TVGQIIAEGLRVHgpGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 166 SALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIETLPQFE 245
Cdd:COG4172 454 SALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLLE 533
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-238 |
8.27e-68 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 212.10 E-value: 8.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskeLKEARKNM 81
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-221 |
5.87e-66 |
|
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: 207.97 E-value: 5.87e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKN 80
Cdd:COG0411 4 LLEVRGLTKRFG-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--ARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENI-------------AYPLRINKWKK--KDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVlvaaharlgrgllAALLRLPRARReeREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 146 VAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-239 |
1.04e-65 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 206.87 E-value: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdnGFKAVT-NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDiVKMNSKELKEARK 79
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQVLhNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK-VNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQSFNLFYQKNVFENIAY-PLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKI 158
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
.
gi 343398708 239 E 239
Cdd:PRK09493 237 Q 237
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-230 |
1.11e-65 |
|
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: 215.15 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNG-FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPT---QGNIFIDGKDIVKMNSKELke 76
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 aRKNMAMIFQ----SFNLFyqkNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARAL 152
Cdd:COG1123 82 -GRRIGMVFQdpmtQLNPV---TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 153 AVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-216 |
1.61e-63 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 200.33 E-value: 1.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKNM 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-238 |
9.17e-63 |
|
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: 199.49 E-value: 9.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkearKNM 81
Cdd:cd03296 3 IEVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWK----KKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSerppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKF 237
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSF 236
|
.
gi 343398708 238 I 238
Cdd:cd03296 237 L 237
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-221 |
4.52e-62 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 198.42 E-value: 4.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFK-AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkMNSKELKEARKN 80
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:TIGR04520 79 VGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDII 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQM-EVVKAicDRAAVIENGEIIEQDT 221
Cdd:TIGR04520 159 ILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMeEAVLA--DRVIVMNKGKIVAEGT 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-239 |
5.96e-61 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 194.97 E-value: 5.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQG-----NIFIDGKDIVKMNSKELK 75
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 EARKNMAMIFQSFNLFYQKNVFEN-IAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAV 154
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATT 234
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
....*
gi 343398708 235 KKFIE 239
Cdd:PRK11264 241 RQFLE 245
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
21-238 |
6.62e-61 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 195.40 E-value: 6.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDI----------VKMNSKELKEARKNMAMIFQSFNL 90
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelVPADRRQLQRIRTRLGMVFQSFNL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 91 FYQKNVFEN-IAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:COG4598 107 WSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 170 PQstksiL--ELLLKIRD--EFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:COG4598 187 PE-----LvgEVLKVMRDlaEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQFL 254
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-238 |
9.02e-61 |
|
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: 194.09 E-value: 9.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKaVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVkmnskELKEARKNM 81
Cdd:cd03299 1 LKVENLSKDWKE-FK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-241 |
5.12e-60 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 192.54 E-value: 5.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDI---VKMNSKELKEAR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNMAMIFQSFNLFYQKNVFEN-IAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRdEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTvLKLFTSPKtatTKKF 237
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQ---TEAF 236
|
....
gi 343398708 238 IETL 241
Cdd:COG4161 237 AHYL 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
1.12e-59 |
|
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: 190.54 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkearKNM 81
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGeIIEQ 219
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG-QIQQ 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-217 |
6.08e-59 |
|
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: 189.57 E-value: 6.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKNM 81
Cdd:cd03219 1 LEVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIA--------YPLRINKWKK--KDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARA 151
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMvaaqartgSGLLLARARReeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRdEFNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-222 |
1.46e-58 |
|
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: 188.53 E-value: 1.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskELKEARKN 80
Cdd:COG4555 1 MIEVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTV 222
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-216 |
3.62e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 186.56 E-value: 3.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVkiYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:COG4619 1 LELEGLS--FRVGGKPIlSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---RRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQkNVFENIAYPLRINKwkKKDIEERVNTLLEYVNLKEKIYEYPA-NLSGGQKQRVAIARALAVQPKIL 159
Cdd:COG4619 76 VAYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-238 |
7.34e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 186.50 E-value: 7.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAvtNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSkelkeARKN 80
Cdd:COG3840 1 MLRLDDLTYRY-GDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-----AERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAY---P-LRINKWKKKdieeRVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALaVQP 156
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLglrPgLKLTAEQRA----QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 157 K-ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTK 235
Cdd:COG3840 148 RpILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
...
gi 343398708 236 KFI 238
Cdd:COG3840 228 AYL 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-228 |
1.37e-57 |
|
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: 186.40 E-value: 1.37e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKn 80
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--ARR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQS----FNLfyqkNVFENIA---YPLR--INKWKKKDiEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARA 151
Cdd:COG1120 77 IAYVPQEppapFGL----TVRELVAlgrYPHLglFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTS 228
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTP 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-216 |
6.34e-57 |
|
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: 182.21 E-value: 6.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskELKEARKNM 81
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIayplrinkwkkkdieervntlleyvnlkekiyeypaNLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-225 |
1.89e-56 |
|
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: 182.57 E-value: 1.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskELKEARKNM 81
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKL 225
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-247 |
5.25e-56 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 182.14 E-value: 5.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDI---VKMNSKELKEAR 78
Cdd:PRK11124 3 IQLNGINCFYGAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNMAMIFQSFNLFYQKNVFEN-IAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRdEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVlKLFTSPKTattkkf 237
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQT------ 233
|
250
....*....|
gi 343398708 238 ietlPQFEDY 247
Cdd:PRK11124 234 ----EAFKNY 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-215 |
5.85e-54 |
|
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: 174.49 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL---RKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyQKNVFENIayplrinkwkkkdieervntlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKaICDRAAVIENGE 215
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-245 |
5.94e-54 |
|
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: 184.50 E-value: 5.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENL-VKIYDNG--FKAVTNINLEIKKGEIFGIIGMSGAGKS----SLIRCINRLEEPTQGNIFIDGKDIVKMNSKE 73
Cdd:COG4172 6 LLSVEDLsVAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 74 LKEARKN-MAMIFQ----SFN-LFyqkNVFENIAYPLRINK-WKKKDIEERVNTLLEYVNLKE---KIYEYPANLSGGQK 143
Cdd:COG4172 86 LRRIRGNrIAMIFQepmtSLNpLH---TIGKQIAEVLRLHRgLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 144 QRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVL 223
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242
|
250 260
....*....|....*....|..
gi 343398708 224 KLFTSPKTATTKKFIETLPQFE 245
Cdd:COG4172 243 ELFAAPQHPYTRKLLAAEPRGD 264
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-225 |
8.06e-54 |
|
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: 175.77 E-value: 8.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG-FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVkmnsKELKEARKN 80
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKL 225
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-221 |
1.35e-53 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 186.58 E-value: 1.35e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:COG2274 474 IELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQkNVFENIAYplrinkWKKKDIEERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIA 149
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITL------GDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKaICDRAAVIENGEIIEQDT 221
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGT 692
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
11-221 |
2.23e-53 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 184.21 E-value: 2.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 11 YDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNL 90
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 91 FyQKNVFENIAYPlrinkwkKKDI-EERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIARALAVQPKI 158
Cdd:COG1132 426 F-SGTIRENIRYG-------RPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-226 |
3.37e-52 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 173.70 E-value: 3.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGF----KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKeLKEA 77
Cdd:PRK13637 3 IKIENLTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQ--SFNLFyQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIY--EYPANLSGGQKQRVAIARALA 153
Cdd:PRK13637 82 RKKVGLVFQypEYQLF-EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYkdKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 154 VQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLF 226
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-166 |
8.41e-52 |
|
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: 168.21 E-value: 8.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKNMAMIFQSFNLFYQKNVF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 98 ENIAYPLRINKWKKKDIEERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATS 166
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
1.29e-51 |
|
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: 170.31 E-value: 1.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVT---NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 R-KNMAMIFQSFNLFYQKNVFENIAYPLRINKwkKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQP 156
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 157 KILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-219 |
2.31e-51 |
|
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: 168.00 E-value: 2.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 3 KIENLVKIYDNGFkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKnma 82
Cdd:cd03214 1 EVENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL--ARK--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 mifqsfnlfyqknvfenIAYplrinkwkkkdieerVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCD 162
Cdd:cd03214 75 -----------------IAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 163 EATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-239 |
2.97e-51 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 170.40 E-value: 2.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG--------FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdivKMNSKE 73
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 74 LKEARKNMAMIFQ----SFNLfyQKNVFENIAYPLRIN-KWKKKDIEERVNTLLEYVNL-KEKIYEYPANLSGGQKQRVA 147
Cdd:COG4167 82 YKYRCKHIRMIFQdpntSLNP--RLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 148 IARALAVQPKILLCDEATSALDPqSTKS-ILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLF 226
Cdd:COG4167 160 LARALILQPKIIIADEALAALDM-SVRSqIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
250
....*....|...
gi 343398708 227 TSPKTATTKKFIE 239
Cdd:COG4167 239 ANPQHEVTKRLIE 251
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-242 |
5.96e-51 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 171.81 E-value: 5.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKNMAMIFQ----SFNLf 91
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQdplaSLNP- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 yQKNVFENIAYPLRIN--KWKKKDIEERVNTLLEYVNLKEK-IYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:PRK15079 114 -RMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNlINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 169 DPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIETLP 242
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-219 |
6.11e-51 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 172.58 E-value: 6.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkearKNM 81
Cdd:PRK10851 3 IEIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRI----NKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGeIIEQ 219
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIEQ 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-215 |
1.40e-50 |
|
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: 165.11 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 3 KIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKNMA 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 MIFQsfnlfyqknvfeniayplrinkwkkkdieervntlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILLCD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 343398708 163 EATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGE 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-238 |
1.66e-50 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 168.42 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRL-----EEPTQGNIFIDGKDIVKMNSKELk 75
Cdd:PRK14239 5 ILQVSDL-SVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 EARKNMAMIFQSFNLFyQKNVFENIAYPLRINKWKKKDI-EERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIAR 150
Cdd:PRK14239 83 DLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFnlTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
....*...
gi 343398708 231 TATTKKFI 238
Cdd:PRK14239 240 HKETEDYI 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-245 |
2.24e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 171.56 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnskelKEARKN 80
Cdd:PRK11607 19 LLEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-----PPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIET 240
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGS 252
|
....*
gi 343398708 241 LPQFE 245
Cdd:PRK11607 253 VNVFE 257
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
6.53e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.42 E-value: 6.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnskelKEARKN 80
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQ--SFNLFYQKNVFENIA---YP-LRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAV 154
Cdd:COG1121 77 IGYVPQraEVDWDFPITVRDVVLmgrYGrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIeNGEIIEQDTVLKLFTSP 229
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-238 |
1.21e-49 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 166.30 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDI--VKMNSKELKEARKN--------MAMIFQSFNL 90
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlVRDKDGQLKVADKNqlrllrtrLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 91 FYQKNVFENI-AYPLRINKWKKKDIEERVNTLLEYVNLKEKIY-EYPANLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:PRK10619 104 WSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 169 DPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-238 |
5.40e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 167.82 E-value: 5.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSkelkEARkNM 81
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA----ENR-HV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFI 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
7.50e-49 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 163.93 E-value: 7.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRL-----EEPTQGNIFIDGKDIVKMNSKELke 76
Cdd:PRK14247 4 IEIRDL-KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 aRKNMAMIFQSFNLFYQKNVFENIAYPLRINKW--KKKDIEERVNTLLEYVNLKEKI---YEYPA-NLSGGQKQRVAIAR 150
Cdd:PRK14247 81 -RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVkdrLDAPAgKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfnLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPR 237
|
....*...
gi 343398708 231 TATTKKFI 238
Cdd:PRK14247 238 HELTEKYV 245
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-237 |
1.00e-48 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 167.90 E-value: 1.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEAR-KNMAMIFQSFNLFYQKN 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 96 VFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKS 175
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 176 ILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKF 237
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-239 |
1.44e-48 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 163.80 E-value: 1.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEE-----PTQGNIFIDGKDIvkmNSKELK- 75
Cdd:PRK14243 11 LRTENL-NVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNL---YAPDVDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 -EARKNMAMIFQSFNLFyQKNVFENIAYPLRINKWKKkDIEERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIAR 150
Cdd:PRK14243 87 vEVRRRIGMVFQKPNPF-PKSIYDNIAYGARINGYKG-DMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFnlTIVLITHQMEVVKAICDRAAV---------IENGEIIEQDT 221
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFfnvelteggGRYGYLVEFDR 242
|
250
....*....|....*...
gi 343398708 222 VLKLFTSPKTATTKKFIE 239
Cdd:PRK14243 243 TEKIFNSPQQQATRDYVS 260
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-217 |
7.24e-48 |
|
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: 160.01 E-value: 7.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 3 KIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnskelkeaRKNMA 82
Cdd:cd03235 1 EVEDLTVSYGG-HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 MIFQSFNLfyqknvfeNIAYPLRIN--------------KWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAI 148
Cdd:cd03235 72 YVPQRRSI--------DRDFPISVRdvvlmglyghkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 149 ARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIeNGEII 217
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
1.61e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 161.31 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFK-AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARK 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKI 158
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQM-EVVKAicDRAAVIENGEIIEQDTVLKLFTSpktattKKF 237
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAILA--DKVIVFSEGKLIAQGKPKEILNN------KEI 235
|
..
gi 343398708 238 IE 239
Cdd:PRK13632 236 LE 237
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-226 |
3.14e-47 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 160.57 E-value: 3.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFK-AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdivKMNSKELKEARKN 80
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQM-EVVKAicDRAAVIENGEIIEQDTVLKLF 226
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLdEAAQA--DRVIVMNKGEILEEGTPEEIF 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-220 |
5.11e-47 |
|
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: 157.84 E-value: 5.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKkGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSK-ELKEARKNMAMIFQSFNLFYQKNVFE 98
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 99 NIAYPLRINKWKKKDIeeRVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILE 178
Cdd:cd03297 95 NLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343398708 179 LLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQD 220
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-229 |
1.97e-46 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 158.31 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIY-------DNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSK 72
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgKHQHQTVlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 73 ELKEARKNMAMIFQ----SFNLfyQKNVFENIAYPLR-INKWKKKDIEERVNTLLEYVNLKEKIYE-YPANLSGGQKQRV 146
Cdd:PRK10419 83 QRKAFRRDIQMVFQdsisAVNP--RKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 147 AIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKL- 225
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKl 240
|
....*
gi 343398708 226 -FTSP 229
Cdd:PRK10419 241 tFSSP 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.99e-46 |
|
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: 164.93 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQkNVFENIAyplrinkWKKKDI-EERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIA 149
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLR-------LGRPDAsDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
5.46e-46 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 156.54 E-value: 5.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRL-----EEPTQGNIFIDGKDIVKMNSKELkE 76
Cdd:PRK14267 5 IETVNL-RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI-E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQSFNLFYQKNVFENIAYPLRINKW--KKKDIEERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIAR 150
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFnlTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
....*...
