|
Name |
Accession |
Description |
Interval |
E-value |
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-259 |
2.41e-148 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 414.55 E-value: 2.41e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAM 82
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSgEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQL-HQSGEKR 161
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLwEPDGPPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 162 ILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYGY 241
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGA 240
|
250
....*....|....*...
gi 491527411 242 RSIVTKHPTLDFPQVHAA 259
Cdd:PRK13548 241 DVLVQPHPETGAPLVLPR 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-260 |
7.25e-131 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 370.21 E-value: 7.25e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLP 84
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSgEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQLHQS--GEKRI 162
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPvdGGPRW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 163 LMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYGYR 242
Cdd:COG4559 162 LFLDEPTSALDLAHQHAVLRLARQLA-RRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYGAD 240
|
250
....*....|....*...
gi 491527411 243 SIVTKHPTLDFPQVHAAA 260
Cdd:COG4559 241 LRVLAHPEGGCPQVLPRA 258
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-256 |
6.78e-98 |
|
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: 286.55 E-value: 6.78e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPEKSAKHIAML 83
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLTFPFLAREVVELGAIP----LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgE 159
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPhlglFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ-----E 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 160 KRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVY 239
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
250
....*....|....*..
gi 491527411 240 GYRSIVTKHPTLDFPQV 256
Cdd:COG1120 236 GVEARVIEDPVTGRPLV 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-223 |
2.50e-71 |
|
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: 216.53 E-value: 2.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPEKSAKHIAMLPQhs 87
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 tltfpflarevvelgaiplslsnkettklalhYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDE 167
Cdd:cd03214 81 --------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQ-----EPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 168 PTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-248 |
7.84e-68 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 209.95 E-value: 7.84e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKqkhdwEPEKSAKH 79
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSgTVRLFGK-----PPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTL--TFPFLAREVVELGAIP----LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQ 153
Cdd:COG1121 77 IGYVPQRAEVdwDFPITVRDVVLMGRYGrrglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 154 lhqsgEKRILMLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLhNGKLVCDDTPWNALTSE 233
Cdd:COG1121 157 -----DPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
|
250
....*....|....*
gi 491527411 234 RIEQVYGYRSIVTKH 248
Cdd:COG1121 230 NLSRAYGGPVALLAH 244
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
6-249 |
8.74e-57 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 182.14 E-value: 8.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLP 84
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSgTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLTFPFLAREVVELGAIP-LSLSNKETTK---LALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEK 160
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPwLSLWGRLSAEdnaRVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ-----DT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYG 240
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFD 236
|
....*....
gi 491527411 241 YRSIVTKHP 249
Cdd:PRK11231 237 VEAEIHPEP 245
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-242 |
1.92e-55 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 179.25 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH---------HITYFGKQKHDWEPEKSAKHIAMLPQHST 88
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtgDVTLNGEPLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 89 LTFPFLAREVVELGAIPLSLSNKETTK----LALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQLHQSGEK---- 160
Cdd:PRK13547 94 PAFAFSAREIVLLGRYPHARRAGALTHrdgeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLWPPHDAaqpp 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYG 240
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYG 253
|
..
gi 491527411 241 YR 242
Cdd:PRK13547 254 FA 255
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-240 |
7.87e-54 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 174.50 E-value: 7.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSNhhityfGKQKHDWEPEKSAKHIA 81
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISrllppdsGEVLVD------GLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHSTLTFPFLAREVVELGAIP-----LSLSNKETTKLALHYMEQTDvlhLAESLYPSLSGGEKQRLHLARVMTQlhq 156
Cdd:COG4604 79 ILRQENHINSRLTVRELVAFGRFPyskgrLTAEDREIIDEAIAYLDLED---LADRYLDELSGGQRQRAFIAMVLAQ--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 157 sgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIE 236
Cdd:COG4604 153 --DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLS 230
|
....
gi 491527411 237 QVYG 240
Cdd:COG4604 231 DIYD 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-224 |
1.24e-52 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 170.02 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKqkhdwEPEKSAKHIAMLPQHS 87
Cdd:cd03235 3 EDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSgSIRVFGK-----PLEKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TL--TFPFLAREVVELGAIP----LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKR 161
Cdd:cd03235 78 SIdrDFPISVRDVVLMGLYGhkglFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ-----DPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 162 ILMLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLhNGKLVCDD 224
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-239 |
2.13e-52 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 170.24 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDwEPEKSAKHIAMLPQHS 87
Cdd:COG1131 4 RGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSgEVRVLGEDVAR-DPAEVRRRIGYVPQEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEKRILMLD 166
Cdd:COG1131 83 AL-YPDLtVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALAL-----LHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 167 EPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPwNALTSERIEQVY 239
Cdd:COG1131 157 EPTSGLDPEARRELWELLRE-LAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP-DELKARLLEDVF 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-256 |
1.88e-51 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 172.72 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLP 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAgTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLTFPFLAREVVELGAIP----LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEK 160
Cdd:PRK09536 84 QDTSLSFEFDVRQVVEMGRTPhrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ-----AT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYG 240
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFD 237
|
250
....*....|....*.
gi 491527411 241 YRSIVTKHPTLDFPQV 256
Cdd:PRK09536 238 ARTAVGTDPATGAPTV 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-256 |
6.37e-48 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 159.77 E-value: 6.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLP 84
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHgHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLTFPFLAREVVELGAIP----LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEK 160
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPhqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ-----ET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYG 240
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYG 242
|
250
....*....|....*.
gi 491527411 241 YRSIVTKHPTLDFPQV 256
Cdd:PRK10253 243 LRCMIIDDPVAGTPLV 258
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-219 |
5.21e-46 |
|
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: 153.01 E-value: 5.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03225 3 KNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGlLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HstltfP---FLAREV---VELGAIPLSLSNKETTKLALHYMEQTDVLHLAE-SLYpSLSGGEKQRLHLARVMTQlhqsg 158
Cdd:cd03225 83 N-----PddqFFGPTVeeeVAFGLENLGLPEEEIEERVEEALELVGLEGLRDrSPF-TLSGGQKQRVAIAGVLAM----- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 159 EKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
9-226 |
6.92e-46 |
|
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: 153.26 E-value: 6.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSAKHIAMLPQh 86
Cdd:COG1122 4 ENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 87 stltFP---FLAREV---VELGAIPLSLSNKETTKLALHYMEQTDVLHLAE-SLYpSLSGGEKQRLHLARV--Mtqlhqs 157
Cdd:COG1122 83 ----NPddqLFAPTVeedVAFGPENLGLPREEIRERVEEALELVGLEHLADrPPH-ELSGGQKQRVAIAGVlaM------ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 158 gEKRILMLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:COG1122 152 -EPEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-226 |
1.20e-45 |
|
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: 153.09 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDwEPEKSAKHIAMLPQ-- 85
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSgSILIDGEDVRK-EPREARRQIGVLPDer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 --HSTLTfpflAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqLHQSgekRIL 163
Cdd:COG4555 84 glYDRLT----VRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARAL--VHDP---KVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 164 MLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSL 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
9-239 |
6.06e-45 |
|
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: 151.18 E-value: 6.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEK---SAKHIAML 83
Cdd:cd03256 4 ENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlVEPTSGSVLIDGTDINKLKGKAlrqLRRQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLTFPFLAREVVELGAIP--------LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlh 155
Cdd:cd03256 84 FQQFNLIERLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 156 qsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPwNALTSERI 235
Cdd:cd03256 162 ---QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP-AELTDEVL 237
|
....
gi 491527411 236 EQVY 239
Cdd:cd03256 238 DEIY 241
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-220 |
6.32e-45 |
|
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: 149.08 E-value: 6.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDwEPEKSAKHIAMLPQHS 87
Cdd:cd03230 4 RNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFL-AREVVElgaiplslsnkettklalhymeqtdvlhlaeslypsLSGGEKQRLHLARVMtqLHQSgekRILMLD 166
Cdd:cd03230 83 SL-YENLtVRENLK------------------------------------LSGGMKQRLALAQAL--LHDP---ELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 167 EPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:cd03230 121 EPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-220 |
1.53e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLP 84
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSgEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHST---------LTFPFLAREVvelgaiplslsnKETTKLALHYMEQtdvLHLAESL----YPSLSGGEKQRLHLARVM 151
Cdd:COG4619 81 QEPAlwggtvrdnLPFPFQLRER------------KFDRERALELLER---LGLPPDIldkpVERLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:COG4619 146 LL-----QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-219 |
3.81e-43 |
|
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: 143.92 E-value: 3.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQhs 87
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSgEILIDGKDIAKLPLEELRRRIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 tltfpflarevvelgaiplslsnkettklalhymeqtdvlhlaeslypsLSGGEKQRLHLARVMtqLHQSgekRILMLDE 167
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARAL--LLNP---DLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491527411 168 PTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-240 |
3.88e-43 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 146.91 E-value: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQHSTLTFPFLAREVVE 100
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 101 LGAiPLSLSNKETTKLALHYMEQtdvLHLAESLYPS---LSGGEKQRLHLARVMTQLH--QSGEKRILMLDEPTSALDLA 175
Cdd:COG4138 92 LHQ-PAGASSEAVEQLLAQLAEA---LGLEDKLSRPltqLSGGEWQRVRLAAVLLQVWptINPEGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 176 HQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYG 240
Cdd:COG4138 168 QQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFG 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-221 |
1.72e-41 |
|
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: 141.24 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 7 SGKNISMTYG-NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSakhIAMLP 84
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSgSILLNGKPIKAKERRKS---IGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHST--LTFPFLAREVVeLGAIPLSLSNKETTklalHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRI 162
Cdd:cd03226 78 QDVDyqLFTDSVREELL-LGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS-----GKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 163 LMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-226 |
4.46e-41 |
|
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: 141.27 E-value: 4.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGkqkHDW----EPEK 75
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSgEILVDG---QDItglsEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 SA--KHIAMLPQHSTLtFPFL-AREVVelgAIPL----SLSNKETTKLALHYMEQTDVLHlAESLYPS-LSGGEKQRLHL 147
Cdd:COG1127 78 YElrRRIGMLFQGGAL-FDSLtVFENV---AFPLrehtDLSEAEIRELVLEKLELVGLPG-AADKMPSeLSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 148 AR--VMtqlhqsgEKRILMLDEPTSALD--LAHQHNTLkIaRETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:COG1127 153 ARalAL-------DPEILLYDEPTAGLDpiTSAVIDEL-I-RELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
...