gi 343398708 231 TATTKKFI 238
Cdd:PRK14267 241 HELTEKYV 248
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-221 |
8.88e-46 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 154.90 E-value: 8.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKNM 81
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENI---AYPLRINKwKKKDIEErvntLLEYV-NLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLllgAYARRRAK-RKARLER----VYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-201 |
1.77e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 154.26 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKN 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 343398708 161 CDEATSALDPQSTKSILELLlkirDEFN---LTIVLITHQMEVV 201
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLF----EEFNrvgVTVLMATHDIGLI 200
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
2.48e-45 |
|
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: 153.50 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGfKAVTNINLEIKKGeIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKelkeARKNM 81
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
20-231 |
2.60e-45 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 157.57 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkearKNMAMIFQSFNLFYQKNVFEN 99
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RDICMVFQSYALFPHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILEl 179
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRE- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 180 llKIRD---EFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKT 231
Cdd:PRK11432 178 --KIRElqqQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPAS 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-217 |
1.50e-44 |
|
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: 151.75 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDN---GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskELKEA 77
Cdd:cd03266 1 MITADALTKRFRDvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-217 |
5.41e-44 |
|
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: 148.35 E-value: 5.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKN- 80
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---SFASPRDARRAg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQsfnlfyqknvfeniayplrinkwkkkdieervntlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03216 77 IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-280 |
1.17e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 151.80 E-value: 1.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdivKMNSKE------L 74
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDrrrigyL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 75 KEAR---KNMamifqsfnlfyqkNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARA 151
Cdd:COG4152 77 PEERglyPKM-------------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTV--LKlftsp 229
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVdeIR----- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 230 KTATTKKF-IETLPQFEDYDELP---VADYKGCILRLGFTKETTTKPIISELIRQ 280
Cdd:COG4152 218 RQFGRNTLrLEADGDAGWLRALPgvtVVEEDGDGAELKLEDGADAQELLRALLAR 272
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-230 |
1.36e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 152.43 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKNMAMIFQ----SFNLf 91
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQnpygSLNP- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 yQKNVFENIAYPLRIN-KWKKKDIEERVNTLLEYVNLKEKIYE-YPANLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:PRK11308 108 -RKKVGQILEEPLLINtSLSAAERREKALAMMAKVGLRPEHYDrYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 170 PQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-238 |
1.40e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 150.57 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEpTQGNIFIDGK-DIVKMNSKE----LKE 76
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFFNQNIYErrvnLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQSFNLFyQKNVFENIAYPLRINKWKKK-DIEERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIARA 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIEN-----GEIIEQDTVLKLF 226
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
250
....*....|..
gi 343398708 227 TSPKTATTKKFI 238
Cdd:PRK14258 245 NSPHDSRTREYV 256
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-226 |
1.52e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 151.04 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVT--NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaR 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTlnDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI---R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNMAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVkAICDRAAVIENGEIIEQDTVLKLF 226
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELF 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-229 |
2.28e-43 |
|
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: 152.56 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKE-LKEARKNMAMIFQSFNLFYQKNVFE 98
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIfLPPHRRRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 99 NIAYPLRINKWKKKDIE-ERVNTLLEYVNLKEKiyeYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSIL 177
Cdd:COG4148 97 NLLYGRKRAPRAERRISfDEVVELLGIGHLLDR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 343398708 178 ELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
2.43e-43 |
|
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: 148.98 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKN 80
Cdd:COG0410 3 MLEVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENI---AYPLRinkwKKKDIEERVNTLLEYV-NLKEKIYEYPANLSGGQKQRVAIARALAVQP 156
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEENLllgAYARR----DRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 157 KILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGT 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
2.62e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 150.38 E-value: 2.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvKMNSKELKEARKN 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLkEKIYEYPAN-LSGGQKQRVAIARALAVQPKI 158
Cdd:PRK13636 84 VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLF 226
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-226 |
3.88e-43 |
|
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: 148.53 E-value: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFyQKNVFENIAYPLRINKwkkkdiEERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIAR 150
Cdd:cd03254 80 GVVLQDTFLF-SGTIMENIRLGRPNAT------DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVLKLF 226
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
5.96e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 149.46 E-value: 5.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvKMNSKELKEARKN 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQ-SFNLFYQKNVFENIAY-PLRInKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKI 158
Cdd:PRK13639 80 VGIVFQnPDDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKT 231
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-222 |
6.74e-43 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.41 E-value: 6.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSkelKEARKN 80
Cdd:COG1129 4 LLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSP---RDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 -MAMIFQSFNLFYQKNVFENIA---YPLR---INkWKKkdIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALA 153
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAENIFlgrEPRRgglID-WRA--MRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 154 VQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTV 222
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPV 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-229 |
9.31e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 149.40 E-value: 9.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIV-KMNSKELKEARKNMAMIFQsfnlFYQK 94
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRKKVGIVFQ----FPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 95 NVFE-----NIAY-PLRINKwKKKDIEERVNTLLEYVNLKEKIYEY-PANLSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:PRK13634 97 QLFEetvekDICFgPMNFGV-SEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 168 LDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-221 |
1.19e-42 |
|
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: 146.87 E-value: 1.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNskeLKEARKN 80
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyQKNVFENIAyPLriNKWKkkdiEERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIA 149
Cdd:cd03244 80 ISIIPQDPVLF-SGTIRSNLD-PF--GEYS----DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELllkIRDEF-NLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-217 |
1.79e-42 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 153.26 E-value: 1.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDiVKMNSKelKEARKN 80
Cdd:COG3845 5 ALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-VRIRSP--RDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 -MAMIFQSFNLFYQKNVFENIAY---PLRINKWKKKDIEERVNTLLE-Y---VNLKEKIyeypANLSGGQKQRVAIARAL 152
Cdd:COG3845 81 gIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSErYgldVDPDAKV----EDLSVGEQQRVEILKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 153 AVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-221 |
2.34e-42 |
|
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: 146.61 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDN-GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnskELKEARKN 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQkNVFENIAYPlrinkwKKKDIEERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIA 149
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYG------RPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSI---LELLLKIRdefnlTIVLITHQMEVVKAIcDRAAVIENGEIIEQDT 221
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVqaaLERLMKNR-----TTFVIAHRLSTIENA-DRIVVLEDGKIVERGT 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-238 |
7.41e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 145.96 E-value: 7.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 10 IYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGK------DIVKMNSKELkeaRKNMAM 83
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKL---RKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 84 IFQSFNLFYQKNVFENIAYPLRINKWK-KKDIEERVNTLLEYVNLKEKIYE---YPAN-LSGGQKQRVAIARALAVQPKI 158
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDrlnSPASqLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEfnLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-239 |
7.90e-42 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 152.17 E-value: 7.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSS----LIRCINrleepTQGNIFIDGKDIVKMNSKELKEARKNMAMIFQSFN--L 90
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNssL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 91 FYQKNVFENIAYPLRINK--WKKKDIEERVNTLLEYVNLK-EKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 168 LDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIE 239
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-242 |
1.24e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 153.09 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKNMAMIFQS--FNLFYQK 94
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 95 NVFENIAYPLRINKW-KKKDIEERVNTLLEYVNLK-EKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQS 172
Cdd:PRK10261 419 TVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 173 TKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIETLP 242
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVP 568
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
5-263 |
2.05e-41 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 145.29 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 5 ENLVKIYDNGF-----KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARK 79
Cdd:PRK11831 5 ANLVDMRGVSFtrgnrCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQSFNLFYQKNVFENIAYPLRIN-KWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKI 158
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 159 LLCDEATSALDPQStksiLELLLKIRDEFN----LTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKtATT 234
Cdd:PRK11831 165 IMFDEPFVGQDPIT----MGVLVKLISELNsalgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRV 239
|
250 260
....*....|....*....|....*....
gi 343398708 235 KKFIETLPQFEDYDELPVADYKGCILRLG 263
Cdd:PRK11831 240 RQFLDGIADGPVPFRYPAGDYHADLLGGG 268
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-219 |
2.30e-41 |
|
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: 143.40 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 23 LEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSkelkeARKNMAMIFQSFNLFYQKNVFENIAY 102
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-----ADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 103 PLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLK 182
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 343398708 183 IRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-243 |
2.67e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 145.23 E-value: 2.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFK-----AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSkeLK 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 EARKNMAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAV 154
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQM-EVVKAicDRAAVIENGEIIEQDTVLKLFtsPKTAT 233
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMeEAVEA--DRIIVMDSGKVVMEGTPKEIF--KEVEM 237
|
250
....*....|
gi 343398708 234 TKKFIETLPQ 243
Cdd:PRK13633 238 MKKIGLDVPQ 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-254 |
7.57e-41 |
|
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: 149.18 E-value: 7.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLE--EPTQGNIFI----------------DG 63
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYhvalcekcgyverpskVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 64 K--------------DIVKMNSKELKEARKNMAMIFQ-SFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLK 128
Cdd:TIGR03269 80 EpcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 129 EKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRA 208
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 343398708 209 AVIENGEIIEQDTVLKLftspktatTKKFIETLPQFEDYDELPVAD 254
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV--------VAVFMEGVSEVEKECEVEVGE 277
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-238 |
1.45e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 145.37 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnsKELKEARKN 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-----NELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVN---TLLEyvnlkekIYEY----PANLSGGQKQRVAIARALA 153
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAeaaRILE-------LEPLldrkPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 154 VQPKILLCDEATSALDpqsTKSILELLLKIRD---EFNLTIVLITH-QMEVVkAICDRAAVIeNGEIIEQ-DTVLKLFTS 228
Cdd:PRK11650 151 REPAVFLFDEPLSNLD---AKLRVQMRLEIQRlhrRLKTTSLYVTHdQVEAM-TLADRVVVM-NGGVAEQiGTPVEVYEK 225
|
250
....*....|
gi 343398708 229 PKTATTKKFI 238
Cdd:PRK11650 226 PASTFVASFI 235
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-219 |
2.06e-40 |
|
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: 140.82 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskeLKEARKNM 81
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-----NIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEErvntLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-221 |
3.20e-40 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 141.67 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 14 GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKNMAMIFQSFNLFYQ 93
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 94 KNVFEN--IAYPLRINK-----------WKKKDIE--ERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKI 158
Cdd:PRK11300 95 MTVIENllVAQHQQLKTglfsgllktpaFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-214 |
4.13e-40 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 140.68 E-value: 4.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnskelKEARKNMAMIFQSFNLFYQKNVFEN 99
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI--------TEPGPDRMVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAypLRINK----WKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKS 175
Cdd:TIGR01184 75 IA--LAVDRvlpdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 343398708 176 ILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENG 214
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-238 |
6.99e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 143.63 E-value: 6.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdivKMNskELKEARKNMAMIFQSFNLFYQKNVFEN 99
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMN--DVPPAERGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDP----QSTKS 175
Cdd:PRK11000 96 MSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrvQMRIE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 176 ILELLLKIRDefnlTIVLITH-QMEVVkAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFI 238
Cdd:PRK11000 176 ISRLHKRLGR----TMIYVTHdQVEAM-TLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-221 |
7.39e-40 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 139.98 E-value: 7.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNLFYqKNVFEN 99
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL---RSQIGLVSQEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLriNKWKKKDIEE--RVNTLLEYVNLKEKIY-----EYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQS 172
Cdd:cd03249 97 IRYGK--PDATDEEVEEaaKKANIHDFIMSLPDGYdtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 343398708 173 TKSILELLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:cd03249 175 EKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-221 |
1.81e-39 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 139.01 E-value: 1.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVK--MNskelKEAR 78
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMH----KRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNM------AMIFQsfNLfyqkNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLkEKIYEYPAN-LSGGQKQRVAIARA 151
Cdd:COG1137 78 LGIgylpqeASIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKAYsLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTiVLIT-HQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIG-VLITdHNVRETLGICDRAYIISEGKVLAEGT 219
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-217 |
2.32e-39 |
|
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: 137.77 E-value: 2.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 4 IENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskelKEARKNMAM 83
Cdd:cd03226 2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 84 IFQS--FNLFyqknvFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03226 76 VMQDvdYQLF-----TDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-221 |
2.53e-39 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 138.77 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSfNLFYQKNV 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQVGVVLQE-NVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 97 FENIAY-----PLR--INKWKKKDIEERVNTLLEYVNlkEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:cd03252 93 RDNIALadpgmSMErvIEAAKLAGAHDFISELPEGYD--TIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 343398708 170 PQSTKSILELLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:cd03252 171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-229 |
2.71e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 139.74 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDivKMNSKELKEARKN 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNL-FYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-216 |
3.33e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 138.18 E-value: 3.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNgfkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSkelkeARKN 80
Cdd:PRK10771 1 MLKLTDITWLYHH---LPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP-----SRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIA---YP-LRINKWKKKDIEErvntLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQP 156
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGlglNPgLKLNAAQREKLHA----IARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 157 KILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-219 |
4.08e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 137.99 E-value: 4.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEAR-KNMAMIFQSFNLFYQKNV 96
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 97 FENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSI 176
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 343398708 177 LELLLKIRDEFNLTIVLITHQMEVVkAICDRAAVIENGEIIEQ 219
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQEE 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-230 |
8.01e-39 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 137.29 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKelKEARKNM 81
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH--KRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDeFNLTiVLIT-HQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKD-RGIG-VLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-221 |
1.40e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 143.75 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDN-GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:COG4987 334 LELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQkNVFEN--IAYPlrinkwkkkDI-EERVNTLLEYVNLKE-----------KIYEYPANLSGGQKQRV 146
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENlrLARP---------DAtDEELWAALERVGLGDwlaalpdgldtWLGEGGRRLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 147 AIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVkAICDRAAVIENGEIIEQDT 221
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGT 552
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
4.17e-38 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 136.35 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 4 IENLVKIYdnGFKAVTN-INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFidgkdivkMNSKELKEARKNMA 82
Cdd:PRK11247 15 LNAVSKRY--GERTVLNqLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL--------AGTAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 MIFQSFNLFYQKNVFENIAYPLRiNKWKKKDIEErvntlLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCD 162
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLK-GQWRDAALQA-----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 343398708 163 EATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-221 |
9.39e-38 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 134.67 E-value: 9.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDI--VKMNSkelkeARK 79
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIreVTLDS-----LRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQSFNLFyQKNVFENIAY-------PLRINKWKKKDIEERVNTLLE-YvnlKEKIYEYPANLSGGQKQRVAIARA 151
Cdd:cd03253 76 AIGVVPQDTVLF-NDTIGYNIRYgrpdatdEEVIEAAKAAQIHDKIMRFPDgY---DTIVGERGLKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 152 LAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
9.66e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.21 E-value: 9.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGF----KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnsKELKE 76
Cdd:COG1101 1 MLELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL--PEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARkNMAMIFQ------SFNLfyqkNVFEN--IAY------PLR--INKWKKKDIEERVNTL---LEYvNLKEKIyeypAN 137
Cdd:COG1101 79 AK-YIGRVFQdpmmgtAPSM----TIEENlaLAYrrgkrrGLRrgLTKKRRELFRELLATLglgLEN-RLDTKV----GL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 138 LSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-216 |
1.10e-37 |
|
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: 132.34 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPVlRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyQKNVFENIayplrinkwkkkdieervntlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03246 78 VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 161 CDEATSALDPQSTKSILELL--LKIRdefNLTIVLITHQMEVVkAICDRAAVIENGEI 216
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIaaLKAA---GATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-223 |
1.15e-37 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 134.17 E-value: 1.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 6 NLVKIYDNG---FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKN-M 81
Cdd:PRK11629 10 NLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQkL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAIcDRAAVIENGEIIEQDTVL 223
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSLM 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-249 |
1.20e-37 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 136.78 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEP---TQGNIFIDGKDIVKMNSKELKEAR-KNMAMIFQ----SF 88
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRaEQISMIFQdpmtSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 89 NLfYQKnVFENIAYPLRINKW--KKKDIEERVNtLLEYVNLKE---KIYEYPANLSGGQKQRVAIARALAVQPKILLCDE 163
Cdd:PRK09473 111 NP-YMR-VGEQLMEVLMLHKGmsKAEAFEESVR-MLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 164 ATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIETLPQ 243
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPR 267
|
....*.