gi 491527411 224 DTP 226
Cdd:COG1127 224 GTP 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-220 |
6.59e-41 |
|
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: 139.93 E-value: 6.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGN----RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSA--- 77
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGlDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 -KHIAMLPQHSTLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVMTql 154
Cdd:cd03255 81 rRHIGFVFQSFNL-LPDLtALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNH-YPSeLSGGQQQRVAIARALA-- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 155 hqsGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASqYADRLVLLHNGKL 220
Cdd:cd03255 157 ---NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-226 |
1.56e-40 |
|
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: 139.56 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGkqkHDWEPEKSA------KHIA 81
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpDSGEVLIDG---EDISGLSEAelyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHSTLtfpFLAREVVELGAIPLS----LSNKETTKLALHYMEQtdV-LHLAESLYPS-LSGGEKQRLHLARVMtqlh 155
Cdd:cd03261 81 MLFQSGAL---FDSLTVFENVAFPLRehtrLSEEEIREIVLEKLEA--VgLRGAEDLYPAeLSGGMKKRVALARAL---- 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 156 qSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:cd03261 152 -ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
9-249 |
3.92e-40 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 139.54 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLcgeisSNHH------ITYFGKQKHDWEPEKSAKHIAM 82
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-----GRHQppsegeILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLTFPFLAREVVELGAIP-------LSLSNKETTKLALHYMeqtDVLHLAESLYPSLSGGEKQRLHLARVMTQlh 155
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIGRYPwhgalgrFGAADREKVEEAISLV---GLKPLAHRLVDSLSGGERQRAWIAMLVAQ-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 156 qsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERI 235
Cdd:PRK10575 165 ---DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETL 241
|
250
....*....|....
gi 491527411 236 EQVYGYRSIVTKHP 249
Cdd:PRK10575 242 EQIYGIPMGILPHP 255
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-221 |
2.79e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 135.94 E-value: 2.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGN----RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSA 77
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSgEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 K----HIAMLPQHSTLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVM 151
Cdd:COG1136 82 RlrrrHIGFVFQFFNL-LPELtALENVALPLLLAGVSRKERRERARELLERVGLGDRLDH-RPSqLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 152 tqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASqYADRLVLLHNGKLV 221
Cdd:COG1136 160 -----VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIV 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-248 |
3.22e-38 |
|
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: 134.06 E-value: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI--SSNHHITYFGKQKHDWEPEKSAKHIAM 82
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLppTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLTFP--FLAREVVELGA-----IPLSLSnKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLAR-VMTQl 154
Cdd:COG1119 83 VSPALQLRFPrdETVLDVVLSGFfdsigLYREPT-DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARaLVKD- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 155 hqsgeKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSER 234
Cdd:COG1119 161 -----PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSEN 235
|
250
....*....|....
gi 491527411 235 IEQVYGYRSIVTKH 248
Cdd:COG1119 236 LSEAFGLPVEVERR 249
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-219 |
3.56e-38 |
|
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: 131.93 E-value: 3.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGK--QKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPDSGSILIDGEdlTDLEDELPPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPFL-AREVVELGaiplslsnkettklalhymeqtdvlhlaeslypsLSGGEKQRLHLARVMTQlhqsgEKRILM 164
Cdd:cd03229 84 DFAL-FPHLtVLENIALG----------------------------------LSGGQQQRVALARALAM-----DPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 165 LDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-234 |
6.15e-38 |
|
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: 138.88 E-value: 6.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNR-----VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKS 76
Cdd:COG1123 258 EPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSgSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 77 ---AKHIAMLPQH--STLtFPFL--AREVVElgaiPL----SLSNKETTKLALHYMEQtdvLHLAESL---YP-SLSGGE 141
Cdd:COG1123 338 relRRRVQMVFQDpySSL-NPRMtvGDIIAE----PLrlhgLLSRAERRERVAELLER---VGLPPDLadrYPhELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 142 KQRLHLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG1123 410 RQRVAIARAL-----ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
250
....*....|...
gi 491527411 222 CDDTPWNALTSER 234
Cdd:COG1123 485 EDGPTEEVFANPQ 497
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
1.75e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.52 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTY----GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKqkhdwEPEK 75
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGlEKPTSGEVLVDGK-----PVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 SAKHIAMLPQHSTLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQtdvLHLA--ESLYPS-LSGGEKQRLHLARVM 151
Cdd:COG1116 78 PGPDRGVVFQEPAL-LPWLtVLDNVALGLELRGVPKAERRERARELLEL---VGLAgfEDAYPHqLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 152 TQlhqsgEKRILMLDEPTSALD----LAHQHNTLKIARETakaqNAAVVVVLHDLNLASQYADRLVLLHNG 218
Cdd:COG1116 154 AN-----DPEVLLMDEPFGALDaltrERLQDELLRLWQET----GKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-170 |
2.17e-37 |
|
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: 128.92 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPEKSAKHIAMLPQHSTLtFPFL-AREV 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQL-FPRLtVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 99 VELGAIPLSLSNKETTKLALHYMEQTDVLHLAESL----YPSLSGGEKQRLHLARVMtqlhqSGEKRILMLDEPTS 170
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARAL-----LTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-221 |
2.64e-37 |
|
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: 130.72 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsaKHIAMLPQHS 87
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGlERPDSGEILIDGRDVTGVPPER--RNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVMTQlhqsgEKRILML 165
Cdd:cd03259 82 AL-FPHLtVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNR-YPHeLSGGQQQRVALARALAR-----EPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 166 DEPTSALDlahQHNTLKIARETAKAQNAA---VVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03259 155 DEPLSALD---AKLREELREELKELQRELgitTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-217 |
3.02e-37 |
|
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: 130.67 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNR----VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPeksakHI 80
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERpTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQTDVLHlAESLYPS-LSGGEKQRLHLARVMTQlhqsg 158
Cdd:cd03293 76 GYVFQQDAL-LPWLtVLDNVALGLELQGVPKAEARERAEELLELVGLSG-FENAYPHqLSGGMRQRVALARALAV----- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 159 EKRILMLDEPTSALD----LAHQHNTLKIARETAKaqnaAVVVVLHDLNLASQYADRLVLLHN 217
Cdd:cd03293 149 DPDVLLLDEPFSALDaltrEQLQEELLDIWRETGK----TVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-234 |
3.77e-37 |
|
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: 136.96 E-value: 3.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTY--GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHH----ITYFGKQKHDWEPEKS 76
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRisgeVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 77 AKHIAMLPQH--STLTFPFLAREVVElGAIPLSLSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVMtq 153
Cdd:COG1123 82 GRRIGMVFQDpmTQLNPVTVGDQIAE-ALENLGLSRAEARARVLELLEAVGLERRLDR-YPHqLSGGQRQRVAIAMAL-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 154 lhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSE 233
Cdd:COG1123 158 ---ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
.
gi 491527411 234 R 234
Cdd:COG1123 235 Q 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-226 |
4.15e-37 |
|
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: 130.63 E-value: 4.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPEKSAKH-IAML 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtFPFL-AREVVELGA----------IPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMt 152
Cdd:cd03219 81 FQIPRL-FPELtVLENVMVAAqartgsglllARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 153 qlhqSGEKRILMLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:cd03219 159 ----ATDPKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-221 |
5.48e-37 |
|
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: 130.32 E-value: 5.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNR----VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSA- 77
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGllKPTSGS-IIFDGKDLLKLSRRLRKi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 --KHIAMLPQHSTLTFPFL---AREVVELGAIPLSLSNKETTKLALhyMEQTDVLHLAESL---YPS-LSGGEKQRLHLA 148
Cdd:cd03257 80 rrKEIQMVFQDPMSSLNPRmtiGEQIAEPLRIHGKLSKKEARKEAV--LLLLVGVGLPEEVlnrYPHeLSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 149 RVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03257 158 RAL-----ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-221 |
9.65e-37 |
|
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: 130.31 E-value: 9.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYG----NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHI 80
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSgEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLTF-PF--LAREVVElgaiPLSLSNK-ETTKLALHYMEQtdvLHLAESL---YP-SLSGGEKQRLHLARVMt 152
Cdd:COG1124 82 QMVFQDPYASLhPRhtVDRILAE----PLRIHGLpDREERIAELLEQ---VGLPPSFldrYPhQLSGGQRQRVAIARAL- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 153 qlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG1124 154 ----ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
1.18e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.53 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsaKH 79
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPDSGRILLDGRDVTGLPPEK--RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtFPFL-AREVVelgAIPLS---LSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLAR--VMt 152
Cdd:COG3842 79 VGMVFQDYAL-FPHLtVAENV---AFGLRmrgVPKAEIRARVAELLELVGLEGLADR-YPHqLSGGQQQRVALARalAP- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 153 qlhqsgEKRILMLDEPTSALDLAH----QHNTLKIARETakaqNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:COG3842 153 ------EPRVLLLDEPLSALDAKLreemREELRRLQREL----GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTP 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-219 |
1.84e-36 |
|
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: 127.11 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNR--VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03228 4 KNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSgEILIDGVDLRDLDLESLRKNIAYVPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPFLAREVVelgaiplslsnkettklalhymeqtdvlhlaeslypsLSGGEKQRLHLARVMtqLHQSgekRILML 165
Cdd:cd03228 84 DPFL-FSGTIRENI-------------------------------------LSGGQRQRIAIARAL--LRDP---PILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 166 DEPTSALDL---AHQHNTLKiaretAKAQNAAVVVVLHDLNLAsQYADRLVLLHNGK 219
Cdd:cd03228 121 DEATSALDPeteALILEALR-----ALAKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-226 |
2.05e-36 |
|
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: 128.39 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQH 86
Cdd:cd03263 4 RNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 87 STLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTqlhqsGEKRILML 165
Cdd:cd03263 84 DAL-FDELtVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALI-----GGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 166 DEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-221 |
9.16e-36 |
|
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: 126.91 E-value: 9.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH------HITYFGKQKHDWE--PEKSAKHI 80
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdegEVLLDGKDIYDLDvdVLELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtFPFLAREVVELGA-IPLSLSNKET--------TKLALHyMEQTDVLHLAeslypSLSGGEKQRLHLARVM 151
Cdd:cd03260 84 GMVFQKPNP-FPGSIYDNVAYGLrLHGIKLKEELderveealRKAALW-DEVKDRLHAL-----GLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 152 tqlhqSGEKRILMLDEPTSALDlahQHNTLKIARETAK-AQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03260 157 -----ANEPEVLLLDEPTSALD---PISTAKIEELIAElKKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-226 |
1.03e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.03 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSA--KHIAMLP 84
Cdd:COG1126 5 ENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLleEPDSGT-ITVDGEDLTDSKKDINKlrRKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLtFPFL-AREVVELGaiPLS---LSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLAR--VMtqlhqs 157
Cdd:COG1126 84 QQFNL-FPHLtVLENVTLA--PIKvkkMSKAEAEERAMELLERVGLADKADA-YPAqLSGGQQQRVAIARalAM------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 158 gEKRILMLDEPTSALD-------------LAHQHNTLkiaretakaqnaavVVVLHDLNLASQYADRLVLLHNGKLVCDD 224
Cdd:COG1126 154 -EPKVMLFDEPTSALDpelvgevldvmrdLAKEGMTM--------------VVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
..