gi 343398708 244 FEDYDE 249
Cdd:PRK09473 268 LDAEGE 273
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-218 |
1.45e-37 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 140.32 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIY---DNGF-KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFID-GKDIVKMNSKELK 75
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 E---ARKNMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLlEYVNLKEKIYE-----YPANLSGGQKQRVA 147
Cdd:TIGR03269 359 GrgrAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITL-KMVGFDEEKAEeildkYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 148 IARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-199 |
3.01e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 133.83 E-value: 3.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVT---NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkea 77
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPalqDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 rknmAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQME 199
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
3.19e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 134.55 E-value: 3.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNskeLKEARKN 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQ-SFNLFYQKNVFENIAY-PLRINkWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKI 158
Cdd:PRK13652 80 VGLVFQnPDDQIFSPTVEQDIAFgPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
3.48e-37 |
|
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: 132.40 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdivkmnsKELKEARKNM 81
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-------PLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-229 |
3.69e-37 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 136.40 E-value: 3.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSK-ELKEARKNMAMIFQSFNLFYQKNVFEN 99
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRINKWKKKDI-EERVNTLLeyvNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILE 178
Cdd:TIGR02142 96 LRYGMKRARPSERRIsFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 343398708 179 LLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-221 |
4.68e-37 |
|
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: 139.47 E-value: 4.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIY-DNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNskeLKEARKN 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyQKNVFENIAYPlRINKWKKKDIEE--RVNTLLEYVN-----LKEKIYEYPANLSGGQKQRVAIARALA 153
Cdd:TIGR02203 408 VALVSQDVVLF-NDTIANNIAYG-RTEQADRAEIERalAAAYAQDFVDklplgLDTPIGENGVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 154 VQPKILLCDEATSALDPQSTKSI---LELLLKIRdefnlTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVqaaLERLMQGR-----TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGT 550
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-243 |
7.35e-37 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 138.68 E-value: 7.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKS----SLIRCinrLEEP----TQGNIFIDGKDIVKMNSKELKEARKN-MAMIFQ-- 86
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvtalSILRL---LPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNkIAMIFQep 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 87 --SFNLFYqkNVFENIAYPLRINKWKKKDiEERVNTL--LEYV---NLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:PRK15134 102 mvSLNPLH--TLEKQLYEVLSLHRGMRRE-AARGEILncLDRVgirQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIE 239
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLN 258
|
....
gi 343398708 240 TLPQ 243
Cdd:PRK15134 259 SEPS 262
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-217 |
9.28e-37 |
|
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: 131.56 E-value: 9.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNLFYQKn 95
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVTLFYGT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 96 VFENIAYPLRINKwkKKDIEE--RVNTLLEYVNLKEKIYEYP-----ANLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:cd03245 94 LRDNITLGAPLAD--DERILRaaELAGVTDFVNKHPNGLDLQigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 343398708 169 DPQSTKSILELLLK-IRDEfnlTIVLITHQMEVVkAICDRAAVIENGEII 217
Cdd:cd03245 172 DMNSEERLKERLRQlLGDK---TLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-207 |
1.56e-36 |
|
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: 131.02 E-value: 1.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYD----NG--FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGK----DIVKMN 70
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 71 SKELKEARKNmAMIFQSfnlfyQknvF----------ENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYE-YPANLS 139
Cdd:COG4778 84 PREILALRRR-TIGYVS-----Q---FlrviprvsalDVVAEPLLERGVDREEARARARELLARLNLPERLWDlPPATFS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 140 GGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDR 207
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADR 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-221 |
2.06e-36 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 130.72 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKNMAMIFQSFNLFYQKNVFEN 99
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER--ARAGIAYVPQGREIFPRLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRINKWKKKDIEERVNTLLEYvnLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILEL 179
Cdd:TIGR03410 96 LLTGLAALPRRSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343398708 180 LLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:TIGR03410 174 IRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-230 |
9.18e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 130.72 E-value: 9.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGF----KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIV-KMNSKELKE 76
Cdd:PRK13641 3 IKFENVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQ-SFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEY-PANLSGGQKQRVAIARALAV 154
Cdd:PRK13641 83 LRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKsPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-229 |
9.45e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 130.69 E-value: 9.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGN---IFIDGkdiVKMNSKELKEARKNMAMIFQS-FNLFY 92
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG---ITLTAKTVWDIREKVGIVFQNpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 QKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQS 172
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 173 TKSILELLLKIRDEFNLTIVLITHQMEVVkAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-230 |
9.48e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 130.67 E-value: 9.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG----FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIV-KMNSKELKE 76
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQ--SFNLFyQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEY-PANLSGGQKQRVAIARALA 153
Cdd:PRK13646 83 VRKRIGMVFQfpESQLF-EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 154 VQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPK 230
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-238 |
2.14e-35 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 129.52 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKI--YDNGF------KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdivKMNSK 72
Cdd:PRK15112 4 LLEVRNLSKTfrYRTGWfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 73 ELKEARKNMAMIFQ--SFNLFYQKNVFENIAYPLRIN-KWKKKDIEERVNTLLEYVNLK-EKIYEYPANLSGGQKQRVAI 148
Cdd:PRK15112 81 DYSYRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 149 ARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTS 228
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250
....*....|
gi 343398708 229 PKTATTKKFI 238
Cdd:PRK15112 241 PLHELTKRLI 250
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-244 |
3.28e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 130.25 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKS-SLIRCINRLEEP---TQGNIFIDGKDIVKMNSKELKE-ARKNMAMIFQ--- 86
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNlVGAEVAMIFQdpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 87 -SFNLFYqkNVFENIAYPLRINKW-KKKDIEERVNTLLEYVNLKE---KIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:PRK11022 100 tSLNPCY--TVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIETL 241
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRAL 257
|
...
gi 343398708 242 PQF 244
Cdd:PRK11022 258 PEF 260
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-217 |
4.92e-35 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 134.47 E-value: 4.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVT---NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA 77
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEvlkGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RK-NMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQP 156
Cdd:PRK10535 84 RReHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 157 KILLCDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVkAICDRAAVIENGEII 217
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
9.37e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 128.67 E-value: 9.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG----FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNI---FIDGKDIVKMNSKE- 73
Cdd:PRK13651 3 IKVKNIVKIFNKKlpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 74 -----------------LKEARKNMAMIFQ--SFNLFYQkNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYE- 133
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 134 YPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIEN 213
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....
gi 343398708 214 GEII 217
Cdd:PRK13651 241 GKII 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
2.00e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.79 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 5 ENLVKIYDNGFK-------AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEA 77
Cdd:PRK13648 5 NSIIVFKNVSFQyqsdasfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQP 156
Cdd:PRK13648 82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 157 KILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQM-EVVKAicDRAAVIENGEIIEQDTVLKLFTSPKTATT 234
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLsEAMEA--DHVIVMNKGTVYKEGTPTEIFDHAEELTR 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-218 |
3.18e-34 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 131.68 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKNMAMIFQSFNLFyQKNV 96
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQVALVSQNVHLF-NDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 97 FENIAYPlRINKWKKKDIEE--RVNTLLEYVNLKEK-----IYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:PRK11176 434 ANNIAYA-RTEQYSREQIEEaaRMAYAMDFINKMDNgldtvIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 343398708 170 PQSTKSI---LELLLKirdefNLTIVLITHQMEVV-KAicDRAAVIENGEIIE 218
Cdd:PRK11176 513 TESERAIqaaLDELQK-----NRTSLVIAHRLSTIeKA--DEILVVEDGEIVE 558
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-241 |
3.44e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 126.36 E-value: 3.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 30 IFGIIGMSGAGKSSLIRCINRLEEPTQG-----NIFIDGKDIvkMNSKELKEARKNMAMIFQSFNLFyQKNVFENIAYPL 104
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPF-PMSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 105 RINKW-KKKDIEERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILEL 179
Cdd:PRK14271 126 RAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 180 LLKIRDEfnLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKFIETL 241
Cdd:PRK14271 206 IRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-218 |
4.10e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.13 E-value: 4.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVkIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCIN-RLEEP--TQGNIFIDGKDIvkmnsKELKEA 77
Cdd:COG4136 1 MLSLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRL-----TALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNVFENIAYPLRiNKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHqmevvkaicDRAAVIENGEIIE 218
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH---------DEEDAPAAGRVLD 205
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-295 |
4.67e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 127.13 E-value: 4.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIY-----DNGFK---------------AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIF 60
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLKgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 61 IDGKDIVKmNSKELKearKNMAMIF-------------QSFNLFyqKNVFeniayplRINKwkkKDIEERVNTLLEYVNL 127
Cdd:COG4586 81 VLGYVPFK-RRKEFA---RRIGVVFgqrsqlwwdlpaiDSFRLL--KAIY-------RIPD---AEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 128 KEKIYEyPA-NLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICD 206
Cdd:COG4586 145 GELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 207 RAAVIENGEIIEQDTVLKLFT--SPKTATTKKFIETLPQFEDYDELPVADYKGCILRLGFTKETTTKPIISELIRQKNL- 283
Cdd:COG4586 224 RVIVIDHGRIIYDGSLEELKErfGPYKTIVLELAEPVPPLELPRGGEVIEREGNRVRLEVDPRESLAEVLARLLARYPVr 303
|
330
....*....|..
gi 343398708 284 DINIISGNIDKI 295
Cdd:COG4586 304 DLTIEEPPIEEV 315
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-239 |
7.41e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 125.59 E-value: 7.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYD--NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaR 78
Cdd:PRK13642 4 ILEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL---R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNMAMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPK 157
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVkAICDRAAVIENGEIIEQDTVLKLFtspktATTKKF 237
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF-----ATSEDM 234
|
..
gi 343398708 238 IE 239
Cdd:PRK13642 235 VE 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-217 |
7.47e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 125.63 E-value: 7.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGF----KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMN-SKELKE 76
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQ-SFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEY-PANLSGGQKQRVAIARALAV 154
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRdEFNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-243 |
7.98e-34 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 131.13 E-value: 7.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDG-------KDIVKMNSKELKEARK----NMAM 83
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsRQVIELSEQSAAQMRHvrgaDMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 84 IFQ----SFNLFYqkNVFENIAYPLRINKWKKKDIEER-VNTLLEYVNLKEK---IYEYPANLSGGQKQRVAIARALAVQ 155
Cdd:PRK10261 109 IFQepmtSLNPVF--TVGEQIAESIRLHQGASREEAMVeAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 156 PKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTK 235
Cdd:PRK10261 187 PAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTR 266
|
....*...
gi 343398708 236 KFIETLPQ 243
Cdd:PRK10261 267 ALLAAVPQ 274
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-238 |
1.49e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 125.73 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYD----NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNI----FIDGKDIVKMNS- 71
Cdd:PRK13631 21 ILRVKNLYCVFDekqeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 72 --------KELKEARKNMAMIFQ--SFNLFyQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEY-PANLSG 140
Cdd:PRK13631 101 tnpyskkiKNFKELRRRVSMVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERsPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 141 GQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQD 220
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250
....*....|....*...
gi 343398708 221 TVLKLFTSPKTATTKKFI 238
Cdd:PRK13631 259 TPYEIFTDQHIINSTSIQ 276
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-244 |
5.23e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 124.63 E-value: 5.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEP----TQGNIFIDGKDIVKMNSKELKE-ARKNMAMIFQ--- 86
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKiIGREIAMIFQeps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 87 -----SFNLFYQknVFENIAYPLRINKW--KKKDIEERVNTLLEYVNLK--EKIYE-YPANLSGGQKQRVAIARALAVQP 156
Cdd:COG4170 100 scldpSAKIGDQ--LIEAIPSWTFKGKWwqRFKWRKKRAIELLHRVGIKdhKDIMNsYPHELTEGECQKVMIAMAIANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 157 KILLCDEATSALDPqSTKS-ILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTK 235
Cdd:COG4170 178 RLLIADEPTNAMES-TTQAqIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTK 256
|
....*....
gi 343398708 236 KFIETLPQF 244
Cdd:COG4170 257 ALLRSMPDF 265
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-226 |
5.79e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 123.69 E-value: 5.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIY--DNGF--KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIdGKDIVKMNSK--EL 74
Cdd:PRK13643 1 MIKFEKVNYTYqpNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKqkEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 75 KEARKNMAMIFQ-SFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYE-YPANLSGGQKQRVAIARAL 152
Cdd:PRK13643 80 KPVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEkSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 153 AVQPKILLCDEATSALDPQSTKSILELLLKIRdEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLF 226
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
5.88e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.92 E-value: 5.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQS-FNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:PRK13647 82 GLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 161 CDEATSALDPQSTKSILELLlkirDEFN---LTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEIL----DRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
8.80e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 121.73 E-value: 8.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIY---------------------DNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNI 59
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 60 FIDGKdivkmnskelkearknMAMIFqSFNLFYQKN--VFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEyPA- 136
Cdd:COG1134 84 EVNGR----------------VSALL-ELGAGFHPEltGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PVk 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 137 NLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*.
gi 343398708 217 IEQDTV 222
Cdd:COG1134 225 VMDGDP 230
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-221 |
1.12e-32 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 128.15 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYD-NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:TIGR03797 452 IEVDRVTFRYRpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV---RRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyQKNVFENIA--YPLRInkwkkkdieERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVA 147
Cdd:TIGR03797 529 LGVVLQNGRLM-SGSIFENIAggAPLTL---------DEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLL 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 148 IARALAVQPKILLCDEATSALDPQSTKSILELLlkirDEFNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESL----ERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-216 |
2.09e-32 |
|
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: 118.69 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA--------RKNMAmifqs 87
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 88 fnLFYQKNVFENIAYPLRinkwkkkdieervntlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:cd03215 89 --LVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 343398708 168 LDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:cd03215 135 VDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-221 |
2.83e-32 |
|
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: 119.44 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIY-DNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnskELKEARKN 80
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyqknvfeniAYPLRINkwkkKDIEERVNTLLEYVNLkeKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03369 84 LTIIPQDPTLF---------SGTIRSN----LDPFDEYSDEEIYGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 161 CDEATSALDPQSTKSILELllkIRDEF-NLTIVLITHQMEVVkAICDRAAVIENGEIIEQDT 221
Cdd:cd03369 149 LDEATASIDYATDALIQKT---IREEFtNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDH 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
11-221 |
7.18e-32 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 125.07 E-value: 7.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 11 YDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNL 90
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRNIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 91 FyQKNVFENIayplRINKWKKKDIE-----ERVNTlLEYVNLKEKIY-----EYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:PRK13657 421 F-NRSIEDNI----RVGRPDATDEEmraaaERAQA-HDFIERKPDGYdtvvgERGRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 161 CDEATSALDPQS---TKSILELLLKIRDEFnltivLITHQMEVVKAiCDRAAVIENGEIIEQDT 221
Cdd:PRK13657 495 LDEATSALDVETeakVKAALDELMKGRTTF-----IIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
7.90e-32 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 117.97 E-value: 7.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnSKELKEARKN 80
Cdd:COG4133 2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRInkWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAAL--YGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQ 197
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
1.72e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.65 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkearkn 80
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 mAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQME 199
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIE 190
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
1.72e-31 |
|
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: 123.55 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQkNVFENIAypLRINKWKKKDIEERVNT--LLEYVN-----LKEKIYEYPANLSGGQKQRVAIARALAV 154
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIR--LARPDASDAEIREALERagLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVkAICDR 207
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADR 525
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-216 |
1.75e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.96 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRL---EEPTQGNIFIDGKDIVKMN--SKELK 75
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 EARKNMAMIFQSFNLFYQKNVFENI------AYPL--RINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVA 147
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVligalgSTPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 148 IARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-229 |
4.14e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 123.68 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNLFyQKNVFEN 99
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL---HRQVALVGQEPVLF-SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRinkwkKKDIEERVNTLLE-----YVNLKEKIY-----EYPANLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:TIGR00958 575 IAYGLT-----DTPDEEIMAAAKAanahdFIMEFPNGYdtevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 170 PQSTKSILELllkiRDEFNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:TIGR00958 650 AECEQLLQES----RSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-218 |
9.12e-31 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 115.71 E-value: 9.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnskelkearknmAMIFqsFNLFYQK 94
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS---------------SLLG--LGGGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 95 N--VFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDP-- 170
Cdd:cd03220 98 EltGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAaf 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 343398708 171 --QSTKSILELLLKIRdefnlTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:cd03220 178 qeKCQRRLRELLKQGK-----TVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
1.37e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 118.39 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYdnGFKAVTN-INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnSKELKEARKN 80
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNgLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:PRK13536 116 IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 161 CDEATSALDPQSTKSILELL--LKIRDEfnlTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLrsLLARGK---TILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-221 |
5.45e-30 |
|
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: 119.92 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNLFyqkN--VF 97
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDTVLF---NdtIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 98 ENIAYPlRINKwKKKDIEE--RVNTLLEYVN--------------LKekiyeypanLSGGQKQRVAIARALAVQPKILLC 161
Cdd:COG5265 450 YNIAYG-RPDA-SEEEVEAaaRAAQIHDFIEslpdgydtrvgergLK---------LSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDefNLTIVLITHQME-VVKAicDRAAVIENGEIIEQDT 221
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLStIVDA--DEILVLEAGRIVERGT 575
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-221 |
8.02e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 113.84 E-value: 8.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 5 ENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkEARKNMAMI 84
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 85 FQSFNLFYQKNVFENIAYPLRINK-WKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDE 163
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 164 ATSALDPQSTKSILELLLKIRDeFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
1.59e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 118.41 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIrciNRLEE--PTQGNIFIDGkdiVKMNSKELKEARK 79
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLGflPYQGSLKING---IELRELDPESWRK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQSFNLFYQkNVFENIAYplrinkwKKKDI-EERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVA 147
Cdd:PRK11174 424 HLSWVGQNPQLPHG-TLRDNVLL-------GNPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLA 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 148 IARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENGEIIEQ 219
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQ 564
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
15-228 |
4.85e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.18 E-value: 4.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIdGKDIVKMNSKELKEA---RKNMAMIFQ--SFN 89
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKIKEVkrlRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 90 LFyQKNVFENIAY-PLRINKwKKKDIEERVNTLLEYVNL-KEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:PRK13645 103 LF-QETIEKDIAFgPVNLGE-NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 168 LDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTS 228
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-216 |
4.93e-29 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 111.41 E-value: 4.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNLFyQKNVFEN 99
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL---HSKVSLVGQEPVLF-ARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLrinkwkkKDIE-ERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:cd03248 108 IAYGL-------QSCSfECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 343398708 168 LDPQSTKSILELLLKirDEFNLTIVLITHQMEVVKAiCDRAAVIENGEI 216
Cdd:cd03248 181 LDAESEQQVQQALYD--WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
4.96e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.36 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnSKELKEARKNM 81
Cdd:PRK13537 8 IDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 162 DEATSALDPQSTKSILELL--LKIRDEfnlTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLrsLLARGK---TILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-221 |
7.50e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 7.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVkiYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARk 79
Cdd:PRK13548 2 MLEARNLS--VRLGGRTLlDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 nmAMIFQSFNLFYQKNVFENIA---YPLRINKWKKKDIEERVNTLLEYVNLKEKiyEYPAnLSGGQKQRVAIARALA--- 153
Cdd:PRK13548 79 --AVLPQHSSLSFPFTVEEVVAmgrAPHGLSRAEDDALVAAALAQVDLAHLAGR--DYPQ-LSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 154 ---VQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-225 |
1.31e-28 |
|
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: 116.65 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 4 IENLVKIYD-NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnSKELKEARKNMA 82
Cdd:TIGR01257 931 VKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 MIFQSFNLFYQKNVFENIAY--PLRINKWKKKDIEerVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILL 160
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFyaQLKGRSWEEAQLE--MEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKL 225
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-229 |
2.26e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 112.28 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKE-LKEARKNMAMIFQSFNLFYQKNVFE 98
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 99 NIAYPLrinkwKKKDIEE--RVNTLLEYVNLKEKiyeYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSI 176
Cdd:PRK11144 96 NLRYGM-----AKSMVAQfdKIVALLGIEPLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 343398708 177 LELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-219 |
1.87e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.61 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIY-DNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:PRK11160 339 LTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQkNVFENiaypLRINKWKKKDieERVNTLLEYVNLkEKIYEYPA-----------NLSGGQKQRVAIA 149
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGL-EKLLEDDKglnawlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITH------QMevvkaicDRAAVIENGEIIEQ 219
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHrltgleQF-------DRICVMDNGQIIEQ 554
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-196 |
2.90e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.72 E-value: 2.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 13 NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNMAMIFQSFNLFy 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY---RQQVSYCAQTPTLF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 QKNVFENIAYPLRINKwkKKDIEERVNTLLEYVNLKEKIYEYPAN-LSGGQKQRVAIARALAVQPKILLCDEATSALDPQ 171
Cdd:PRK10247 94 GDTVYDNLIFPWQIRN--QQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180
....*....|....*....|....*
gi 343398708 172 STKSILELLLKIRDEFNLTIVLITH 196
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-221 |
5.90e-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: 5.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKN 80
Cdd:PRK11614 5 MLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIA----------YPLRInkwkkkdieERVNTLleYVNLKEKIYEYPANLSGGQKQRVAIAR 150
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAmggffaerdqFQERI---------KWVYEL--FPRLHERRIQRAGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-217 |
6.17e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 110.40 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 6 NLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEePT---QGNIFIDGKDIVKMNSKELKeaRKNMA 82
Cdd:PRK13549 10 NITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTE--RAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 MIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEE---RVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:PRK13549 86 IIHQELALVKELSVLENIFLGNEITPGGIMDYDAmylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-228 |
8.10e-27 |
|
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: 105.94 E-value: 8.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENlVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGN-IFIDGKDIVKMNSKELkeaRK 79
Cdd:COG1119 3 LLELRN-VTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWEL---RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQSFNLFYQKNV----------FENIAYPLRINKwkkkDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIA 149
Cdd:COG1119 79 RIGLVSPALQLRFPRDEtvldvvlsgfFDSIGLYREPTD----EQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQME-VVKAIcDRAAVIENGEIIEQDTVLKLFTS 228
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLKDGRVVAAGPKEEVLTS 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-217 |
1.44e-26 |
|
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: 103.78 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRCIN--RLEEPTQGNIFIDGKDIvkmnskELKEARKNMAMIFQSFNLFYQKN 95
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 96 VFENIAYPlrinkwkkkdieervntlleyVNLKekiyeypaNLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKS 175
Cdd:cd03213 99 VRETLMFA---------------------AKLR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 343398708 176 ILELLLKIRDEfNLTIVLITHQ--MEVVKAiCDRAAVIENGEII 217
Cdd:cd03213 150 VMSLLRRLADT-GRTIICSIHQpsSEIFEL-FDKLLLLSQGRVI 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.64e-26 |
|
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: 103.76 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLE--EPTQGNIFIDGKDIVKMNSKElkEARK 79
Cdd:cd03217 1 LEIKDL-HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEE--RARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQsfnlfyqknvfeniaYPLRINKWKkkdieerVNTLLEYVNlkekiyeypANLSGGQKQRVAIARALAVQPKIL 159
Cdd:cd03217 78 GIFLAFQ---------------YPPEIPGVK-------NADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAI-CDRAAVIENGEIIE 218
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-244 |
2.04e-26 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 106.81 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLV---KIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLeepTQGNIFI-------DGKDIVKMN 70
Cdd:PRK15093 3 LLDIRNLTiefKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVtadrmrfDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 71 SKEL-KEARKNMAMIFQ--------SFNLFYQknVFENIA-------YPLRINKWKKKDIEervntLLEYVNLKEK---I 131
Cdd:PRK15093 80 PRERrKLVGHNVSMIFQepqscldpSERVGRQ--LMQNIPgwtykgrWWQRFGWRKRRAIE-----LLHRVGIKDHkdaM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 132 YEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVI 211
Cdd:PRK15093 153 RSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
250 260 270
....*....|....*....|....*....|...
gi 343398708 212 ENGEIIEQDTVLKLFTSPKTATTKKFIETLPQF 244
Cdd:PRK15093 233 YCGQTVETAPSKELVTTPHHPYTQALIRAIPDF 265
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-219 |
2.40e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.78 E-value: 2.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 12 DNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnSKELKEARKNMAMIFQSFNLF 91
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV----SDLEKALSSLISVLNQRPYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 yqknvfeniayplrinkwkkkdieerVNTLLEyvNLKEKiyeypanLSGGQKQRVAIARALAVQPKILLCDEATSALDPQ 171
Cdd:cd03247 88 --------------------------DTTLRN--NLGRR-------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 343398708 172 STKSILELLLKIRDefNLTIVLITHQMEVVKAIcDRAAVIENGEIIEQ 219
Cdd:cd03247 133 TERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-214 |
4.74e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.95 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYdNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKElkEARKN 80
Cdd:PRK09700 5 YISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL--AAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENI---AYPLR----INKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALA 153
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 154 VQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENG 214
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-220 |
5.20e-26 |
|
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: 103.57 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYD-----NGFK---------------AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFI 61
Cdd:cd03267 1 IEVSNLSKSYRvyskePGLIgslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 62 DGKDivkmNSKELKEARKNMAMIF-QSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSG 140
Cdd:cd03267 81 AGLV----PWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 141 GQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQD 220
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-241 |
2.22e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 102.76 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKnMAMIFQSFNLFYQKNVFEN 99
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV--ARR-IGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IA---YPLR--INKWKKKDiEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTK 174
Cdd:PRK10253 102 VArgrYPHQplFTRWRKED-EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 175 SILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDtvlklftSPKTATTKKFIETL 241
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG-------APKEIVTAELIERI 240
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-225 |
2.94e-25 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 106.36 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFyQKNVFENIayplrINKWKKKDIEERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIAR 150
Cdd:TIGR01193 551 NYLPQEPYIF-SGSILENL-----LLGAKENVSQDEIWAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 151 ALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfnlTIVLITHQMEVVKAIcDRAAVIENGEIIEQDTVLKL 225
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDEL 695
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-215 |
3.11e-25 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 100.62 E-value: 3.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNG----FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCInrLEE--PTQGNIFIDGKdivkmnskelk 75
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEleKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 earknMAMIFQS---FNLfyqkNVFENIAYPLRINkwkkkdiEERVNTLLEYVNLKEKIYEYPA-----------NLSGG 141
Cdd:cd03250 68 -----IAYVSQEpwiQNG----TIRENILFGKPFD-------EERYEKVIKACALEPDLEILPDgdlteigekgiNLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 142 QKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAiCDRAAVIENGE 215
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
18-235 |
3.40e-25 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 101.70 E-value: 3.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSslIRCINRLE------EPTQGNIFIDGKDIVkmnSKELKEarKNMAMIFQ----S 87
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVA---PCALRG--RKIATIMQnprsA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 88 FNlfyqknvfeniayPLR------INKWKKKDIEERVNTL---LEYVNLKE--KIYE-YPANLSGGQKQRVAIARALAVQ 155
Cdd:PRK10418 92 FN-------------PLHtmhthaRETCLALGKPADDATLtaaLEAVGLENaaRVLKlYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 156 PKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTK 235
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTR 238
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-217 |
4.30e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.11 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 3 KIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA----- 77
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 ---RKNMAMIfQSFnlfyqkNVFENIA----YPLRINKW---KKKDIEERVNTLLEYVNLKEKIYEYPA-NLSGGQKQRV 146
Cdd:COG3845 339 pedRLGRGLV-PDM------SVAENLIlgryRRPPFSRGgflDRKAIRAFAEELIEEFDVRTPGPDTPArSLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 147 AIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-223 |
5.65e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEARKN 80
Cdd:PRK11701 6 LLSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMifQSFNLFYQKNVFE----------NIAYPLRINKWKK-KDIEERVNTLLEYVNL-KEKIYEYPANLSGGQKQRVAI 148
Cdd:PRK11701 85 RLL--RTEWGFVHQHPRDglrmqvsaggNIGERLMAVGARHyGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 149 ARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQ---DTVL 223
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESgltDQVL 240
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-222 |
9.06e-25 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 99.78 E-value: 9.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDivkMNSKELKearkNM 81
Cdd:TIGR03740 1 LETKNLSKRFGKQ-TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHP---WTRKDLH----KI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVFENiaypLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:TIGR03740 73 GSLIESPPLYENLTAREN----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTV 222
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-235 |
9.71e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 105.21 E-value: 9.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTN-INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNskeLKEARKN 80
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHgLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFeNIAyPLriNKWKKKDIEERvntlLEYVNLKEKI-----------YEYPANLSGGQKQRVAIA 149
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRF-NLD-PF--NEHNDADLWES----LERAHLKDVIrrnslgldaevSEAGENFSVGQRQLLSLA 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILElllKIRDEF-NLTIVLITHQMEVVkaI-CDRAAVIENGEIIEQDTVLKLFT 227
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDVRTDALIQK---TIREEFkSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLS 1461
|
....*...
gi 343398708 228 SPKTATTK 235
Cdd:PLN03130 1462 NEGSAFSK 1469
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-232 |
1.12e-24 |
|
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: 104.44 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKN 80
Cdd:COG4618 331 LSVENLTVVPPGSKRPIlRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyqkN--VFENIAyplR---------INKWKKKDIEERVNTLleyvnlkEKIYEYP-----ANLSGGQKQ 144
Cdd:COG4618 408 IGYLPQDVELF---DgtIAENIA---RfgdadpekvVAAAKLAGVHEMILRL-------PDGYDTRigeggARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 145 RVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVkAICDRAAVIENGEII---EQDT 221
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRDGRVQafgPRDE 552
|
250
....*....|.