gi 491527411 225 TP 226
Cdd:COG1126 219 PP 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
9-220 |
1.61e-35 |
|
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: 126.11 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKQ--KHDWEPEKSAKHIAMLP 84
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLleEPDSG-TIIIDGLKltDDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLtFPFL-AREVVELGAIP-LSLSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVMTQlhqsgEKR 161
Cdd:cd03262 83 QQFNL-FPHLtVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADA-YPAqLSGGQQQRVAIARALAM-----NPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 162 ILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-215 |
4.02e-35 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 124.27 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 15 YGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITyfgkqkhdwepEKSAKHIAMLPQHSTL--TF 91
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVR-----------RAGGARVAYVPQRSEVpdSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 92 PFLAREVVELG----AIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDE 167
Cdd:NF040873 71 PLTVRDLVAMGrwarRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQ-----EADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491527411 168 PTSALDL-AHQHNTLKIARETakAQNAAVVVVLHDLNLASQyADRLVLL 215
Cdd:NF040873 146 PTTGLDAeSRERIIALLAEEH--ARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-221 |
8.34e-34 |
|
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: 119.84 E-value: 8.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH-IAML 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSgEILVDGKEVSFASPRDARRAgIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQhstltfpflarevvelgaiplslsnkettklalhymeqtdvlhlaeslypsLSGGEKQRLHLARVMtqlhqSGEKRIL 163
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARAL-----ARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 164 MLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-226 |
1.12e-33 |
|
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: 122.45 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH- 79
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSgRILFDGRDITGLPPHRIARLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtFPFL-AREVVELGA----------IPLSL-----SNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQ 143
Cdd:COG0411 81 IARTFQNPRL-FPELtVLENVLVAAharlgrgllaALLRLprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 144 RLHLARVMTqlhqsGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:COG0411 160 RLEIARALA-----TEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
...
gi 491527411 224 DTP 226
Cdd:COG0411 235 GTP 237
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-226 |
3.31e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.33 E-value: 3.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEISSNHHITYFGKQKHDwepeksaKHIA 81
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIagletpdSGRIVLNGRDLFTNLPPRE-------RRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHSTLtFPFL-AREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVMTQlhqsgE 159
Cdd:COG1118 79 FVFQHYAL-FPHMtVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADR-YPSqLSGGQRQRVALARALAV-----E 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 160 KRILMLDEPTSALDlAHQHNTL-KIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:COG1118 152 PEVLLLDEPFGALD-AKVRKELrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTP 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
8.70e-33 |
|
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: 125.26 E-value: 8.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH 79
Cdd:COG4988 333 GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSgSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtFPFLAREVVELGAIPLSlsnKETTKLALhymEQTDVLHLAESLyPS------------LSGGEKQRLHL 147
Cdd:COG4988 413 IAWVPQNPYL-FAGTIRENLRLGRPDAS---DEELEAAL---EAAGLDEFVAAL-PDgldtplgeggrgLSGGQAQRLAL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 148 ARVMtqLHQSgekRILMLDEPTSALDLAHQH---NTLKiaretAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCDD 224
Cdd:COG4988 485 ARAL--LRDA---PLLLLDEPTAHLDAETEAeilQALR-----RLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
..
gi 491527411 225 TP 226
Cdd:COG4988 554 TH 555
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
9-253 |
2.31e-32 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 118.88 E-value: 2.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMtyGNRvvLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQHST 88
Cdd:PRK03695 4 NDVAV--STR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 89 LTFpflarevvelgAIP----LSLS-----NKETTKLALHYMEQ----TDVLHLAESlypSLSGGEKQRLHLARVMTQLH 155
Cdd:PRK03695 80 PPF-----------AMPvfqyLTLHqpdktRTEAVASALNEVAEalglDDKLGRSVN---QLSGGEWQRVRLAAVVLQVW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 156 QSG--EKRILMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSE 233
Cdd:PRK03695 146 PDInpAGQLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
250 260
....*....|....*....|...
gi 491527411 234 RIEQVYGY---RSIVTKHPTLDF 253
Cdd:PRK03695 225 NLAQVFGVnfrRLDVEGHPMLIS 247
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-226 |
8.03e-32 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 118.65 E-value: 8.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 14 TYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGkqkHDW--EPEKSAKHIAMLPQHSTLT 90
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAG---YDVvrEPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 91 FPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqLHQSgekRILMLDEPTS 170
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASL--IHQP---DVLFLDEPTT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 171 ALDlAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:TIGR01188 154 GLD-PRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTP 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-223 |
1.40e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.28 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH- 79
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSgEILLDGEPVRFRSPRDAQAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtFP--------FLAREVVELGAIplslSNKETTKLALHYMEQtdvLHLAESlyP-----SLSGGEKQRLH 146
Cdd:COG1129 81 IAIIHQELNL-VPnlsvaeniFLGREPRRGGLI----DWRAMRRRARELLAR---LGLDID--PdtpvgDLSVAQQQLVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 147 LARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:COG1129 151 IARAL-----SRDARVLILDEPTASLTEREVERLFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
9-241 |
8.96e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.08 E-value: 8.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVldDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKH-DWEPEKsaKHIAMLPQHS 87
Cdd:COG3840 5 DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtALPPAE--RPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFL-AREVVELGAIP-LSLSNKETTKLAlHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILML 165
Cdd:COG3840 81 NL-FPHLtVAQNIGLGLRPgLKLTAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR-----KRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 166 DEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVYGY 241
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
9-226 |
1.02e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLK------------LLCGEISSNhhityfGKQKHDWEPEKS 76
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKVN------DPKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 77 AkhiAMLPQHSTLtFPFL-AREVVELGAIPL-SLSNKETTKLAlhyMEQTDVLHLAESL--YPS-LSGGEKQRLHLARVM 151
Cdd:PRK09493 79 A---GMVFQQFYL-FPHLtALENVMFGPLRVrGASKEEAEKQA---RELLAKVGLAERAhhYPSeLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 152 TQlhqsgeKRILML-DEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK09493 152 AV------KPKLMLfDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-221 |
1.05e-30 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 113.44 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGeVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTqlhqsGEKRILML 165
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV-----GDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 166 DEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-226 |
7.25e-30 |
|
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: 111.31 E-value: 7.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI---SSNHHItyFGkqkHDW--EPEKSAKHIAML 83
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLkptSGRATV--AG---HDVvrEPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqLHqsgEKRIL 163
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL--VH---RPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 164 MLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-220 |
8.25e-30 |
|
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: 110.00 E-value: 8.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYG--NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAM 82
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSgRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLtFPflarevvelGAIplslsnkettklalhymeqtdvlhlAESLypsLSGGEKQRLHLARVMTqlhqsGEKRI 162
Cdd:cd03246 81 LPQDDEL-FS---------GSI-------------------------AENI---LSGGQRQRLGLARALY-----GNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 163 LMLDEPTSALDLAHQHnTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKL 220
Cdd:cd03246 118 LVLDEPNSHLDVEGER-ALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
9-221 |
8.76e-30 |
|
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: 111.52 E-value: 8.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNR----VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGK---QKHDWEPEKSAKHI 80
Cdd:cd03258 5 KNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGlERPTSGSVLVDGTdltLLSGKELRKARRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtfpFLAREVVELGAIPLSL---SNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVMtqlhq 156
Cdd:cd03258 85 GMIFQHFNL---LSSRTVFENVALPLEIagvPKAEIEERVLELLELVGLEDKADA-YPAqLSGGQKQRVGIARAL----- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 157 SGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-226 |
2.16e-29 |
|
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: 116.09 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYG--NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:COG2274 477 ENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSgRILIDGIDLRQIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPflarevvelGAIP--LSLSNKETTKLALHY-MEQTDVLHLAESLyP------------SLSGGEKQRLHLARV 150
Cdd:COG2274 557 DVFL-FS---------GTIRenITLGDPDATDEEIIEaARLAGLHDFIEAL-PmgydtvvgeggsNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 151 MtqLHQSgekRILMLDEPTSALDLAHQH---NTLKiaretAKAQNAAVVVVLHDLNLAsQYADRLVLLHNGKLVCDDTP 226
Cdd:COG2274 626 L--LRNP---RILILDEATSALDAETEAiilENLR-----RLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTH 693
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-226 |
3.61e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 112.47 E-value: 3.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLsgKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKQKHDWEPEKsaK 78
Cdd:COG3839 1 MASLEL--ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGleDPTSG-EILIGGRDVTDLPPKD--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIAMLPQHSTLtFPFL-AREVVelgAIPLSLS-------NKETTKLAlhymeqtDVLHLAESL--YPS-LSGGEKQRLHL 147
Cdd:COG3839 76 NIAMVFQSYAL-YPHMtVYENI---AFPLKLRkvpkaeiDRRVREAA-------ELLGLEDLLdrKPKqLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 148 ARVMTQlhqsgEKRILMLDEPTSALDlAHqhntLKIA--RETAKAQ---NAAVVVVLHDLNLASQYADRLVLLHNGKLVC 222
Cdd:COG3839 145 GRALVR-----EPKVFLLDEPLSNLD-AK----LRVEmrAEIKRLHrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQ 214
|
....
gi 491527411 223 DDTP 226
Cdd:COG3839 215 VGTP 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-225 |
5.94e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.13 E-value: 5.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG---EISSNH---HITYFGKQ--KHDWEPE 74
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGARvegEILLDGEDiyDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 KSAKHIAMLPQHSTLtFP--------FLAR-----------EVVElgaipLSLsnketTKLALhYMEQTDVLHlaESLYp 135
Cdd:COG1117 89 ELRRRVGMVFQKPNP-FPksiydnvaYGLRlhgikskseldEIVE-----ESL-----RKAAL-WDEVKDRLK--KSAL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 136 SLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDlahQHNTLKIaRETAK--AQNAAVVVVLHDLNLASQYADRLV 213
Cdd:COG1117 154 GLSGGQQQRLCIARALAV-----EPEVLLMDEPTSALD---PISTAKI-EELILelKKDYTIVIVTHNMQQAARVSDYTA 224
|
250
....*....|...