gi 343398708 222 VLKLFTSPKTA 232
Cdd:COG4618 553 VLARLARPAAA 563
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-229 |
1.16e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 100.19 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENL-VKIydNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARK 79
Cdd:COG4559 1 MLEAENLsVRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--ARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 nMAMIFQSFNLFYQKNVFENIA---YPLRINKWKKKDIEERVNTLLEYVNLKEKIYeypANLSGGQKQRVAIARALA--- 153
Cdd:COG4559 77 -RAVLPQHSSLAFPFTVEEVVAlgrAPHGSSAAQDRQIVREALALVGLAHLAGRSY---QTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 154 ----VQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-225 |
1.39e-24 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 103.66 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 14 GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKN-MAMIFQSFNLFY 92
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI---DFKSSKEALENgISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 QKNVFENI---AYPLR---INKWKK-KDIEERVNTLLEYVNLKEKIyeypANLSGGQKQRVAIARALAVQPKILLCDEAT 165
Cdd:PRK10982 87 QRSVMDNMwlgRYPTKgmfVDQDKMyRDTKAIFDELDIDIDPRAKV----ATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 166 SALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKL 225
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
5.00e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 102.44 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFyQKNVFENiaypLRINKwkkKDI-EERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIA 149
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVREN----LRLAR---PDAtDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfnLTIVLITHQ 197
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-218 |
7.77e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.53 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 14 GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEArkNMAMIFQSFNLFYQ 93
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA--GVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 94 KNVFENI---AYPLRINKWKKKDIEERVNTLLEyvNLKEKI-YEYP-ANLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:PRK11288 94 MTVAENLylgQLPHKGGIVNRRLLNYEAREQLE--HLGVDIdPDTPlKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 343398708 169 DPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:PRK11288 172 SAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-233 |
8.23e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 8.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDiVKMNSkeLKEARKN-MAMI---FQSFNLF 91
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP-VRIRS--PRDAIRAgIAYVpedRKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 YQKNVFENIAYPL--RINKW---KKKDIEERVNTLLEYVNLKEKIYEYPA-NLSGGQKQRVAIARALAVQPKILLCDEAT 165
Cdd:COG1129 343 LDLSIRENITLASldRLSRGgllDRRRERALAEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 166 SALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI--------IEQDTVLKLFTSPKTAT 233
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIvgeldreeATEEAIMAAATGGAAAA 497
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-221 |
2.02e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKn 80
Cdd:PRK11231 2 TLRTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL--ARR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFYQKNVFENIAY---PLrINKWKK--KDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQ 155
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYgrsPW-LSLWGRlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 156 PKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-221 |
2.59e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.56 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeaRKNM 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSfNLFYQKNVFENIAYplrinkwkKKDI-EERVNTLLEYVNLKEKIYEYPA-----------NLSGGQKQRVAIA 149
Cdd:PRK10790 418 AMVQQD-PVVLADTFLANVTL--------GRDIsEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 150 RALAVQPKILLCDEATSALDPQSTKSILELLLKIRDefNLTIVLITHQME-VVKAicDRAAVIENGEIIEQDT 221
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStIVEA--DTILVLHRGQAVEQGT 557
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-219 |
4.58e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 4.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvKMNSKELKEARKNMAMIFQSFN--LFYQkNVFE 98
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPEqqIFYT-DIDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 99 NIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILE 178
Cdd:PRK13638 98 DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 343398708 179 LLLKIRDEFNlTIVLITHQMEVVKAICDRAAVIENGEIIEQ 219
Cdd:PRK13638 178 IIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-218 |
5.47e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIdGKDiVKM-----NSKELK 75
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GET-VKIgyfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 76 EarknmamifqsfnlfyQKNVFENIAyplrinKWKKKDIEERVNTLLEYVNLK-EKIYEYPANLSGGQKQRVAIARALAV 154
Cdd:COG0488 392 P----------------DKTVLDELR------DGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 155 QPKILLCDEATSALDPQsTKSILELLLkirDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:COG0488 450 PPNVLLLDEPTNHLDIE-TLEALEEAL---DDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-247 |
7.03e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 99.67 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTN-INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNskeLKEARK 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPPVLHgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQSFNLFYQKNVFeNIAYPLRINK---WKK------KDIEERvntllEYVNLKEKIYEYPANLSGGQKQRVAIAR 150
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRF-NIDPFSEHNDadlWEAlerahiKDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSLAR 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 151 ALAVQPKILLCDEATSALDPQsTKSILEllLKIRDEF-NLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVR-TDSLIQ--RTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
250
....*....|....*...
gi 343398708 230 KTATTKKFIETLPQFEDY 247
Cdd:PLN03232 1461 TSAFFRMVHSTGPANAQY 1478
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-217 |
7.84e-23 |
|
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: 98.74 E-value: 7.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEE--PTQGNIFIDGKDIVKMNSKELKeaR 78
Cdd:TIGR02633 1 LLEMKGIVKTFG-GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTE--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNMAMIFQSFNLFYQKNVFENI-------------AYPLRINkwkkkdieeRVNTLLEYVNLKEKIYEYP-ANLSGGQKQ 144
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIflgneitlpggrmAYNAMYL---------RAKNLLRELQLDADNVTRPvGDYGGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 145 RVAIARALAVQPKILLCDEATSALDPQSTKSILELllkIRD--EFNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTEKETEILLDI---IRDlkAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-221 |
4.70e-22 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 97.32 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNskeLKEARKNMAMIFQSFNLFyqknvfen 99
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDPVLF-------- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 iAYPLRIN-KWKKKDIEERVNTLLEYVNLKEKIYEYPA-----------NLSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:TIGR00957 1373 -SGSLRMNlDPFSQYSDEEVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 168 LDPQSTKSILElllKIRDEF-NLTIVLITHQMevvKAICD--RAAVIENGEIIEQDT 221
Cdd:TIGR00957 1452 VDLETDNLIQS---TIRTQFeDCTVLTIAHRL---NTIMDytRVIVLDKGEVAEFGA 1502
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-216 |
7.06e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 7.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVkIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKN 80
Cdd:PRK09536 3 MIDVSDLS-VEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV---EALSARAASRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQ----SFNlFYQKNVFENIAYP--LRINKWKKKDiEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAV 154
Cdd:PRK09536 79 VASVPQdtslSFE-FDVRQVVEMGRTPhrSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-229 |
7.11e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.93 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkeARKnMAMIFQSFNLFYQKNVFENI 100
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAF--ARK-VAYLPQQLPAAEGMTVRELV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 101 A---YPLR--INKWKKKDiEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKS 175
Cdd:PRK10575 107 AigrYPWHgaLGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 343398708 176 ILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-217 |
9.05e-22 |
|
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: 91.95 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEEP--TQGNIFIDGKDIVKmnskelKEARKNMAMIFQSFNLFY 92
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPRKP------DQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 QKNVFENIAYPLRI---NKWKKKDIEERV-NTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:cd03234 95 GLTVRETLTYTAILrlpRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 343398708 169 DPQSTKSILELLLKIRDEfNLTIVLITHQ--MEVVKaICDRAAVIENGEII 217
Cdd:cd03234 175 DSFTALNLVSTLSQLARR-NRIVILTIHQprSDLFR-LFDRILLLSSGEIV 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-204 |
2.63e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.40 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDivkmnskelkearknmamifqsfNLFYQK-NVFE 98
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPD-----------------------NQFGREaSLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 99 NIayplrinkWKKKDIEERVNtLLEYVNLKEkIYEY---PANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKS 175
Cdd:COG2401 105 AI--------GRKGDFKDAVE-LLNAVGLSD-AVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|....*....
gi 343398708 176 ILELLLKIRDEFNLTIVLITHQMEVVKAI 204
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHHYDVIDDL 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-217 |
6.26e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 4 IENLVKIYDnGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGK------------------- 64
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqeppldddltvl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 65 DIVKMNSKELKEARKNM-----AMIFQSFNLFYQKNVFENIAyplRINKWkkkDIEERVNTLLEYVNLKEKIYEYP-ANL 138
Cdd:COG0488 80 DTVLDGDAELRALEAELeeleaKLAEPDEDLERLAELQEEFE---ALGGW---EAEARAEEILSGLGFPEEDLDRPvSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 139 SGGQKQRVAIARALAVQPKILLCDEATSALDpqsTKSI--LELLLKirdEFNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIewLEEFLK---NYPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
.
gi 343398708 217 I 217
Cdd:COG0488 228 T 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-226 |
1.26e-20 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 89.58 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnskELKEARKN 80
Cdd:cd03288 20 IKIHDLCVRYENNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL---PLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyqknvfeniAYPLRIN-KWKKKDIEERVNTLLEYVNLKEKIYEYPA-----------NLSGGQKQRVAI 148
Cdd:cd03288 97 LSIILQDPILF---------SGSIRFNlDPECKCTDDRLWEALEIAQLKNMVKSLPGgldavvteggeNFSVGQRQLFCL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 149 ARALAVQPKILLCDEATSALDpQSTKSILE--LLLKIRDEfnlTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVLKLF 226
Cdd:cd03288 168 ARAFVRKSSILIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
12-218 |
1.45e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 92.34 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 12 DNGFkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKNMAMIFQSFNLF 91
Cdd:PRK10522 334 DNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLFSAVFTDFHLF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 YQknvfeniayplRINKWKKKDIEERVNTLLEYVNLKEKIYE-----YPANLSGGQKQRVAIARALAVQPKILLCDEATS 166
Cdd:PRK10522 410 DQ-----------LLGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAA 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 343398708 167 ALDPQSTKSILELLLKIRDEFNLTIVLITH-QMEVVKAicDRAAVIENGEIIE 218
Cdd:PRK10522 479 DQDPHFRREFYQVLLPLLQEMGKTIFAISHdDHYFIHA--DRLLEMRNGQLSE 529
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-229 |
2.23e-20 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 91.70 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnskELKEARKNMAMIFQSFNLFyQKNV 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLF-SDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 97 FENIAypLRINKWKKKDIEErVNTLleyVNLKEKIYEYPAN-----------LSGGQKQRVAIARALAVQPKILLCDEAT 165
Cdd:PRK10789 406 ANNIA--LGRPDATQQEIEH-VARL---ASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 166 SALDPQSTKSILELLLKIRDEfnLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVLKLFTSP 229
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| NIL |
smart00930 |
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ... |
257-330 |
2.37e-20 |
|
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 197998 [Multi-domain] Cd Length: 76 Bit Score: 83.33 E-value: 2.37e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 257 GCILRLGFTKETTTKPIISELIRQKNLDINIISGNIDKIKEGKVGHLIVEIF-EKDRVDEIKNFLEDKKVLVEEV 330
Cdd:smart00930 2 GRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTgDEEDIEAALAYLREQGVEVEVL 76
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
18-197 |
5.07e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFI-DGKDIV------KMNSKELKEArknmamifqsfnl 90
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLflpqrpYLPLGTLREA------------- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 91 fyqknvfenIAYPLRINKWKkkdiEERVNTLLEYVNL---KEKIYE---YPANLSGGQKQRVAIARALAVQPKILLCDEA 164
Cdd:COG4178 446 ---------LLYPATAEAFS----DAELREALEAVGLghlAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|....
gi 343398708 165 TSALDPQSTKSILELLlkiRDEF-NLTIVLITHQ 197
Cdd:COG4178 513 TSALDEENEAALYQLL---REELpGTTVISVGHR 543
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-197 |
6.65e-20 |
|
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: 84.90 E-value: 6.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIfidgkdivkmnskeLKEARKNM 81
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------GMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSfNLFYQKNVFENIAYPlrinkWKKKdieervntlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03223 67 LFLPQR-PYLPLGTLREQLIYP-----WDDV-------------------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....*.
gi 343398708 162 DEATSALDPQSTKSILELLlkirDEFNLTIVLITHQ 197
Cdd:cd03223 116 DEATSALDEESEDRLYQLL----KELGITVISVGHR 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-239 |
1.40e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 89.70 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRcinrleePTQGNIFIDGKDIVKMNSKELKearkNMAMIFQSFNLFYQKNVFEN 99
Cdd:PTZ00265 1247 EQNVGMKNVNEFSLTKEGGSGEDSTVF-------KNSGKILLDGVDICDYNLKDLR----NLFSIVSQEPMLFNMSIYEN 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPlrinkwKKKDIEERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:PTZ00265 1316 IKFG------KEDATREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 169 DPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAiCDRAAVIEN----GEIIEQDTVLKLFTSPKTATTKKFIE 239
Cdd:PTZ00265 1390 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAHGTHEELLSVQDGVYKKYVK 1463
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-225 |
1.62e-19 |
|
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: 86.83 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENL-VKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEpTQGNIFIDGkdiVKMNSKELKEARKN 80
Cdd:cd03289 3 MTVKDLtAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG---VSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyqknvfeniAYPLRIN-----KWKkkdiEERVNTLLEYVNLKEKIYEYPANL-----------SGGQKQ 144
Cdd:cd03289 79 FGVIPQKVFIF---------SGTFRKNldpygKWS----DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 145 RVAIARALAVQPKILLCDEATSALDPQSTKSILELLlkiRDEF-NLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVL 223
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL---KQAFaDCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQ 221
|
..
gi 343398708 224 KL 225
Cdd:cd03289 222 KL 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-212 |
2.30e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELkearknM 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL------V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSFNLFYQKNVF-ENIAYPLR------INKWKKKDiEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAV 154
Cdd:PRK15056 81 AYVPQSEEVDWSFPVLvEDVVMMGRyghmgwLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIE 212
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
15-221 |
5.33e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 5.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGN--IF---IDGKDIvkmnskelkEARKNMAMIFQSFN 89
Cdd:NF033858 279 FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawLFgqpVDAGDI---------ATRRRVGYMSQAFS 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 90 LFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 343398708 170 PQSTKSILELLLKIRDEFNLTIVLITHQM-EVvkAICDRAAVIENGEIIEQDT 221
Cdd:NF033858 430 PVARDMFWRLLIELSREDGVTIFISTHFMnEA--ERCDRISLMHAGRVLASDT 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-225 |
1.46e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKE--------LKEARKNMAMIFQsfn 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 90 lfyqKNVFENI---AYPLRINKW---KKKDIEERVNTLLEYVNLKEKIYEYP-ANLSGGQKQRVAIARALAVQPKILLCD 162
Cdd:PRK10762 345 ----MSVKENMsltALRYFSRAGgslKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 163 EATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI-----IEQDTVLKL 225
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKL 487
|
|
| NIL |
pfam09383 |
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ... |
259-329 |
1.73e-18 |
|
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.
Pssm-ID: 462781 [Multi-domain] Cd Length: 73 Bit Score: 78.26 E-value: 1.73e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 259 ILRLGFTKETTTKPIISELIRQKNLDINIISGNIDKIKEGKVGHLIVEIF-EKDRVDEIKNFLEDKKVLVEE 329
Cdd:pfam09383 2 LVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPgDPEQIEAALAYLREQGVEVEV 73
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-222 |
1.81e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.83 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 14 GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEArkNMAMIFQSFNLFYQ 93
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA--GIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 94 KNVFENI------AYPLRINKWKKkdIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:PRK10762 94 LTIAENIflgrefVNRFGRIDWKK--MYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 168 LDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTV 222
Cdd:PRK10762 172 LTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREV 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-243 |
2.67e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 15 FKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnSKELKEARKNMAMIFQS---FNLF 91
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVKKGMAYITESrrdNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 YQKNVFENIAYP--LRINKWK------------KKDIEERVNTLLEYVNLKEKIYEypanLSGGQKQRVAIARALAVQPK 157
Cdd:PRK09700 354 PNFSIAQNMAISrsLKDGGYKgamglfhevdeqRTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 158 ILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIEqdtvlkLFTSPKTATTKKF 237
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ------ILTNRDDMSEEEI 502
|
....*..
gi 343398708 238 IE-TLPQ 243
Cdd:PRK09700 503 MAwALPQ 509
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-215 |
3.32e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.80 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGfKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIfidgkdivkmnskelkearknm 81
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 amifqsfnlfyqknvfeniayplrinKWKKKdieervntlleyvnlkEKIYeYPANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:cd03221 58 --------------------------TWGST----------------VKIG-YFEQLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 343398708 162 DEATSALDPQStKSILELLLKirdEFNLTIVLITHQMEVVKAICDRAAVIENGE 215
Cdd:cd03221 95 DEPTNHLDLES-IEALEEALK---EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-216 |
1.19e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 14 GFKavtNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKE--------LKEARknmamif 85
Cdd:PRK15439 278 GFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarglvyLPEDR------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 86 QSFNLFYQKNVFENIA------YPLRINKWKKKDIEERVNTLLeyvNLKEKIYEYPA-NLSGGQKQRVAIARALAVQPKI 158
Cdd:PRK15439 348 QSSGLYLDAPLAWNVCalthnrRGFWIKPARENAVLERYRRAL---NIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 159 LLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-206 |
2.03e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIfidgkdivkmnskeLKEARKNMAMIFQSFNLfyqkn 95
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNGKLRIGYVPQKLYL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 96 vfeNIAYPLRINKW-------KKKDIE---ERVNTlleyvnlkEKIYEYP-ANLSGGQKQRVAIARALAVQPKILLCDEA 164
Cdd:PRK09544 79 ---DTTLPLTVNRFlrlrpgtKKEDILpalKRVQA--------GHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343398708 165 TSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICD 206
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTD 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-214 |
2.39e-17 |
|
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: 83.14 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYD-NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKmnskELKEARK 79
Cdd:TIGR01257 1937 ILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 80 NMAMIFQSFNLFYQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:TIGR01257 2013 NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENG 214
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-227 |
2.83e-17 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.04 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 4 IENLVKIYDNGFKAV-TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEpTQGNIFIDGkdiVKMNSKELKEARKNMA 82
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVlQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG---VSWNSVTLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 MIFQSFNLF---YQKNVFENIAYPlrinkwkkkdiEERVNTLLEYVNLKEKIYEYPANL-----------SGGQKQRVAI 148
Cdd:TIGR01271 1296 VIPQKVFIFsgtFRKNLDPYEQWS-----------DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 149 ARALAVQPKILLCDEATSALDPqSTKSILELLLKirDEF-NLTIVLITHQMEVVKAiCDRAAVIENGEIIEQDTVLKLFT 227
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLK--QSFsNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-216 |
1.11e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSkeLKEARKNMAMIFQSFNLFYQKNVFENI 100
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP--AKAHQLGIYLVPQEPLLFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 101 AYPLRinkwKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELL 180
Cdd:PRK15439 108 LFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRI 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 343398708 181 LKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK15439 184 RELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
2-199 |
3.20e-16 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 76.22 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELK-EARKN 80
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFQSFNLFyQKNVFENIAYPLRINKWKKKDIEERVN-----TLLEYVNLKEkIYEYPANLSGGQKQRVAIARALAVQ 155
Cdd:cd03290 81 VAYAAQKPWLL-NATVEENITFGSPFNKQRYKAVTDACSlqpdiDLLPFGDQTE-IGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 343398708 156 PKILLCDEATSALDPQSTKSIL-ELLLKIRDEFNLTIVLITHQME 199
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-218 |
4.77e-16 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 78.78 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGkdivkmnskelkearkNMAMIFQSFNLFYQKNV 96
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------------SAALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 97 FENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSI 176
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343398708 177 LELLLKIRdEFNLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:PRK13545 183 LDKMNEFK-EQGKTIFFISHSLSQVKSFCTKALWLHYGQVKE 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-218 |
5.31e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.22 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLvKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCI--NRLEEPTQGNIFIDGKDIVKMNSkelkEAR 78
Cdd:CHL00131 7 ILEIKNL-HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEP----EER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 79 KNMAmIFQSFNlfYQKNV-------FENIAYPLRINKWKKKDIE-----ERVNTLLEYVNLKEKIYEYPAN--LSGGQKQ 144
Cdd:CHL00131 82 AHLG-IFLAFQ--YPIEIpgvsnadFLRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPSFLSRNVNegFSGGEKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 145 RVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVKAIC-DRAAVIENGEIIE 218
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYVHVMQNGKIIK 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-197 |
1.02e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.53 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKEL------KEARKNMAMifqsfnlfyq 93
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAMKPALT---------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 94 knVFENIAYPLRINKWKKKDIEErvntLLEYVNLKEkIYEYPA-NLSGGQKQRVAIARALAVQPKILLCDEATSALDPQS 172
Cdd:PRK13539 90 --VAENLEFWAAFLGGEELDIAA----ALEAVGLAP-LAHLPFgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*
gi 343398708 173 TKSILELLLkIRDEFNLTIVLITHQ 197
Cdd:PRK13539 163 VALFAELIR-AHLAQGGIVIAATHI 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-216 |
1.24e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEEPTQGNIFIDGKDIVKMNSkeLKEARKNMAMIFQS---FNLF 91
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNP--QQAIAQGIAMVPEDrkrDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 YQKNVFENIAYPL--RINKWKKKDIEERVNTLLEYVN-LKEKIY--EYP-ANLSGGQKQRVAIARALAVQPKILLCDEAT 165
Cdd:PRK13549 354 PVMGVGKNITLAAldRFTGGSRIDDAAELKTILESIQrLKVKTAspELAiARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 343398708 166 SALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-197 |
1.34e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEEPT--QGNIFIDGKdivKMNSKELKEarknMAMIFQSFNLFYQK-N 95
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVkgSGSVLLNGM---PIDAKEMRA----ISAYVQQDDLFIPTlT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 96 VFENIAYP--LRI-NKWKKKDIEERVNTLLEYVNLKE------KIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATS 166
Cdd:TIGR00955 116 VREHLMFQahLRMpRRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190
....*....|....*....|....*....|.
gi 343398708 167 ALDPQSTKSILELLLKIRDEfNLTIVLITHQ 197
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQK-GKTIICTIHQ 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-292 |
1.49e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.86 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 19 TNINLEIKKGEIFGIIGMSGAGKSSLIRC-INRLEEPTQGNIFIDGKdivkmnskelkearknMAMIFQSFNLFyQKNVF 97
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVVIRGT----------------VAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 98 ENIAYPLRINK---WKKKDIE--ERVNTLLEYVNLKEkIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQS 172
Cdd:PLN03130 697 DNILFGSPFDPeryERAIDVTalQHDLDLLPGGDLTE-IGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 173 TKSILELLLKirDEF-NLTIVLITHQMEVVKAIcDRAAVIENGEIIEQDTVLKLFTSPKtaTTKKFIETLPQFEDYDE-- 249
Cdd:PLN03130 776 GRQVFDKCIK--DELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNGP--LFQKLMENAGKMEEYVEen 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 343398708 250 ----------LPVADYKGCILRLGFTKETTTKPIISELIRQKNLDINIISGNI 292
Cdd:PLN03130 851 geeeddqtssKPVANGNANNLKKDSSSKKKSKEGKSVLIKQEERETGVVSWKV 903
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
12-224 |
1.51e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 75.24 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 12 DNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGkdivkmnskelkearkNMAMIFQSFNLF 91
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 YQKNVFENIAYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQ 171
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 172 STKSILELLLKIRdEFNLTIVLITHQMEVVKAICDRAAVIENG---EIIEQDTVLK 224
Cdd:PRK13546 178 FAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGklkDYGELDDVLP 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-202 |
1.91e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDgkDIVKMNSKELKEARKNMAMIFQSfNLFYQKNVFEN 99
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPL-------------------------RINKWKKK---DIEERVNTL-----------------LEYVNLKEKI--- 131
Cdd:PTZ00265 480 IKYSLyslkdlealsnyynedgndsqenknKRNSCRAKcagDLNDMSNTTdsneliemrknyqtikdSEVVDVSKKVlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 132 ---------YEY-----PANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQ 197
Cdd:PTZ00265 560 dfvsalpdkYETlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
|
....*
gi 343398708 198 MEVVK 202
Cdd:PTZ00265 640 LSTIR 644
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-218 |
5.05e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 14 GFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEePT---QGNIFIDG-----KDIvkmNSKElkeaRKNMAMIF 85
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDI---RDSE----ALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 86 QSFNLFYQKNVFENI------AYPLRINkWKKkdIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKIL 159
Cdd:NF040905 85 QELALIPYLSIAENIflgnerAKRGVID-WNE--TNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 160 LCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-216 |
1.92e-14 |
|
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: 73.71 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEEPTQGNIFIDGKDIVKMNSKE--------LKEARKNMAMIFQ 86
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQairagiamVPEDRKRHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 87 sfnLFYQKN----VFENIAYPLRINKWKKKDIeerVNTLLEYVNLKEKIYEYP-ANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:TIGR02633 354 ---LGVGKNitlsVLKSFCFKMRIDAAAELQI---IGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-234 |
3.60e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMNSKELKEA--------RKNMAMIFQSfnlfy 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpedRKAEGIIPVH----- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 qkNVFENIAYPLR---------IN-KWKKKDIEERVNTLleyvNLKEKIYEYP-ANLSGGQKQRVAIARALAVQPKILLC 161
Cdd:PRK11288 347 --SVADNINISARrhhlragclINnRWEAENADRFIRSL----NIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 162 DEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII--------EQDTVLKLfTSPKTAT 233
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAgelareqaTERQALSL-ALPRTSA 498
|
.
gi 343398708 234 T 234
Cdd:PRK11288 499 A 499
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-197 |
5.76e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 69.31 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 13 NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnSKELKEARKNMAMIFQSFNLFY 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 QKNVFENIAYPLRINKWKKKDIEErvntLLEYVNLKEkIYEYPAN-LSGGQKQRVAIARALAVQPKILLCDEATSALDPQ 171
Cdd:TIGR01189 87 ELSALENLHFWAAIHGGAQRTIED----ALAAVGLTG-FEDLPAAqLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*....
gi 343398708 172 StksiLELLLKIRDEFNLT---IVLITHQ 197
Cdd:TIGR01189 162 G----VALLAGLLRAHLARggiVLLTTHQ 186
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-197 |
1.40e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 71.32 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEePTQGNIfidgkdivkmnskeLKEARKN 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGR--------------LTKPAKG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 mamifqsfNLFY--QKNVF------ENIAYPLRINKWKKKDIEER------VNTLLEYVNLKEKIYEYPAN----LSGGQ 142
Cdd:TIGR00954 516 --------KLFYvpQRPYMtlgtlrDQIIYPDSSEDMKRRGLSDKdleqilDNVQLTHILEREGGWSAVQDwmdvLSGGE 587
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 143 KQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLlkirDEFNLTIVLITHQ 197
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSHR 638
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-197 |
1.44e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 19 TNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnsKELKEArknmamiFQSfNLFY---QKN 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----RRQRDE-------YHQ-DLLYlghQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 96 V------FENIAYPLRINKWKKkdiEERVNTLLEYVNLKEkiYEY-PAN-LSGGQKQRVAIARALAVQPKILLCDEATSA 167
Cdd:PRK13538 85 IkteltaLENLRFYQRLHGPGD---DEALWEALAQVGLAG--FEDvPVRqLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190
....*....|....*....|....*....|....
gi 343398708 168 LDPQSTKSILELLLKirdefNL----TIVLITHQ 197
Cdd:PRK13538 160 IDKQGVARLEALLAQ-----HAeqggMVILTTHQ 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-292 |
2.83e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRC-INRLEEPTQGNIFIdgkdivkmnskelkeaRKNMAMIFQS---FNLFYQ 93
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVI----------------RGSVAYVPQVswiFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 94 KNV-----FENIAYplrinkWKKKDIEERVNTL--LEYVNLKEkIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATS 166
Cdd:PLN03232 697 ENIlfgsdFESERY------WRAIDVTALQHDLdlLPGRDLTE-IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 167 ALDPQSTKSILELLLKirDEFN-LTIVLITHQMEVVKAIcDRAAVIENGEIIEQDTVLKLFTSpkTATTKKFIETLPQFE 245
Cdd:PLN03232 770 ALDAHVAHQVFDSCMK--DELKgKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS--GSLFKKLMENAGKMD 844
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 246 DYDELPVADYKgcILRLGFTKETTT-----------KPIISELIRQKNLDINIISGNI 292
Cdd:PLN03232 845 ATQEVNTNDEN--ILKLGPTVTIDVsernlgstkqgKRGRSVLVKQEERETGIISWNV 900
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-218 |
7.45e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 11 YDNGFKAVTN-INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKNMAMIFQSFN 89
Cdd:PTZ00243 1318 YREGLPLVLRgVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI---GAYGLRELRRQFSMIPQDPV 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 90 LFyQKNVFENIAYPLRINkwkkkdiEERVNTLLEYVNLKEK-----------IYEYPANLSGGQKQRVAIARALAVQ-PK 157
Cdd:PTZ00243 1395 LF-DGTVRQNVDPFLEAS-------SAEVWAALELVGLRERvasesegidsrVLEGGSNYSVGQRQLMCMARALLKKgSG 1466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 343398708 158 ILLCDEATSALDPQSTKSILElllKIRDEF-NLTIVLITHQMEVVkAICDRAAVIENGEIIE 218
Cdd:PTZ00243 1467 FILMDEATANIDPALDRQIQA---TVMSAFsAYTVITIAHRLHTV-AQYDKIIVMDHGAVAE 1524
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-227 |
7.76e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNgFKAVTNINLEIKKGEIFGIIGMSGA------------GKSSLIR-------CINRLEEPTQgnifID 62
Cdd:NF000106 14 VEVRGLVKHFGE-VKAVDGVDLDVREGTVLGVLGP*GAa**rgalpahv*GPDAGRRpwrf*twCANRRALRRT----IG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 63 GKDIVKMNSKELKEARKNMAMIFQSFNLfyqknvfeniayplrinkwKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQ 142
Cdd:NF000106 89 *HRPVR*GRRESFSGRENLYMIGR*LDL-------------------SRKDARARADELLERFSLTEAAGRAAAKYSGGM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 143 KQRVAIARALAVQPKILLCDEATSALDPQSTKSIL-ELLLKIRDefNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDT 221
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWdEVRSMVRD--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
....*.
gi 343398708 222 VLKLFT 227
Cdd:NF000106 228 VDELKT 233
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-212 |
9.35e-13 |
|
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: 67.05 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 24 EIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIV-KMNSKELKEARKNMAMIFQSFNLFYQKNVFEN-IA 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQYIKADYEGTVRDLLSSITKDFYTHPYFKTeIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 102 YPLRINKWkkkdIEERVNTlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLL 181
Cdd:cd03237 101 KPLQIEQI----LDREVPE-----------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190
....*....|....*....|....*....|.
gi 343398708 182 KIRDEFNLTIVLITHQMEVVKAICDRAAVIE 212
Cdd:cd03237 160 RFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
12-196 |
1.14e-12 |
|
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: 68.29 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 12 DNGFkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmNSKELKEARKNMAMIFQSFNLF 91
Cdd:COG4615 343 DEGF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAYRQLFSAVFSDFHLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 YQknvfeniAYPLRinkwkKKDIEERVNTLLEYVNLKEKIyeypA---------NLSGGQKQRVAIARALAVQPKILLCD 162
Cdd:COG4615 419 DR-------LLGLD-----GEADPARARELLERLELDHKV----SvedgrfsttDLSQGQRKRLALLVALLEDRPILVFD 482
|
170 180 190
....*....|....*....|....*....|....*...