gi 491527411 214 LLHNGKLV-CDDT 225
Cdd:COG1117 225 FFYLGELVeFGPT 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-226 |
7.16e-29 |
|
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: 114.48 E-value: 7.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY--GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:COG4987 337 EDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSgSITLGGVDLRDLDEDDLRRRIAVVPQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtfpFLA--REvvelgaiPLSLSNKETTKLAL-HYMEQTDVLHLAESLyP------------SLSGGEKQRLHLARV 150
Cdd:COG4987 417 RPHL---FDTtlRE-------NLRLARPDATDEELwAALERVGLGDWLAAL-PdgldtwlgeggrRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 151 MtqLHQSgekRILMLDEPTSALDlahqhntlkiaRETAKA---------QNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:COG4987 486 L--LRDA---PILLLDEPTEGLD-----------AATEQAlladllealAGRTVLLITHRLAGLER-MDRILVLEDGRIV 548
|
....*
gi 491527411 222 CDDTP 226
Cdd:COG4987 549 EQGTH 553
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-226 |
1.09e-28 |
|
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: 108.29 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI-SSNHHITYFGKQKHDWEPEKSAKH-IAML 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLpPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtFPFLA-REVVELGAIPLSLSNKETTklalhyMEQtdVLhlaeSLYP-----------SLSGGEKQRLHLARVM 151
Cdd:cd03224 81 PEGRRI-FPELTvEENLLLGAYARRRAKRKAR------LER--VY----ELFPrlkerrkqlagTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 152 TqlhqsGEKRILMLDEPTSALdlahqhnTLKIARETA------KAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDT 225
Cdd:cd03224 148 M-----SRPKLLLLDEPSEGL-------APKIVEEIFeairelRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
.
gi 491527411 226 P 226
Cdd:cd03224 216 A 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-214 |
1.73e-28 |
|
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: 107.56 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDwEPEKSAKHIAML 83
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAgEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtFPFL-AREVVELGAiplSLSNKETTKLALH-YMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTqlhqsGEKR 161
Cdd:COG4133 81 GHADGL-KPELtVRENLRFWA---ALYGLRADREAIDeALEAVGLAGLADLPVRQLSAGQKRRVALARLLL-----SPAP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 162 ILMLDEPTSALDlahQHNTLKIAR--ETAKAQNAAVVVVLHDLnLASQYADRLVL 214
Cdd:COG4133 152 LWLLDEPFTALD---AAGVALLAEliAAHLARGGAVLLTTHQP-LELAAARVLDL 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-227 |
2.80e-28 |
|
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: 107.71 E-value: 2.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsaKHIAMLPQHS 87
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGfETPTSGEILLDGKDITNLPPHK--RPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFLarEVVELGAIPLSLSNKETTKLALHYMEQTDVLHLA--ESLYPS-LSGGEKQRLHLAR--VMtqlhqsgEKRI 162
Cdd:cd03300 82 AL-FPHL--TVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEgyANRKPSqLSGGQQQRVAIARalVN-------EPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 163 LMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPW 227
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-239 |
2.83e-28 |
|
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: 107.63 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEP--EKSAKHIAML 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtFPFLARE-----VVELgaipLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsg 158
Cdd:cd03218 81 PQEASI-FRKLTVEenilaVLEI----RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALAT----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 159 EKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQV 238
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKV 229
|
.
gi 491527411 239 Y 239
Cdd:cd03218 230 Y 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
9-221 |
3.11e-28 |
|
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: 106.92 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDwePEKSAKHIAMLPQHS 87
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKpDSGEITFDGKSYQK--NIEALRRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLTFPFLAREVVELGAIPLSLSNKETtklalhyMEQTDVLHLAES---LYPSLSGGEKQRLHLARVMTqlhqsGEKRILM 164
Cdd:cd03268 82 GFYPNLTARENLRLLARLLGIRKKRI-------DEVLDVVGLKDSakkKVKGFSLGMKQRLGIALALL-----GNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 165 LDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-221 |
5.46e-28 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 106.59 E-value: 5.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISS----NHHITYFGKQKHdwePEKSAKHIAMLPQHSTLTFPF 93
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 94 LAREVVELGAI---PLSLSNKETTKL-ALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPT 169
Cdd:cd03234 97 TVRETLTYTAIlrlPRKSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW-----DPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 170 SALDLAHQHNTLKIARETAKaQNAAVVVVLH----DLnlaSQYADRLVLLHNGKLV 221
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLAR-RNRIVILTIHqprsDL---FRLFDRILLLSSGEIV 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-239 |
7.90e-28 |
|
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: 106.60 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH-IAM 82
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSgSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLtFPFL-AREVVELGAIPLSLSNKETTKLALHYmeqtdvlhlaeSLYP-----------SLSGGEKQRLHLARV 150
Cdd:COG0410 83 VPEGRRI-FPSLtVEENLLLGAYARRDRAEVRADLERVY-----------ELFPrlkerrrqragTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 151 -MTqlhqsgEKRILMLDEPTsaLDLAHqhntlKIARE------TAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:COG0410 151 lMS------RPKLLLLDEPS--LGLAP-----LIVEEifeiirRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLE 217
|
250
....*....|....*.
gi 491527411 224 DTPWNALTSERIEQVY 239
Cdd:COG0410 218 GTAAELLADPEVREAY 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
10-226 |
9.61e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 9.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGK---QKHDWEpeksaKHIAMLPQ 85
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGlEHQTSGHIRFHGTdvsRLHARD-----RKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtfpFLAREVVELGAIPLSL-------SNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLARVMtqlhqS 157
Cdd:PRK10851 82 HYAL---FRHMTVFDNIAFGLTVlprrerpNAAAIKAKVTQLLEMVQLAHLADR-YPAqLSGGQKQRVALARAL-----A 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 158 GEKRILMLDEPTSALD----------LAHQHNTLKIARetakaqnaavVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK10851 153 VEPQILLLDEPFGALDaqvrkelrrwLRQLHEELKFTS----------VFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-221 |
1.03e-27 |
|
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: 105.80 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsaKHIAMLPQHS 87
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGlEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFLAreVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESL--YPS-LSGGEKQRLHLARVMTqlhqsGEKRILM 164
Cdd:cd03301 82 AL-YPHMT--VYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLdrKPKqLSGGQRQRVALGRAIV-----REPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 165 LDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-221 |
1.12e-27 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE---------ISSNHHITYFgkqkhdwepe 74
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElepdsgtvkLGETVKIGYF---------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 ksAKHIAMLPQHSTLtfpflaREVVElgaiplSLSNKETTKLALHYMEQ-----TDVLHLAEslypSLSGGEKQRLHLAR 149
Cdd:COG0488 384 --DQHQEELDPDKTV------LDELR------DGAPGGTEQEVRGYLGRflfsgDDAFKPVG----VLSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 150 VMTQlhqsgEKRILMLDEPTSALDLahqhntlkiarETAKAQNAA-------VVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG0488 446 LLLS-----PPNVLLLDEPTNHLDI-----------ETLEALEEAlddfpgtVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
9-253 |
1.68e-27 |
|
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: 105.88 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsaKHIAMLPQHS 87
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGlERPDSGTILFGGEDATDVPVQE--RNVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFLA-REVVELG--AIPLSLSNKETTKLAlHYMEQTDVLHLA--ESLYPS-LSGGEKQRLHLARVMtqlhqSGEKR 161
Cdd:cd03296 84 AL-FRHMTvFDNVAFGlrVKPRSERPPEAEIRA-KVHELLKLVQLDwlADRYPAqLSGGQRQRVALARAL-----AVEPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 162 ILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGklvcddtpwnaltseRIEQVyGY 241
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG---------------RIEQV-GT 220
|
250
....*....|..
gi 491527411 242 RSIVTKHPTLDF 253
Cdd:cd03296 221 PDEVYDHPASPF 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-226 |
2.61e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWepekSAKHIAMLPQHSTLTFP------FL 94
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY----SRKGLMKLRESVGMVFQdpdnqlFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 95 AR--EVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSAL 172
Cdd:PRK13636 98 ASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM-----EPKVLVLDEPTAGL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 173 DLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-221 |
2.91e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 109.35 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH 79
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSgEILIDGKPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 -IAMLPQHSTLtFP--------FLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAEslypSLSGGEKQRLHLARV 150
Cdd:COG3845 81 gIGMVHQHFML-VPnltvaeniVLGLEPTKGGRLDRKAARARIRELSERYGLDVDPDAKVE----DLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 151 mtqLHQsgEKRILMLDEPTSAL------DLahqhntLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG3845 156 ---LYR--GARILILDEPTAVLtpqeadEL------FEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
9-224 |
1.18e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.21 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAK---HIAML 83
Cdd:COG2884 5 ENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSgQVLVNGQDLSRLKRREIPYlrrRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQhstlTFPFLA-REVVELGAIPLSL---SNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLAR--VMtqlhqs 157
Cdd:COG2884 85 FQ----DFRLLPdRTVYENVALPLRVtgkSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARalVN------ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 158 gEKRILMLDEPTSALDlahQHNTLKIAR--ETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDD 224
Cdd:COG2884 155 -RPELLLADEPTGNLD---PETSWEIMEllEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-232 |
1.80e-26 |
|
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: 103.15 E-value: 1.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEISSNhhityfGKQKHDWEPEKSAKHI 80
Cdd:cd03295 4 ENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInrlieptSGEIFID------GEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtFPFlaREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAES----LYPS-LSGGEKQRLHLARVMtqlh 155
Cdd:cd03295 78 GYVIQQIGL-FPH--MTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefadRYPHeLSGGQQQRVGVARAL---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 156 qSGEKRILMLDEPTSALD----LAHQHNTLKIARETAKAqnaaVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALT 231
Cdd:cd03295 151 -AADPPLLLMDEPFGALDpitrDQLQEEFKRLQQELGKT----IVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
.
gi 491527411 232 S 232
Cdd:cd03295 226 S 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-215 |
2.80e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.99 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSNhhityfGKQKHDWEPEK 75
Cdd:TIGR02857 320 SSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLgfvdpteGSIAVN------GVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 SAKHIAMLPQHSTLTFPFLAREVV--ELGAIPLSLSNKeTTKLALHYMEQTDVLHLAESLYPS---LSGGEKQRLHLARV 150
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFAGTIAENIRlaRPDASDAEIREA-LERAGLDEFVAALPQGLDTPIGEGgagLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 151 MtqLHQSGekrILMLDEPTSALDLAHQHNTLKIARETakAQNAAVVVVLHDLNLASQyADRLVLL 215
Cdd:TIGR02857 473 F--LRDAP---LLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-221 |
5.27e-26 |
|
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: 101.20 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSnhhitYFGKQKHDWEPEKSAK--HIAML 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP-----DSGEVLFDGKPLDIAArnRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtfpFLAREVVE----LGAIPlSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLarVMTQLHQSge 159
Cdd:cd03269 76 PEERGL---YPKMKVIDqlvyLAQLK-GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQF--IAAVIHDP-- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491527411 160 kRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03269 148 -ELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-221 |
8.89e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 105.63 E-value: 8.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:COG1132 343 ENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRfyDPTSG-RILIDGVDIRDLTLESLRRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPFLAREVVELGAIPLSLsnkETTKLALhymEQTDVLHLAESLyP------------SLSGGEKQRLHLARVMtq 153
Cdd:COG1132 422 DTFL-FSGTIRENIRYGRPDATD---EEVEEAA---KAAQAHEFIEAL-PdgydtvvgergvNLSGGQRQRIAIARAL-- 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 154 LHQSgekRILMLDEPTSALDLAHQHntlKIARETAK-AQNAAVVVVLHDLNLAsQYADRLVLLHNGKLV 221
Cdd:COG1132 492 LKDP---PILILDEATSALDTETEA---LIQEALERlMKGRTTIVIAHRLSTI-RNADRILVLDDGRIV 553
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-244 |
1.04e-25 |
|
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: 100.87 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGNrVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKsaKHIAMLPQHST 88
Cdd:cd03299 5 NLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSgKILLNGKDITNLPPEK--RDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 89 LtFPFLA-REVVELGAIPLSLSNKETTKlalHYMEQTDVLHLAESL--YP-SLSGGEKQRLHLARVMTQlhqsgEKRILM 164
Cdd:cd03299 82 L-FPHMTvYKNIAYGLKKRKVDKKEIER---KVLEIAEMLGIDHLLnrKPeTLSGGEQQRVAIARALVV-----NPKILL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 165 LDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNAL---TSERIEQVYGY 241
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFkkpKNEFVAEFLGF 232
|
...
gi 491527411 242 RSI 244
Cdd:cd03299 233 NNI 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-221 |
1.21e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.11 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDwepeKSAKHIAML 83
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSgEVLWDGEPLDP----EDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtFP---------FLARevveL-GaiplsLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLArvMTQ 153
Cdd:COG4152 77 PEERGL-YPkmkvgeqlvYLAR----LkG-----LSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI--AAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 154 LHqsgEKRILMLDEPTSALDLAHQhNTLK-IAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG4152 145 LH---DPELLILDEPFSGLDPVNV-ELLKdVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-221 |
1.92e-25 |
|
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: 99.68 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIR---AGEVTALLGPNGAGKSTLLKLLCG-------EISSNHHITYFGKQKHDWEPEKsaKHIAMLPQHSTLt 90
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGlekpdggTIVLNGTVLFDSRKKINLPPQQ--RKIGLVFQQYAL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 91 FPFL-AREVVELGaiplsLSNKETTKLALHYMEQTDVLHLAESL--YPS-LSGGEKQRLHLARVMTQlhqsgEKRILMLD 166
Cdd:cd03297 87 FPHLnVRENLAFG-----LKRKRNREDRISVDELLDLLGLDHLLnrYPAqLSGGEKQRVALARALAA-----QPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 167 EPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-227 |
1.99e-25 |
|
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: 100.97 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY--GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFG----KQKHDWEpekSAKHIA 81
Cdd:TIGR04520 4 ENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLpTSGKVTVDGldtlDEENLWE---IRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHstltfP---FLAREV---VELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlh 155
Cdd:TIGR04520 81 MVFQN-----PdnqFVGATVeddVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM-- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491527411 156 qsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTPW 227
Cdd:TIGR04520 154 ---RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPR 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-239 |
2.22e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.10 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH-IAM 82
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSgRIFLDGEDITHLPMHKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHST----LTfpflARE----VVELgaipLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtql 154
Cdd:COG1137 83 LPQEASifrkLT----VEDnilaVLEL----RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 155 hqSGEKRILMLDEPTSALD-------------LAHQ--------HNtlkiARETakaqnaavvvvlhdLNLasqyADRLV 213
Cdd:COG1137 152 --ATNPKFILLDEPFAGVDpiavadiqkiirhLKERgigvlitdHN----VRET--------------LGI----CDRAY 207
|
250 260
....*....|....*....|....*.
gi 491527411 214 LLHNGKLVCDDTPWNALTSERIEQVY 239
Cdd:COG1137 208 IISEGKVLAEGTPEEILNNPLVRKVY 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-220 |
2.28e-25 |
|
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: 99.40 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVV-LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPEKSAK---HIAML 83
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDVSDLRGRAIPYlrrKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtfpFLAREVVELGAIPLSLSN---KETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEK 160
Cdd:cd03292 84 FQDFRL---LPDRNVYENVAFALEVTGvppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVN-----SP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAKAqNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-244 |
2.65e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.47 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLK----LLCGEISSNHHITYFGKQ-----KHDWEP 73
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTvqregRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 74 EKSAKHIAMLPQHSTLTFPFLAREVVELGAIP--------LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRL 145
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALGstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 146 HLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDT 225
Cdd:PRK09984 162 AIARALMQ-----QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
250
....*....|....*....
gi 491527411 226 PwNALTSERIEQVygYRSI 244
Cdd:PRK09984 237 S-QQFDNERFDHL--YRSI 252
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-226 |
4.92e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.26 E-value: 4.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG----EISSNHHITYFG---KQKHDW 71
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpDDNPNSKITVDGitlTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 72 EPEKSAKHIAMLPQHStltfpFLAREV---VELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLA 148
Cdd:PRK13640 81 DIREKVGIVFQNPDNQ-----FVGATVgddVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 149 RVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTP 226
Cdd:PRK13640 156 GIL-----AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSP 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-239 |
5.65e-25 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 99.27 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEP--EKSAKHIAM 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHST----LTFPFLAREVVElgaIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsg 158
Cdd:TIGR04406 81 LPQEASifrkLTVEENIMAVLE---IRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALAT----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 159 EKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQV 238
Cdd:TIGR04406 153 NPKFILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV 231
|
.
gi 491527411 239 Y 239
Cdd:TIGR04406 232 Y 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-221 |
1.17e-24 |
|
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: 96.61 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYG--NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSaKHIAM 82
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQgEITLDGVPVSDLEKALS-SLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHstltfPFLArevvelgaiplslsnkETTklalhymeqtdvlhLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRI 162
Cdd:cd03247 80 LNQR-----PYLF----------------DTT--------------LRNNLGRRFSGGERQRLALARILLQ-----DAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 163 LMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLnLASQYADRLVLLHNGKLV 221
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLENGKII 175
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-221 |
1.38e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEIS-SNHHItyfgkqkhDWEPEKSAKHI 80
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiAGNHF--------DFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLTF------PFLAreVVE-LGAIP---LSLSNKETTKLAlhyMEQTDVLHLAE--SLYP-SLSGGEKQRLHL 147
Cdd:PRK11124 78 RELRRNVGMVFqqynlwPHLT--VQQnLIEAPcrvLGLSKDQALARA---EKLLERLRLKPyaDRFPlHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 148 ARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARE---TAKAQnaavVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK11124 153 ARALMM-----EPQVLLFDEPTAALDPEITAQIVSIIRElaeTGITQ----VIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-223 |
1.46e-24 |
|
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: 97.18 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 23 DINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPekSAKHIAMLPQHSTLtFPFLAREV-VE 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVDVTAAPP--ADRPVSMLFQENNL-FAHLTVEQnVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 101 LGAIPlSLSNKETTKLALH-YMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHN 179
Cdd:cd03298 93 LGLSP-GLKLTAEDRQAIEvALARVGLAGLEKRLPGELSGGERQRVALARVLVR-----DKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491527411 180 TLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-213 |
2.19e-24 |
|
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: 97.12 E-value: 2.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 19 VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE-ISSNHHITYfgkqKHDWEP----EKSAKHIAMLPQHsTLTF-- 91
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNyLPDSGSILV----RHDGGWvdlaQASPREILALRRR-TIGYvs 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 92 PFL-------AREVVELGAIPLSLSNKETTKLALHYMEQtdvLHLAE---SLYPS-LSGGEKQRLHLARVMTqlhqsGEK 160
Cdd:COG4778 100 QFLrviprvsALDVVAEPLLERGVDREEARARARELLAR---LNLPErlwDLPPAtFSGGEQQRVNIARGFI-----ADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 161 RILMLDEPTSALDlahQHNTLKIAR--ETAKAQNAAVVVVLHDLNLASQYADRLV 213
Cdd:COG4778 172 PLLLLDEPTASLD---AANRAVVVEliEEAKARGTAIIGIFHDEEVREAVADRVV 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-221 |
2.23e-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: 101.36 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 16 GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQHSTLtFP-- 92
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAgSVRLDGADLSQWDREELGRHIGYLPQDVEL-FDgt 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 93 -------FL---AREVVElgaiplslsnkeTTKLA-LHYMeqtdVLHL--------AESLYPsLSGGEKQRLHLARVMTq 153
Cdd:COG4618 422 iaeniarFGdadPEKVVA------------AAKLAgVHEM----ILRLpdgydtriGEGGAR-LSGGQRQRIGLARALY- 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 154 lhqsGEKRILMLDEPTSALD-LAHQHntLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:COG4618 484 ----GDPRLVVLDEPNSNLDdEGEAA--LAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQ 545
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-219 |
2.32e-24 |
|
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: 94.82 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIssnhhityfgkqkhdwEPEKsakhiAMLPQ 85
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGEL----------------EPDE-----GIVTW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPflarevvelgaiplslsnkettklalhYMEQtdvlhlaeslypsLSGGEKQRLHLARVMtqlhqSGEKRILML 165
Cdd:cd03221 60 GSTVKIG---------------------------YFEQ-------------LSGGEKMRLALAKLL-----LENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 166 DEPTSALDLAhqhnTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:cd03221 95 DEPTNHLDLE----SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-220 |
7.70e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYfgkqkhdwepEKSAKhIAMLPQHS 87
Cdd:COG0488 2 ENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSgEVSI----------PKGLR-IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLTFPFLAREVVELGAIPL--------------SLSNKETTKLA--LHYMEQTDV-------------LHLAESLYP--- 135
Cdd:COG0488 71 PLDDDLTVLDTVLDGDAELraleaeleeleaklAEPDEDLERLAelQEEFEALGGweaearaeeilsgLGFPEEDLDrpv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 136 -SLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLahqhntlkiarETA-------KAQNAAVVVVLHD---LNl 204
Cdd:COG0488 151 sELSGGWRRRVALARALLS-----EPDLLLLDEPTNHLDL-----------ESIewleeflKNYPGTVLVVSHDryfLD- 213
|
250
....*....|....*.
gi 491527411 205 asQYADRLVLLHNGKL 220
Cdd:COG0488 214 --RVATRILELDRGKL 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-226 |
9.84e-24 |
|
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: 95.58 E-value: 9.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNR----VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEK 75
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGlDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 SAK----HIA-------MLPqhsTLTfpflAREVVelgAIPLSL-SNKETTKLALHYMEQTDVLHLAESlYPS-LSGGEK 142
Cdd:COG4181 84 RARlrarHVGfvfqsfqLLP---TLT----ALENV---MLPLELaGRRDARARARALLERVGLGHRLDH-YPAqLSGGEQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 143 QRLHLARVMtqlhqSGEKRILMLDEPTSALDlahQHNTLKIA---RETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGK 219
Cdd:COG4181 153 QRVALARAF-----ATEPAILFADEPTGNLD---AATGEQIIdllFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGR 223
|
....*..