gi 343398708 163 EATSALDPQsTKSI--LELL--LKIRdefNLTIVLITH 196
Cdd:COG4615 483 EWAADQDPE-FRRVfyTELLpeLKAR---GKTVIAISH 516
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-218 |
1.68e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.35 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENL-VKIYDNGFkaVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLE--EPTQGNIFIDGKDIVKMNSKElkEA 77
Cdd:PRK09580 1 MLSIKDLhVSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQ--------SFNLFYQKNVFEniayplrINKWKKKDIEERVNtLLEYVNLKEKIYEYPANL---------SG 140
Cdd:PRK09580 77 GEGIFMAFQypveipgvSNQFFLQTALNA-------VRSYRGQEPLDRFD-FQDLMEEKIALLKMPEDLltrsvnvgfSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 141 GQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAI-CDRAAVIENGEIIE 218
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIkPDYVHVLYQGRIVK 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-216 |
1.68e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 17 AVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdivKMNSKELKEARKN--------------MA 82
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGK---KINNHNANEAINHgfalvteerrstgiYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 83 MIFQSFNlfyqkNVFENI-AYPLRINKWKKKDIEERVNTLLEYVNLKEKIYEYP-ANLSGGQKQRVAIARALAVQPKILL 160
Cdd:PRK10982 340 YLDIGFN-----SLISNIrNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-196 |
3.49e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 6 NLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFI-------------------DGKDI 66
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqpgikvgylpqepqldptkTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 67 VKMNSKELKEARKNMAMIFQSFN--------LFYQKNVFENIayplrINKWKKKDIEERVNTLLEYVNLKEKiyEYP-AN 137
Cdd:TIGR03719 89 VEEGVAEIKDALDRFNEISAKYAepdadfdkLAAEQAELQEI-----IDAADAWDLDSQLEIAMDALRCPPW--DADvTK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 138 LSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTkSILELLLKirdEFNLTIVLITH 196
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-AWLERHLQ---EYPGTVVAVTH 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-169 |
5.83e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 5.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEePTQGNIFIDGKDIVKMNSKELkeARKNmAMIFQSFNLFYQKNVF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAEL--ARHR-AYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 98 ENIA--YPLRINKwkkKDIEERVNTLLEYVNLKEKiYEYPAN-LSGGQKQRVAIARA-LAVQP------KILLCDEATSA 167
Cdd:COG4138 88 QYLAlhQPAGASS---EAVEQLLAQLAEALGLEDK-LSRPLTqLSGGEWQRVRLAAVlLQVWPtinpegQLLLLDEPMNS 163
|
..
gi 343398708 168 LD 169
Cdd:COG4138 164 LD 165
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-196 |
1.35e-11 |
|
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: 65.34 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDgkDIVKmnskelkearknM 81
Cdd:TIGR03719 323 IEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVK------------L 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMIFQSF-NLFYQKNVFENIAYPLRINKWKKKDIEERVntlleYV---NLK-----EKIyeypANLSGGQKQRVAIARAL 152
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVgrfNFKgsdqqKKV----GQLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 343398708 153 AVQPKILLCDEATSALDPQSTKSILELLLkirdEFNLTIVLITH 196
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALL----NFAGCAVVISH 498
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-215 |
2.45e-11 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.34 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdiVKMNSKelkearknmamifqsFNLFYQKNVFEN 99
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--ISFSSQ---------------FSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRINkwkkkdiEERVNTLLEYVNLKEKIYEYPA-----------NLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:cd03291 118 IIFGVSYD-------EYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 343398708 169 DPQSTKSILE-LLLKIRDefNLTIVLITHQMEVVKaICDRAAVIENGE 215
Cdd:cd03291 191 DVFTEKEIFEsCVCKLMA--NKTRILVTSKMEHLK-KADKILILHEGS 235
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-197 |
3.25e-11 |
|
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: 61.49 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 19 TNINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEEPT-QGNIFIDGKDIvkmnskelkearknmamifqsfnlfyqknv 96
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPL------------------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 97 feNIAYPLRINKWKKKDIEERVNTLLEYVnlkekiyEYPANLSG---GQKQRVAIARALAVQPKILLCDEATSALDPQST 173
Cdd:cd03232 74 --DKNFQRSTGYVEQQDVHSPNLTVREAL-------RFSALLRGlsvEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|....
gi 343398708 174 KSILELLLKIRDEfNLTIVLITHQ 197
Cdd:cd03232 145 YNIVRFLKKLADS-GQAILCTIHQ 167
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
28-197 |
4.13e-11 |
|
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: 61.35 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 28 GEIFGIIGMSGAGKSSLIRCINRLEEPTQGNifidgkdiVKMNSKELKEAR----KNMAMIFQSFNLFYQKNVFENIAYp 103
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGR--------VLLNGGPLDFQRdsiaRGLLYLGHAPGIKTTLSVLENLRF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 104 lrinkWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKi 183
Cdd:cd03231 97 -----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG- 170
|
170
....*....|....
gi 343398708 184 RDEFNLTIVLITHQ 197
Cdd:cd03231 171 HCARGGMVVLTTHQ 184
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
8-202 |
1.11e-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: 59.64 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 8 VKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCInrleeptqgnifidgkdivkmnskeLKEARKNMAMIFQS 87
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG-------------------------LYASGKARLISFLP 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 88 fNLFYQKNVFeniayplrINKWKKkdieeRVNTLLEYVNLKEKIyeypANLSGGQKQRVAIARALAVQPK--ILLCDEAT 165
Cdd:cd03238 56 -KFSRNKLIF--------IDQLQF-----LIDVGLGYLTLGQKL----STLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190
....*....|....*....|....*....|....*..
gi 343398708 166 SALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVK 202
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLS 153
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-218 |
1.99e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGkdivkmnskelkearkNMAMIFQsfNLFYQKNVF-EN 99
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------------SVAYVPQ--QAWIQNDSLrEN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRINKWKKKDIEERVNTLLEYVNL----KEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKS 175
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPDLEILpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 343398708 176 ILELLLKIRDEF-NLTIVLITHQMEVVKAIcDRAAVIENGEIIE 218
Cdd:TIGR00957 799 IFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISE 841
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-214 |
2.93e-10 |
|
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: 61.46 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKdiVKMNSKelkearknmamifqsFNLFYQKNVFEN 99
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--ISFSPQ---------------TSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 100 IAYPLRINkwkkkdiEERVNTLLEYVNLKEKIYEYP-----------ANLSGGQKQRVAIARALAVQPKILLCDEATSAL 168
Cdd:TIGR01271 507 IIFGLSYD-------EYRYTSVIKACQLEEDIALFPekdktvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 343398708 169 DPQSTKSILE-LLLKIRDefNLTIVLITHQMEVVKAiCDRAAVIENG 214
Cdd:TIGR01271 580 DVVTEKEIFEsCLCKLMS--NKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-237 |
3.66e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEEPT-------QGNIFIDGKDIVKMNSKELKEARKNMAMIFQSFNLF 91
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAFAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 YQKNVFENIAYP--LRINKWKKKDiEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALA---------VQPKILL 160
Cdd:PRK13547 99 SAREIVLLGRYPhaRRAGALTHRD-GEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYLL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIENGEIIEQDTVLKLFTSPKTATTKKF 237
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGF 254
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-203 |
3.85e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 58.34 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 33 IIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVKMnskelkeARKNMAMIFQSFNLFYQKNVFENIAYplrinkWKK- 111
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------AKPYCTYIGHNLGLKLEMTVFENLKF------WSEi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 112 KDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQStKSILELLLKIRDEFNLTI 191
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN-RDLLNNLIVMKANSGGIV 176
|
170
....*....|..
gi 343398708 192 VLITHQMEVVKA 203
Cdd:PRK13541 177 LLSSHLESSIKS 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-197 |
4.83e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 4.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 28 GEIFGIIGMSGAGKSSLircINRLEEPTQGNIFIdGKdIVKMNSKELKEARKNMAMIFQSFNLFYQKNVFENIAY----- 102
Cdd:PLN03211 94 GEILAVLGPSGSGKSTL---LNALAGRIQGNNFT-GT-ILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFcsllr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 103 -PLRINKWKKKDIEERVNTLLEYVNLKEKIY--EYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILEL 179
Cdd:PLN03211 169 lPKSLTKQEKILVAESVISELGLTKCENTIIgnSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170
....*....|....*...
gi 343398708 180 LLKIRDEfNLTIVLITHQ 197
Cdd:PLN03211 249 LGSLAQK-GKTIVTSMHQ 265
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-197 |
4.99e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 25 IKKGEIFGIIGMSGAGKSSLIRCinrLEEPTQGNIFIDGKDIVkmNSKELKEArknmamiFQSFNLFYQKN--------V 96
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLV--NGRPLDSS-------FQRSIGYVQQQdlhlptstV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 97 FENIAY------PLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPA-NLSGGQKQRVAIARALAVQPKILL-CDEATSAL 168
Cdd:TIGR00956 854 RESLRFsaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGeGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170 180
....*....|....*....|....*....
gi 343398708 169 DPQSTKSILELLLKIRDEfNLTIVLITHQ 197
Cdd:TIGR00956 934 DSQTAWSICKLMRKLADH-GQAILCTIHQ 961
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-196 |
6.56e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 6.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 21 INLEIKKGEIFGIIGMSGAGKSSLIRCINRLeEPTQGNIFIDGKDIVKMNSKELKEARknmAMIFQSFNLFYQKNVFENI 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 101 AYPLRiNKWKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARA-LAVQPKI------LLCDEATSALD-PQs 172
Cdd:PRK03695 91 TLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDvAQ- 168
|
170 180
....*....|....*....|....
gi 343398708 173 tKSILELLLKIRDEFNLTIVLITH 196
Cdd:PRK03695 169 -QAALDRLLSELCQQGIAVVMSSH 191
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-217 |
1.38e-09 |
|
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: 56.89 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 13 NGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEeptqGNIFIDGKdiVKMNSKELKEarknMAMIFQSFNLF 91
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTE----GNVSVEGD--IHYNGIPYKE----FAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 92 yqkNVFENIAYPlrinkwkkkdiEERVNTLLEYVnLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQ 171
Cdd:cd03233 88 ---VSEEDVHFP-----------TLTVRETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 343398708 172 STKSILELLLKIRDEFNLTIVLITHQM-EVVKAICDRAAVIENGEII 217
Cdd:cd03233 153 TALEILKCIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQI 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-210 |
1.49e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.84 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 27 KGEIFGIIGMSGAGKSSLIRCI-NRLEEPTQGNIFIDGkdivkmnskelkearknmamifqsfnlfyqknvfeniayplr 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 106 inkwkkkdieERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILEL-----L 180
Cdd:smart00382 39 ----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlL 108
|
170 180 190
....*....|....*....|....*....|
gi 343398708 181 LKIRDEFNLTIVLITHQMEVVKAICDRAAV 210
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-197 |
1.54e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 18 VTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIvkmnSKELKEARKNMAMIFQSFNLFYQKNVF 97
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 98 ENIAYPLRINKwKKKDIEERVnTLLEYvnlkEKIYEYPAN-LSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSI 176
Cdd:PRK13540 93 ENCLYDIHFSP-GAVGITELC-RLFSL----EHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|.
gi 343398708 177 LELLLKIRDEFNlTIVLITHQ 197
Cdd:PRK13540 167 ITKIQEHRAKGG-AVLLTSHQ 186
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-196 |
8.85e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 8.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCIN-------------------RLEE--P--TQGNIFidgkDIVKMNSKELKE 76
Cdd:PRK11147 21 NAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqdlivaRLQQdpPrnVEGTVY----DFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 77 ARKNMAMIFQSFNLFYQKNVFENIAyplRI-------NKWKkkdIEERVNTLLEYVNLKEkiyEYP-ANLSGGQKQRVAI 148
Cdd:PRK11147 97 YLKRYHDISHLVETDPSEKNLNELA---KLqeqldhhNLWQ---LENRINEVLAQLGLDP---DAAlSSLSGGWLRKAAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 343398708 149 ARALAVQPKILLCDEATSALDPQsTKSILELLLKirdEFNLTIVLITH 196
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIE-TIEWLEGFLK---TFQGSIIFISH 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-196 |
1.28e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFkAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIdGkDIVKMNSKElkEARKNM 81
Cdd:PRK11819 325 IEAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKLAYVD--QSRDAL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 AMifqsfnlfyQKNVFENIAYPLRINKWKKKDIEERVntlleYV---NLK----EKIYeypANLSGGQKQRVAIARALAV 154
Cdd:PRK11819 400 DP---------NKTVWEEISGGLDIIKVGNREIPSRA-----YVgrfNFKggdqQKKV---GVLSGGERNRLHLAKTLKQ 462
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343398708 155 QPKILLCDEATSALDPQSTKSILELLLkirdEFNLTIVLITH 196
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALL----EFPGCAVVISH 500
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-216 |
1.53e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDgKDIVK-------MNSKelkeARKNMamifqsfnLFY 92
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-RSIAYvpqqawiMNAT----VRGNI--------LFF 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 QKNVFENIAYPLRINKwkkkdIEERVNTLLEyvNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQS 172
Cdd:PTZ00243 745 DEEDAARLADAVRVSQ-----LEADLAQLGG--GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 343398708 173 TKSILE--LLLKIRDEfnlTIVLITHQMEVVkAICDRAAVIENGEI 216
Cdd:PTZ00243 818 GERVVEecFLGALAGK---TRVLATHQVHVV-PRADYVVALGDGRV 859
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-215 |
6.23e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDnGFKAVTNINlEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIfidgkdivkmnSKELKearknm 81
Cdd:COG1245 342 VEYPDLTKSYG-GFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 82 amifqsfnlfyqknvfenIAY-PLRInkwkKKDIEERVNTLLEYVNLK-----------------EKIYEYP-ANLSGGQ 142
Cdd:COG1245 403 ------------------ISYkPQYI----SPDYDGTVEEFLRSANTDdfgssyykteiikplglEKLLDKNvKDLSGGE 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 143 KQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIEnGE 215
Cdd:COG1245 461 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GE 532
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-169 |
1.11e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 1 MIKIENLVKIYDnGFKAVTNiNLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVK---MNSKELKEA 77
Cdd:PRK13409 340 LVEYPDLTKKLG-DFSLEVE-GGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKpqyIKPDYDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 78 RKNMAMIFQSFNLFYQKNvfeNIAYPLRInkwkkkdieervntlleyvnlkEKIYEYPAN-LSGGQKQRVAIARALAVQP 156
Cdd:PRK13409 418 EDLLRSITDDLGSSYYKS---EIIKPLQL----------------------ERLLDKNVKdLSGGELQRVAIAACLSRDA 472
|
170
....*....|...
gi 343398708 157 KILLCDEATSALD 169
Cdd:PRK13409 473 DLYLLDEPSAHLD 485
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-204 |
1.69e-07 |
|
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: 51.07 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 30 IFGIIGMSGAGKSSLIRCINRL---EEPTQGNIFIDGKDIVKMNSK------ELKEARKNMAMIFQSFnlfyqkNVFENI 100
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEVraqvklAFENANGKKYTITRSL------AILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 101 AYpLRinkwkkkdiEERVNTLLEyvnlkekiyEYPANLSGGQKQ------RVAIARALAVQPKILLCDEATSALDPQS-T 173
Cdd:cd03240 98 IF-CH---------QGESNWPLL---------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiE 158
|
170 180 190
....*....|....*....|....*....|.