gi 491527411 220 LVCDDTP 226
Cdd:COG4181 224 LVEDTAA 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
10-240 |
1.38e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.59 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQkhdwEPEK---SAKHIAMLPQ 85
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAgKITVLGVP----VPARarlARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILML 165
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN-----DPQLLIL 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 166 DEPTSALDLAHQHNTLKIAReTAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPwNALTSERIE----QVYG 240
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP-HALIDEHIGcqviEIYG 273
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-221 |
2.69e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 94.69 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-CGEISSNHHITYFGkQKHDWEPEKSAKHIAMLPQHS 87
Cdd:COG4161 6 KNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPDSGQLNIAG-HQFDFSQKPSEKAIRLLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLTF------PFLAreVVE-LGAIP---LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqs 157
Cdd:COG4161 85 GMVFqqynlwPHLT--VMEnLIEAPckvLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM---- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 158 gEKRILMLDEPTSALDLAHQHNTLKIARE---TAKAQnaavVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG4161 159 -EPQVLLFDEPTAALDPEITAQVVEIIRElsqTGITQ----VIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
9-223 |
4.96e-23 |
|
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: 93.42 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03245 6 RNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGlYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPFLaREVVELGAIPLS---------------LSNKETTKLALHYMEQTDvlhlaeslypSLSGGEKQRLHLARV 150
Cdd:cd03245 86 DVTLFYGTL-RDNITLGAPLADderilraaelagvtdFVNKHPNGLDLQIGERGR----------GLSGGQRQAVALARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 151 MtqLHQSgekRILMLDEPTSALDLAHQHNTLKIARETAKAQnaAVVVVLHDLNLAsQYADRLVLLHNGKLVCD 223
Cdd:cd03245 155 L--LNDP---PILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
7.43e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 94.29 E-value: 7.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAK 78
Cdd:PRK13632 4 KSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSgEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIAMLPQHSTLTFpflarevveLGA-----IPLSLSNK-----ETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLA 148
Cdd:PRK13632 84 KIGIIFQNPDNQF---------IGAtveddIAFGLENKkvppkKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 149 RVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTPWN 228
Cdd:PRK13632 155 SVLAL-----NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKE 228
|
....*..
gi 491527411 229 ALTSERI 235
Cdd:PRK13632 229 ILNNKEI 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-223 |
8.05e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.11 E-value: 8.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 25 NIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPeKSAKHIAMLPQHSTLtFPFLA-REVVELGA 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-PSRRPVSMLFQENNL-FSHLTvAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 104 IP-LSLSNKETTKLAlHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLK 182
Cdd:PRK10771 97 NPgLKLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVR-----EQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491527411 183 IARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-224 |
1.55e-22 |
|
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: 92.40 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 19 VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSNHHITYFGKQKHdwepeksAKHIA-MLPQHSTLT 90
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSgllqptsGEVRVAGLVPWKRRKKF-------LRRIGvVFGQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 91 FPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqLHqsgEKRILMLDEPTS 170
Cdd:cd03267 108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAAL--LH---EPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 171 ALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDD 224
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-226 |
2.22e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 94.63 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsaKH 79
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGfETPDSGRIMLDGQDITHVPAEN--RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtFPFLA-REVVELGAIPLSLSNKETTKL---ALHyMEQTDvlHLAESLYPSLSGGEKQRLHLARVMTQlh 155
Cdd:PRK09452 88 VNTVFQSYAL-FPHMTvFENVAFGLRMQKTPAAEITPRvmeALR-MVQLE--EFAQRKPHQLSGGQQQRVAIARAVVN-- 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 156 qsgEKRILMLDEPTSALD--LAHQ-HNTLK-IARETakaqNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK09452 162 ---KPKVLLLDESLSALDykLRKQmQNELKaLQRKL----GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-239 |
3.31e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.88 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEP--EKSAKHIAM 82
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLtFPFLA--REVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEK 160
Cdd:PRK10895 83 LPQEASI-FRRLSvyDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL-----AANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIArETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSERIEQVY 239
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-225 |
5.06e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 5.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL------------CGEISSNHHITYFGKQk 68
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 69 hdwEPEKSAKHIAMLPQHSTlTFPFLAREVVELGAIPLSLSNKETTKLALH--------YMEQTDVLHlAESLypSLSGG 140
Cdd:PRK14239 80 ---DTVDLRKEIGMVFQQPN-PFPMSIYENVVYGLRLKGIKDKQVLDEAVEkslkgasiWDEVKDRLH-DSAL--GLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 141 EKQRLHLARVMtqlhqSGEKRILMLDEPTSALD---LAHQHNTLKIARetakaQNAAVVVVLHDLNLASQYADRLVLLHN 217
Cdd:PRK14239 153 QQQRVCIARVL-----ATSPKIILLDEPTSALDpisAGKIEETLLGLK-----DDYTMLLVTRSMQQASRISDRTGFFLD 222
|
....*....
gi 491527411 218 GKLV-CDDT 225
Cdd:PRK14239 223 GDLIeYNDT 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-239 |
6.94e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI-SSNHHITYFGKQKHDWEPEKSAKH 79
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPrATSGRIVFDGKDITDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 -IAMLPQHSTLTFPFLAREVVELGAIplsLSNKEttklalHYMEQTD-VLHLAESLYP-------SLSGGEKQRLHLAR- 149
Cdd:PRK11614 81 aVAIVPEGRRVFSRMTVEENLAMGGF---FAERD------QFQERIKwVYELFPRLHErriqragTMSGGEQQMLAIGRa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 150 VMTQlhqsgeKRILMLDEPTSALD---LAHQHNTLKIAREtakaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK11614 152 LMSQ------PRLLLLDEPSLGLApiiIQQIFDTIEQLRE----QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTG 221
|
250
....*....|...
gi 491527411 227 WNALTSERIEQVY 239
Cdd:PRK11614 222 DALLANEAVRSAY 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-221 |
8.27e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 91.41 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTY---------GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPE 74
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 KSA---KHIAMLPQHSTLTF-PflAREVVELGAIPL----SLSNKETTKLALHYMEQTDV-LHLAESLYPSLSGGEKQRL 145
Cdd:TIGR02769 82 QRRafrRDVQLVFQDSPSAVnP--RMTVRQIIGEPLrhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 146 HLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:TIGR02769 160 NIARAL-----AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-221 |
8.89e-22 |
|
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: 90.37 E-value: 8.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYG-NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfyDVSSGS-ILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPFLAREVVELGAipLSLSNKETTKLALHYMEQTDVLHLAESlYPS--------LSGGEKQRLHLARVMTQlhqs 157
Cdd:cd03253 83 DTVL-FNDTIGYNIRYGR--PDATDEEVIEAAKAAQIHDKIMRFPDG-YDTivgerglkLSGGEKQRVAIARAILK---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 158 gEKRILMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:cd03253 155 -NPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-232 |
9.94e-22 |
|
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: 91.17 E-value: 9.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 16 GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKS-----AKHIAMLPQHSTLt 90
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVFQSFAL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 91 FPflAREVVELGAIPLSLSN---KETTKLALHYMEQTDvLHLAESLYPS-LSGGEKQRLHLARVMTQlhqsgEKRILMLD 166
Cdd:cd03294 114 LP--HRTVLENVAFGLEVQGvprAEREERAAEALELVG-LEGWEHKYPDeLSGGMQQRVGLARALAV-----DPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 167 EPTSALD----LAHQHNTLKIARETAKaqnaAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTS 232
Cdd:cd03294 186 EAFSALDplirREMQDELLRLQAELQK----TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-235 |
1.15e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.46 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISsnhHITYFGKQKHDWEPEKsAKHI 80
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP---HGTYEGEIIFEGEELQ-ASNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 ---------------AMLPQHSTLTFPFLAREVVELGAIPLSLSNKETTKLalhyMEQtdvLHLAESLYP---SLSGGEK 142
Cdd:PRK13549 77 rdteragiaiihqelALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKL----LAQ---LKLDINPATpvgNLGLGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 143 QRLHLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVC 222
Cdd:PRK13549 150 QLVEIAKAL-----NKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
250
....*....|...
gi 491527411 223 DDtPWNALTSERI 235
Cdd:PRK13549 224 TR-PAAGMTEDDI 235
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-226 |
1.76e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.46 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHD---WEPE 74
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLpEAGTITVGGMVLSEetvWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 KsakHIAMLPQHSTLTFpflarevveLGA-----IPLSLSNK--------ETTKLALHYMEQTDVLHLAESlypSLSGGE 141
Cdd:PRK13635 81 R---QVGMVFQNPDNQF---------VGAtvqddVAFGLENIgvpreemvERVDQALRQVGMEDFLNREPH---RLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 142 KQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:PRK13635 146 KQRVAIAGVLAL-----QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
|
....*
gi 491527411 222 CDDTP 226
Cdd:PRK13635 220 EEGTP 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-226 |
2.09e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.79 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHhityfGKQKHDwepekSAKHIAMLPQ--H 86
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDE-----GVIKRN-----GKLRIGYVPQklY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 87 STLTFPFLAREVVELgaiplslsnKETTKLA--LHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQLHQsgekrILM 164
Cdd:PRK09544 78 LDTTLPLTVNRFLRL---------RPGTKKEdiLPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQ-----LLV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491527411 165 LDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRlVLLHNGKLVCDDTP 226
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDE-VLCLNHHICCSGTP 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
10-221 |
5.49e-21 |
|
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: 91.72 E-value: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYG-NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQHs 87
Cdd:TIGR01193 478 DVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSgEILLNGFSLKDIDRHTLRQFINYLPQE- 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 tltfPFL------------AREVVE----LGAIPLSLSNKETTKLALHYmeQTDvlhLAESLYpSLSGGEKQRLHLARVM 151
Cdd:TIGR01193 557 ----PYIfsgsilenlllgAKENVSqdeiWAACEIAEIKDDIENMPLGY--QTE---LSEEGS-SISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDLAHQHntlKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:TIGR01193 627 LT-----DSKVLILDESTSNLDTITEK---KIVNNLLNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKII 687
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-226 |
6.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.12 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKST-------LLKLLCGEIS-SNHHITyfgkqkhdwePEKSAKHIAMLPQHSTLTFP 92
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTlmqhfnaLLKPSSGTITiAGYHIT----------PETGNKNLKKLRKKVSLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 93 F--------LAREVVELGAIPLSLSNKETTKLALHYMEQtdvLHLAESLYP----SLSGGEKQRLHLARVMTQlhqsgEK 160
Cdd:PRK13641 93 FpeaqlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKK---VGLSEDLISkspfELSGGQMRRVAIAGVMAY-----EP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAKAQNaAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASP 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-237 |
9.55e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 9.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSNHHITYFGKQKhDWEP 73
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINflekpseGSIVVNGQTINLVRDK-DGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 74 EKSAKH--------IAMLPQHSTL-TFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPS-LSGGEKQ 143
Cdd:PRK10619 80 KVADKNqlrllrtrLTMVFQHFNLwSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 144 RLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:PRK10619 160 RVSIARALAM-----EPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
250
....*....|....*..
gi 491527411 224 DTP---WNALTSERIEQ 237
Cdd:PRK10619 234 GAPeqlFGNPQSPRLQQ 250
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-221 |
1.00e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 87.96 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWE----PEKSAKH 79
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHgTATYIMRSGAELElyqlSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IA-----MLPQHSTLTFPFLAREVVELGAIPLSLSNKETTKL---ALHYMEQTDV-LHLAESLYPSLSGGEKQRLHLARV 150
Cdd:TIGR02323 83 LMrtewgFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIratAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 151 MTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:TIGR02323 163 LVT-----RPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-215 |
1.11e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.00 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGN----RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPEKsakhi 80
Cdd:COG4525 4 LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLApSSGEITLDGVPVTGPGADR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtFPFL-AREVVELGaipLSL---SNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTqlhq 156
Cdd:COG4525 79 GVVFQKDAL-LPWLnVLDNVAFG---LRLrgvPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA---- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 157 sGEKRILMLDEPTSALDLAH----QHNTLKIARETAKaqnaAVVVVLHDLNLASQYADRLVLL 215
Cdd:COG4525 151 -ADPRFLLMDEPFGALDALTreqmQELLLDVWQRTGK----GVFLITHSVEEALFLATRLVVM 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
1.38e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGNR--VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAK 78
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQgEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIAMLPQ--H---STLtfpflaREvvelgaiPLSLSNKETTKLALHYM-EQTDVLHLAESLYP----------SLSGGEK 142
Cdd:PRK11160 415 AISVVSQrvHlfsATL------RD-------NLLLAAPNASDEALIEVlQQVGLEKLLEDDKGlnawlgeggrQLSGGEQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 143 QRLHLARVMtqLHQsgeKRILMLDEPTSALDLAHQHNTLKIARETakAQNAAVVVVLHDLNLASQYaDRLVLLHNGKLV 221
Cdd:PRK11160 482 RRLGIARAL--LHD---APLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTGLEQF-DRICVMDNGQII 552
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-226 |
1.60e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.15 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGkqKHDWEPEKSAKHIAMLPQHSTLTFPF---- 93
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG--ERVITAGKKNKKLKPLRKKVGIVFQFpehq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 94 LAREVVE----LGAIPLSLSNKETTKLAlhyMEQTDVLHLAESLY---P-SLSGGEKQRLHLARVMTQlhqsgEKRILML 165
Cdd:PRK13634 98 LFEETVEkdicFGPMNFGVSEEDAKQKA---REMIELVGLPEELLarsPfELSGGQMRRVAIAGVLAM-----EPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 166 DEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-221 |
1.74e-20 |
|
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: 86.90 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03254 6 ENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfyDPQKG-QILIDGIDIRDISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPFLAREVVELGAiplSLSNKETTKLALHYMEQTD-VLHLAESLYPS-------LSGGEKQRLHLARVMtqLHQS 157
Cdd:cd03254 85 DTFL-FSGTIMENIRLGR---PNATDEEVIEAAKEAGAHDfIMKLPNGYDTVlgenggnLSQGERQLLAIARAM--LRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 158 gekRILMLDEPTSALDlAHQHNTLKIARETAKaQNAAVVVVLHDLNLAsQYADRLVLLHNGKLV 221
Cdd:cd03254 159 ---KILILDEATSNID-TETEKLIQEALEKLM-KGRTSIIIAHRLSTI-KNADKILVLDDGKII 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-221 |
4.05e-20 |
|
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: 84.91 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMT------YGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH---HITYFGKQKHdwePE 74
Cdd:cd03213 2 VTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsgEVLINGRPLD---KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 KSAKHIAMLPQHSTLtFPFLarevvelgaiplslsnkeTTKLALHYmeqtdVLHLAeslypSLSGGEKQRLHLARVMTQl 154
Cdd:cd03213 79 SFRKIIGYVPQDDIL-HPTL------------------TVRETLMF-----AAKLR-----GLSGGERKRVSIALELVS- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 155 hqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDL-NLASQYADRLVLLHNGKLV 221
Cdd:cd03213 129 ----NPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPsSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-222 |
4.40e-20 |
|
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: 84.89 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG----EISSNhHITYFGKQKHDWEP-EKSAKHI 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpkyEVTEG-EILFKGEDITDLPPeERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQH----STLTFPFLAREVVElgaiplslsnkettklalhymeqtdvlhlaeslypSLSGGEKQRLHLARVMTQlhq 156
Cdd:cd03217 80 FLAFQYppeiPGVKNADFLRYVNE-----------------------------------GFSGGEKKRNEILQLLLL--- 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 157 sgEKRILMLDEPTSALDLahqhNTLKIARETAKA---QNAAVVVVLHDLNLASQY-ADRLVLLHNGKLVC 222
Cdd:cd03217 122 --EPDLAILDEPDSGLDI----DALRLVAEVINKlreEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
4.93e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGNR-----VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFG----KQKHDWE 72
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 73 PE------KSAKHIAMLPQHSTLTFPF----LAREVVE----LGAIPLSLSNKETTKLALHYMEQT--DVLHLAESLYpS 136
Cdd:PRK13631 98 ELitnpysKKIKNFKELRRRVSMVFQFpeyqLFKDTIEkdimFGPVALGVKKSEAKKLAKFYLNKMglDDSYLERSPF-G 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 LSGGEKQRLHLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLH 216
Cdd:PRK13631 177 LSGGQKRRVAIAGIL-----AIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
250
....*....|....*....
gi 491527411 217 NGKLVCDDTPWNALTSERI 235
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQHI 269
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
10-220 |
5.00e-20 |
|
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: 87.86 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGNRVVldDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-------EISSNHHITYFGKQKHDWEPEKSAkhIAM 82
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGltrpdegEIVLNGRTLFDSRKGIFLPPEKRR--IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLtFPFLA-REVVELGaiplsLSNKETTKLALHYMEQTDVL---HLAESLYPSLSGGEKQRLHLAR-VMTQlhqs 157
Cdd:TIGR02142 80 VFQEARL-FPHLSvRGNLRYG-----MKRARPSERRISFERVIELLgigHLLGRLPGRLSGGEKQRVAIGRaLLSS---- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 158 geKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:TIGR02142 150 --PRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-218 |
5.06e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.29 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSA--KHIAM 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHgSITLDGKPVEGPGAERGVvfQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLtfpflarEVVELGAIPLSLSNKETTKLALHYMEQTDvLHLAESLYP-SLSGGEKQRLHLARVMtqlhqSGEKR 161
Cdd:PRK11248 82 LPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVG-LEGAEKRYIwQLSGGQRQRVGIARAL-----AANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 162 ILMLDEPTSALDL----AHQHNTLKIARETAKaqnaAVVVVLHDLNLASQYADRLVLLHNG 218
Cdd:PRK11248 149 LLLLDEPFGALDAftreQMQTLLLKLWQETGK----QVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
9-221 |
5.32e-20 |
|
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: 85.67 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNR---VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEISSNhhityfGKQKHDWEPEKSAK 78
Cdd:cd03249 4 KNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGEILLD------GVDIRDLNLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIAMLPQHSTLtFPFLAREVVELGAIPLSLSN-KETTKLALHY---MEQTDVLH-LAESLYPSLSGGEKQRLHLARVMTQ 153
Cdd:cd03249 78 QIGLVSQEPVL-FDGTIAENIRYGKPDATDEEvEEAAKKANIHdfiMSLPDGYDtLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 154 lhqsgEKRILMLDEPTSALDLAHQH---NTLKIAREtakaqNAAVVVVLHDLNlASQYADRLVLLHNGKLV 221
Cdd:cd03249 157 -----NPKILLLDEATSALDAESEKlvqEALDRAMK-----GRTTIVIAHRLS-TIRNADLIAVLQNGQVV 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-226 |
6.70e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 15 YGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKqkhdwepeksakhIAML--------PQ 85
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSgRVEVNGR-------------VSALlelgagfhPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HStltfpflAREVVELGAIPLSLSNKETTKLalhyMEqtDVLHLAE---SLY-P--SLSGGEKQRLHLArVMTQLhqsgE 159
Cdd:COG1134 103 LT-------GRENIYLNGRLLGLSRKEIDEK----FD--EIVEFAElgdFIDqPvkTYSSGMRARLAFA-VATAV----D 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 160 KRILMLDEPTSALDLAHQHNTLKIAREtAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:COG1134 165 PDILLVDEVLAVGDAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-220 |
7.04e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.39 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhiTYFGKQK-HDWEPEKsaKHIAMLPQ 85
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGleDITSGD--LFIGEKRmNDVPPAE--RGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPFLAreVVELGAIPLSLSNKETTKLALHYMEQTDVL---HLAESLYPSLSGGEKQRLHLARVMTqlhqsGEKRI 162
Cdd:PRK11000 83 SYAL-YPHLS--VAENMSFGLKLAGAKKEEINQRVNQVAEVLqlaHLLDRKPKALSGGQRQRVAIGRTLV-----AEPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 163 LMLDEPTSALDLAHQHNT-LKIAReTAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMrIEISR-LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-240 |
8.22e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 8.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGeissnhhITY--FGKQKHDWEPEKSAK 78
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG-------LTHpdAGSISLCGEPVPSRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIA-----MLPQHSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQ 153
Cdd:PRK13537 76 RHArqrvgVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 154 lhqsgEKRILMLDEPTSALDLAHQHNTLKIAReTAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTSE 233
Cdd:PRK13537 156 -----DPDVLVLDEPTTGLDPQARHLMWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
250
....*....|
gi 491527411 234 ---RIEQVYG 240
Cdd:PRK13537 230 igcDVIEIYG 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-220 |
1.06e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.77 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYF-GKQKHDWEPEKSAKHI 80
Cdd:PRK10247 4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDISTLKPEIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQ---------HSTLTFPFLAR-EVVELGAIPLSLSNKEttkLALHYMEQTdvlhLAEslypsLSGGEKQRLHLARV 150
Cdd:PRK10247 84 SYCAQtptlfgdtvYDNLIFPWQIRnQQPDPAIFLDDLERFA---LPDTILTKN----IAE-----LSGGEKQRISLIRN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491527411 151 MTQLhqsgeKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNlASQYADRLVLL--HNGKL 220
Cdd:PRK10247 152 LQFM-----PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITLqpHAGEM 217
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
9-222 |
1.13e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG----EISSNhHITYFGKQKHDWEPEKSAKH-IAML 83
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkyEVTSG-SILLDGEDILELSPDERARAgIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQH-------STLTFPFLArevveLGAIPLS-LSNKETTKLALHYMEQtdvLHLAES-----LYPSLSGGEKQRLHLARV 150
Cdd:COG0396 83 FQYpveipgvSVSNFLRTA-----LNARRGEeLSAREFLKLLKEKMKE---LGLDEDfldryVNEGFSGGEKKRNEILQM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 151 MTQlhqsgEKRILMLDEPTSALDLAhqhnTLKIARET---AKAQNAAVVVVLHD---LNLASqyADRLVLLHNGKLVC 222
Cdd:COG0396 155 LLL-----EPKLAILDETDSGLDID----ALRIVAEGvnkLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVK 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
1.19e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLsgKNISMTYGNRV-----VLDDINIDIRAGEVTALLGPNGAGKSTLLK----LLCGEISSnhhITYFGKQKHD--- 70
Cdd:PRK13651 2 QIKV--KNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnaLLLPDTGT---IEWIFKDEKNkkk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 71 -----WEPE---------KSAKHIAMLPQHSTLTFPF----LAREVVE----LGAIPLSLSNKETTKLALHYMEQT--DV 126
Cdd:PRK13651 77 tkekeKVLEklviqktrfKKIKKIKEIRRRVGVVFQFaeyqLFEQTIEkdiiFGPVSMGVSKEEAKKRAAKYIELVglDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 127 LHLAESLYpSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLAS 206
Cdd:PRK13651 157 SYLQRSPF-ELSGGQKRRVALAGILAM-----EPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVL 229
|
250 260
....*....|....*....|....*...