gi 343398708 174 KSILELLLKIRDEFNLTIVLITHQMEVVKAI 204
Cdd:cd03240 159 ESLAEIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
136-196 |
1.72e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 1.72e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 136 ANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTkSILELLLKirdEFNLTIVLITH 196
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLEQFLH---DYPGTVVAVTH 218
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-212 |
3.64e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 4 IENLVKIYDNG--FKavtNINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNI-FIDGKDIVKMNSKELKEARKN 80
Cdd:PRK15064 322 VENLTKGFDNGplFK---NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDHAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MamifqsfnlfyqkNVFENIAyplrinKWKK-KDIEERVNTLL-------EYVNLKEKiyeypaNLSGGQKQRVAIARAL 152
Cdd:PRK15064 399 L-------------TLFDWMS------QWRQeGDDEQAVRGTLgrllfsqDDIKKSVK------VLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 153 AVQPKILLCDEATSALDPQSTKSiLELLLkirDEFNLTIVLITHQMEVVKAICDRaaVIE 212
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMESIES-LNMAL---EKYEGTLIFVSHDREFVSSLATR--IIE 507
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-202 |
4.42e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.90 E-value: 4.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 343398708 138 LSGGQKQRVAIARALA---VQPKILLC-DEATSALDPQSTKSILELLLKIRDEFNLTIVlITHQMEVVK 202
Cdd:cd03227 78 LSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAE 145
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
2-212 |
1.04e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 48.34 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLVKIYDNGFkavTNINL-EIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDGKDIVkmnskelkearkn 80
Cdd:cd03222 1 QLYPDCVKRYGVFF---LLVELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 mamifqsfnlfyqknvfeniayplrinkWKKKDIEervntlleyvnlkekiyeypanLSGGQKQRVAIARALAVQPKILL 160
Cdd:cd03222 65 ----------------------------YKPQYID----------------------LSGGELQRVAIAAALLRNATFYL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 343398708 161 CDEATSALDPQSTKSILELLLKIRDEFNLTIVLITHQMEVVKAICDRAAVIE 212
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-219 |
1.05e-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: 48.79 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLI----------RCINRLeePTQGNIFIDGKDIVKMNSKE---------LKEARKN 80
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESL--SAYARQFLGQMDKPDVDSIEglspaiaidQKTTSRN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 -------MAMIFQSFNLFYQknvfeniayplRINkwkkkdIEERVNTL----LEYVNLKEKIyeypANLSGGQKQRVAIA 149
Cdd:cd03270 91 prstvgtVTEIYDYLRLLFA-----------RVG------IRERLGFLvdvgLGYLTLSRSA----PTLSGGEAQRIRLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 343398708 150 RALAVQPK--ILLCDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVKA---ICD--RAAVIENGEIIEQ 219
Cdd:cd03270 150 TQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIRAadhVIDigPGAGVHGGEIVAQ 225
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-196 |
1.70e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 2 IKIENLvkiydNGFKAVTNINLEikkGEIFGIIGMSGAGKSSLIRCI-------------------NRLEEPT------- 55
Cdd:COG0419 5 LRLENF-----RSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIryalygkarsrsklrsdliNVGSEEAsvelefe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 56 -QGNIFI------DGKDIVKMNSKELKEarknmaMIFQSFNLfyqkNVFENIAYPLRInkwKKKDIEERVNTLLEYVNLK 128
Cdd:COG0419 77 hGGKRYRierrqgEFAEFLEAKPSERKE------ALKRLLGL----EIYEELKERLKE---LEEALESALEELAELQKLK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 129 EKI------YEYPANLSGGQKQRVAIARALAvqpkiLLCDeaTSALDPQSTKSILELLLKIRdefnltivLITH 196
Cdd:COG0419 144 QEIlaqlsgLDPIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-206 |
2.41e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 47.99 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLI---------RCINRLEEPTQGNIFIDG-----KDIVKMNSKELKEARKNMAMIF 85
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGlehidKVIVIDQSPIGRTPRSNPATYT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 86 QSF----NLF--------YQKNVFE------NIAYPLRINKWKKKD-------IEERVNTL----LEYVNLKEKIYEypa 136
Cdd:cd03271 93 GVFdeirELFcevckgkrYNRETLEvrykgkSIADVLDMTVEEALEffenipkIARKLQTLcdvgLGYIKLGQPATT--- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 137 nLSGGQKQRVAIARALAVQ---PKILLCDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVKAiCD 206
Cdd:cd03271 170 -LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIKC-AD 239
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-216 |
2.86e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFidgkdivkmnskelKEARKNMAMIFQ---------SFNL 90
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------------RSAKVRMAVFSQhhvdgldlsSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 91 FYQKNVFENIAyplrinkwkkkdiEERVNTLLEYVNLKEKIYEYPA-NLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:PLN03073 593 LYMMRCFPGVP-------------EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 343398708 170 PQSTKSILELLLKirdeFNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PLN03073 660 LDAVEALIQGLVL----FQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
20-214 |
4.61e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIR-----CINRL-EEPTQGNIFIDG-----------------------------K 64
Cdd:PRK00635 613 DLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVEEFiEQGFCSNLSIQWgaisrlvhitrdlpgrsqrsipltyikafD 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 65 DIVKMNSKELKEARKNMAMIFQSFNL-------------------------------FYQKNVFE------NIAYPLRIN 107
Cdd:PRK00635 693 DLRELFAEQPRSKRLGLTKSHFSFNTplgacaecqglgsitttdnrtsipcpsclgkRFLPQVLEvrykgkNIADILEMT 772
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 108 KWKKKD-------IEERVNTL----LEYVNLKEKIYeypaNLSGGQKQRVAIARAL---AVQPKILLCDEATSALDPQST 173
Cdd:PRK00635 773 AYEAEKffldepsIHEKIHALcslgLDYLPLGRPLS----SLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDI 848
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 343398708 174 KSILELLLKIRDEFNlTIVLITHQMEVVKaICDRaaVIENG 214
Cdd:PRK00635 849 KALIYVLQSLTHQGH-TVVIIEHNMHVVK-VADY--VLELG 885
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-217 |
9.98e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 136 ANLSGGQKQRVAIARALAVQ----PKILlcDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVkAICDR---- 207
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAEligiTYIL--DEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRiidi 550
|
90
....*....|..
gi 343398708 208 --AAVIENGEII 217
Cdd:PRK00635 551 gpGAGIFGGEVL 562
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-257 |
1.70e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 25 IKKGEIFGIIGMSGAGKSSLIRCINrlEEPTQGNIFIDGKdiVKMNSKELKEARK----NMAMIFQSFNLFYQKNVFENI 100
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIA--SNTDGFHIGVEGV--ITYDGITPEEIKKhyrgDVVYNAETDVHFPHLTVGETL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 101 AYPLRI----NKWKKKDIEERVNTLLEYVnlkEKIY------------EYPANLSGGQKQRVAIARALAVQPKILLCDEA 164
Cdd:TIGR00956 160 DFAARCktpqNRPDGVSREEYAKHIADVY---MATYglshtrntkvgnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 165 TSALDPQSTKSILELLLKIRDEFNLTIVLITHQ-MEVVKAICDRAAVIENGEIIEQ---DTVLKLFTS-----PKTATTK 235
Cdd:TIGR00956 237 TRGLDSATALEFIRALKTSANILDTTPLVAIYQcSQDAYELFDKVIVLYEGYQIYFgpaDKAKQYFEKmgfkcPDRQTTA 316
|
250 260
....*....|....*....|....
gi 343398708 236 KFIETL--PQFedydELPVADYKG 257
Cdd:TIGR00956 317 DFLTSLtsPAE----RQIKPGYEK 336
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
93-197 |
2.03e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 93 QKNVFENIAY------PLRINKWKKKDIEERVNTLLEYVNLKEKIYEYPA--NLSGGQKQRVAIARALAVQPKILLCDEA 164
Cdd:PLN03140 967 QVTVRESLIYsaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
90 100 110
....*....|....*....|....*....|...
gi 343398708 165 TSALDPQSTKSILELLLKIRDEfNLTIVLITHQ 197
Cdd:PLN03140 1047 TSGLDARAAAIVMRTVRNTVDT-GRTVVCTIHQ 1078
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
114-202 |
3.60e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 114 IEERVNTL----LEYVNLKEKIYeypaNLSGGQKQRVAIARAL---AVQPKILLCDEATSALDPQSTKSILELLLKIRDE 186
Cdd:TIGR00630 806 ISRKLQTLcdvgLGYIRLGQPAT----TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK 881
|
90
....*....|....*.
gi 343398708 187 FNlTIVLITHQMEVVK 202
Cdd:TIGR00630 882 GN-TVVVIEHNLDVIK 896
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-216 |
4.01e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 20 NINLEIKKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFID-----GK--------------DIVKMNSKELKEARKN 80
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpnerlGKlrqdqfafeeftvlDTVIMGHTELWEVKQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFqsfnlfyqknvfeniAYP-------LRINKWKKK-------DIEERVNTLLEYVNLKEKIYEYP-ANLSGGQKQR 145
Cdd:PRK15064 99 RDRIY---------------ALPemseedgMKVADLEVKfaemdgyTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 343398708 146 VAIARALAVQPKILLCDEATSALDpQSTKSILELLLKIRdefNLTIVLITHQMEVVKAICDRAAVIENGEI 216
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLD-INTIRWLEDVLNER---NSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
139-204 |
7.79e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 7.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 343398708 139 SGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKirdeFNLTIVLITHQMEVVKAI 204
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK----WPKTFIVVSHAREFLNTV 407
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
138-219 |
8.46e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 138 LSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
..
gi 343398708 218 EQ 219
Cdd:PRK10938 215 ET 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-217 |
9.38e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.01 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 16 KAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCI-------NrleepTQGNIFIDGKDI-VKMNSKELK-------EARKN 80
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrsygrN-----ISGTVFKDGKEVdVSTVSDAIDaglayvtEDRKG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 81 MAMIFqsfnlfyQKNVFENIAYPlRINKWKKK----DIEERV--NTLLEYVNLKE-KIYEYPANLSGGQKQRVAIARALA 153
Cdd:NF040905 349 YGLNL-------IDDIKRNITLA-NLGKVSRRgvidENEEIKvaEEYRKKMNIKTpSVFQKVGNLSGGNQQKVVLSKWLF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 343398708 154 VQPKILLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITHQMEVVKAICDRAAVIENGEII 217
Cdd:NF040905 421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
106-218 |
1.02e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 106 INKWKkkdIEERVNTLLEYVNLKEKIYEYP-ANLSGGQKQRVAIARALAVQPKILLCDEATSALDPQSTkSILELLLKir 184
Cdd:PRK10636 120 IDAWT---IRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAV-IWLEKWLK-- 193
|
90 100 110
....*....|....*....|....*....|....
gi 343398708 185 dEFNLTIVLITHQMEVVKAICDRAAVIENGEIIE 218
Cdd:PRK10636 194 -SYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
136-180 |
1.09e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 40.30 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 343398708 136 ANLSGGQKQR---VAIARALAVQ----------PKILLCDEATSALDPQSTKSILELL 180
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELL 88
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
58-233 |
1.70e-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: 43.46 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 58 NIFIDGKDIVKMNSKELKEArknmaMIFqsFNLFYQKNVFENIAYPLRinkwkkKDIEERVNTL----LEYVNLKEKIye 133
Cdd:TIGR00630 422 AVTVGGKSIADVSELSIREA-----HEF--FNQLTLTPEEKKIAEEVL------KEIRERLGFLidvgLDYLSLSRAA-- 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 134 ypANLSGGQKQRVAIARALAVQPK--ILLCDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVKAiCDR---- 207
Cdd:TIGR00630 487 --GTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGN-TLIVVEHDEDTIRA-ADYvidi 562
|
170 180
....*....|....*....|....*...
gi 343398708 208 --AAVIENGEIIEQDTVLKLFTSPKTAT 233
Cdd:TIGR00630 563 gpGAGEHGGEVVASGTPEEILANPDSLT 590
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-169 |
1.85e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.35 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 26 KKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIfiDGK----DIV-------------KMNSKELKEARK--NMAMIFQ 86
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPpdwdEILdefrgselqnyftKLLEGDVKVIVKpqYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 87 SFnlfyQKNVFENIayplrinkwKKKDIEERVNTLLEYVNLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCDEATS 166
Cdd:cd03236 102 AV----KGKVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
...
gi 343398708 167 ALD 169
Cdd:cd03236 169 YLD 171
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
13-196 |
2.11e-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: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 13 NGFKAVTNINLE-IKKGEIFGIIGMSGAGKSSLIRCINRL---EEPTQGNifiDGKDIVKMNSKElKEARknMAMIFQSF 88
Cdd:cd03279 12 GPFREEQVIDFTgLDNNGLFLICGPTGAGKSTILDAITYAlygKTPRYGR---QENLRSVFAPGE-DTAE--VSFTFQLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 89 NLFYqknvfeniayplRINKWKKKDIEERVNTLL----EYVNLKEKIYEypaNLSGGQKQRVAIARALAVQPKI------ 158
Cdd:cd03279 86 GKKY------------RVERSRGLDYDQFTRIVLlpqgEFDRFLARPVS---TLSGGETFLASLSLALALSEVLqnrgga 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 343398708 159 ----LLCDEATSALDPQSTKSILELLLKIRDEfNLTIVLITH 196
Cdd:cd03279 151 rleaLFIDEGFGTLDPEALEAVATALELIRTE-NRMVGVISH 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-169 |
3.99e-03 |
|
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: 39.00 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 26 KKGEIFGIIGMSGAGKSSLIRCINRLEEPTQGNIFIDG-KDIV--------------KMNSKELKEARKN--MAMIFQSF 88
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPsWDEVlkrfrgtelqdyfkKLANGEIKVAHKPqyVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 89 nlfyqknvfeniayplrinKWKKKDIEERVN---TLLEYV---NLKEKIYEYPANLSGGQKQRVAIARALAVQPKILLCD 162
Cdd:COG1245 177 -------------------KGTVRELLEKVDergKLDELAeklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
....*..
gi 343398708 163 EATSALD 169
Cdd:COG1245 238 EPSSYLD 244
|
|
| PLN03210 |
PLN03210 |
Resistant to P. syringae 6; Provisional |
5-68 |
4.35e-03 |
|
Resistant to P. syringae 6; Provisional
Pssm-ID: 215633 [Multi-domain] Cd Length: 1153 Bit Score: 39.09 E-value: 4.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 343398708 5 ENLVKIYDNGFKAVTNINLEIKKGEIFGIIGMSGAGKSSLIRCI-NRLEEPTQGNIFIDGKDIVK 68
Cdd:PLN03210 184 EDFVGIEDHIAKMSSLLHLESEEVRMVGIWGSSGIGKTTIARALfSRLSRQFQSSVFIDRAFISK 248
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
33-200 |
5.40e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 37.29 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 33 IIGMSGAGKSSLIRCInrleeptqgnIFIDGKDIVKMNSKELKEARK--NMAMIFQSF-NLFYQKNVFeniayplrinkw 109
Cdd:cd03239 27 IVGPNGSGKSNIVDAI----------CFVLGGKAAKLRRGSLLFLAGggVKAGINSASvEITFDKSYF------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 343398708 110 kkkdieervntlleyVNLKEKIYEYpanLSGGQKQRVAIARALAVQ---PKILLC-DEATSALDPQSTKSILELLLKIRD 185
Cdd:cd03239 85 ---------------LVLQGKVEQI---LSGGEKSLSALALIFALQeikPSPFYVlDEIDAALDPTNRRRVSDMIKEMAK 146
|
170
....*....|....*
gi 343398708 186 EFNLTIVlITHQMEV 200
Cdd:cd03239 147 HTSQFIV-ITLKKEM 160
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-203 |
7.34e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 7.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 343398708 135 PAN-LSGGQKQRVAIARALA--VQPKIL-LCDEATSALDPQSTKSILELLLKIRDEFNlTIVLITHQMEVVKA 203
Cdd:COG0178 823 PATtLSGGEAQRVKLASELSkrSTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDKGN-TVVVIEHNLDVIKT 894
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-169 |
8.19e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.87 E-value: 8.19e-03
10 20 30
....*....|....*....|....*....|...
gi 343398708 137 NLSGGQKQRVAIARALAVQPKILLCDEATSALD 169
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| |