gi 491527411 207 QYADRLVLLHNGKLVCDDTPWNALTSER 234
Cdd:PRK13651 230 EWTKRTIFFKDGKIIKDGDTYDILSDNK 257
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
6-221 |
1.32e-19 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 84.62 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG----EISSNhHITYFGKQKHDWEP-EKSAKHI 80
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyEVTSG-TILFKGQDLLELEPdERARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQH-------STLTFPFLA----REVVELGAIPLSLSNKE-TTKLALHYMeqtDVLHLAESLYPSLSGGEKQRLHLA 148
Cdd:TIGR01978 80 FLAFQYpeeipgvSNLEFLRSAlnarRSARGEEPLDLLDFEKLlKEKLALLDM---DEEFLNRSVNEGFSGGEKKRNEIL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 149 RVMTQlhqsgEKRILMLDEPTSALDLahqhNTLKIARETA---KAQNAAVVVVLHDLNLASQYA-DRLVLLHNGKLV 221
Cdd:TIGR01978 157 QMALL-----EPKLAILDEIDSGLDI----DALKIVAEGInrlREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIV 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-221 |
1.33e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTY---GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSNHHITYFGKQKHDWEPEKSAKH 79
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTltfPFLAREVVELGAIPLSLSNKETTKLALHYMEQT--------DVLHLAESLYPSLSGGEKQRLHLARVM 151
Cdd:PRK14246 92 VGMVFQQPN---PFPHLSIYDNIAYPLKSHGIKEKREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK14246 169 AL-----KPKVLLMDEPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-221 |
1.44e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGkqkHDWEPEKSA------KHI 80
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGiERPSAGKIWFSG---HDITRLKNRevpflrRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtfpFLAREVVELGAIPLSL---SNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqs 157
Cdd:PRK10908 82 GMIFQDHHL---LMDRTVYDNVAIPLIIagaSGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN---- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 158 gEKRILMLDEPTSALDLAHQHNTLKIARETAKAqNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK10908 155 -KPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-223 |
1.60e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN-----RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAM 82
Cdd:COG1101 5 KNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSgSILIDGKDVTKLPEYKRAKYIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTL-TFPFLarEVVElgaiPLSLSNKETTKLAL----------HYMEQTDVLHLA-----ESLYPSLSGGEKQRLH 146
Cdd:COG1101 85 VFQDPMMgTAPSM--TIEE----NLALAYRRGKRRGLrrgltkkrreLFRELLATLGLGlenrlDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 147 LarVMTQLHQSgekRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:COG1101 159 L--LMATLTKP---KLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-250 |
1.86e-19 |
|
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: 87.19 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGeisSNHHITYFGKQKHDWEPEKsAKHI---- 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG---VYPHGTWDGEIYWSGSPLK-ASNIrdte 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 -----------AMLPQHSTLTFPFLAREVVELGAIplsLSNKETTKLALHYMEQTDVLHLAESLYPS-LSGGEKQRLHLA 148
Cdd:TIGR02633 77 ragiviihqelTLVPELSVAENIFLGNEITLPGGR---MAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 149 RVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCdDTPWN 228
Cdd:TIGR02633 154 KALNK-----QARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVA-TKDMS 226
|
250 260
....*....|....*....|..
gi 491527411 229 ALTSERIEQVYGYRSIVTKHPT 250
Cdd:TIGR02633 227 TMSEDDIITMMVGREITSLYPH 248
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
9-220 |
1.98e-19 |
|
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: 84.06 E-value: 1.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNR---VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEISSNhhityfGKQKHDWEPEKSAK 78
Cdd:cd03248 15 QNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqGGQVLLD------GKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIAMLPQHSTLtfpfLAREVVELGAIPL-SLSNKETTKLALHYMEQTDVLHLAESLYPS-------LSGGEKQRLHLARV 150
Cdd:cd03248 89 KVSLVGQEPVL----FARSLQDNIAYGLqSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 151 MTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETakAQNAAVVVVLHDLNLAsQYADRLVLLHNGKL 220
Cdd:cd03248 165 LIR-----NPQVLILDEATSALDAESEQQVQQALYDW--PERRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
2.15e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 84.74 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHhityfGKQKHDWEPEKSAKHiAML 83
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTS-----GEVLIKGEPIKYDKK-SLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLTFPF----------LAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQ 153
Cdd:PRK13639 75 EVRKTVGIVFqnpddqlfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 154 lhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13639 155 -----KPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-226 |
2.68e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.42 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSA 77
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGiEKVKSGEIFYNNQAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 KHIAMLPQH-------STLTFPflarevVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARV 150
Cdd:PRK13648 83 KHIGIVFQNpdnqfvgSIVKYD------VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 151 MTqLHQSgekrILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTP 226
Cdd:PRK13648 157 LA-LNPS----VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTP 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-221 |
2.72e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 85.51 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNR----VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKqkhdwepEKSA------ 77
Cdd:COG1135 5 ENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLlERPTSGSVLVDGV-------DLTAlserel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 ----KHIAMLPQHSTLtfpFLAREVVELGAIPLSLSN---KETTKLALHYMEQTDVLHLAESlYPS-LSGGEKQRLHLAR 149
Cdd:COG1135 78 raarRKIGMIFQHFNL---LSSRTVAENVALPLEIAGvpkAEIRKRVAELLELVGLSDKADA-YPSqLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 150 VMtqlhqSGEKRILMLDEPTSALDlahQHNT-------LKIARETakaqNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG1135 154 AL-----ANNPKVLLCDEATSALD---PETTrsildllKDINREL----GLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-226 |
3.97e-19 |
|
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: 86.39 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG----EISSN---HHITY------------------ 63
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyEPTSGriiYHVALcekcgyverpskvgepcp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 64 -----FGKQKHD-WEPEKS-----AKHIAMLPQHstlTFPFLAREVV---ELGAIP-LSLSNKETTKLALHYMEQTDVLH 128
Cdd:TIGR03269 84 vcggtLEPEEVDfWNLSDKlrrriRKRIAIMLQR---TFALYGDDTVldnVLEALEeIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 129 LAESLYPSLSGGEKQRLHLARvmtQLHQsgEKRILMLDEPTSALD-----LAHqhntlKIARETAKAQNAAVVVVLHDLN 203
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLAR---QLAK--EPFLFLADEPTGTLDpqtakLVH-----NALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|...
gi 491527411 204 LASQYADRLVLLHNGKLVCDDTP 226
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTP 253
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-221 |
7.60e-19 |
|
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: 83.95 E-value: 7.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTY--GNRVV--LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHH----ITYFGK-----QKHDW 71
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGItsgeILFDGEdllklSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 72 EpEKSAKHIAMLPQHSTLTF-PFL--AREVVELGAIPLSLSNKETTKLALHYMEQTDvLHLAESL---YPS-LSGGEKQR 144
Cdd:COG0444 81 R-KIRGREIQMIFQDPMTSLnPVMtvGDQIAEPLRIHGGLSKAEARERAIELLERVG-LPDPERRldrYPHeLSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 145 LHLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG0444 159 VMIARAL-----ALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-221 |
8.18e-19 |
|
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: 82.03 E-value: 8.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 19 VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDwEPEKSAKHIAMLPQHSTLTFPFLARE 97
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 98 VVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqLHQSGekrILMLDEPTSALDLAHQ 177
Cdd:cd03266 98 NLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL--VHDPP---VLLLDEPTTGLDVMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491527411 178 HNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:cd03266 173 RALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-234 |
8.70e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.24 E-value: 8.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 13 MTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGeI--SSNHHITYfgkqkhdwePEksAKHIAMLPQHS--- 87
Cdd:COG4178 371 RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LwpYGSGRIAR---------PA--GARVLFLPQRPylp 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 --TLtfpflaREVVELGAIPLSLSNKEttklALHYMEQTDVLHLAESLYPS------LSGGEKQRLHLARVMtqLHQSge 159
Cdd:COG4178 439 lgTL------REALLYPATAEAFSDAE----LREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLL--LHKP-- 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 160 kRILMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLAsQYADRLVLLHngklvcDDTPWNALTSER 234
Cdd:COG4178 505 -DWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGHRSTLA-AFHDRVLELT------GDGSWQLLPAEA 569
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-218 |
9.65e-19 |
|
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: 82.13 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsakhiaMLPQHSTLTFPFL-AREV 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQITEPGPDR------MVVFQNYSLLPWLtVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 99 VELG--AIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEKRILMLDEPTSALDLAH 176
Cdd:TIGR01184 75 IALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARAL-----SIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491527411 177 ----QHNTLKIAREtakaQNAAVVVVLHDLNLASQYADRLVLLHNG 218
Cdd:TIGR01184 150 rgnlQEELMQIWEE----HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-224 |
9.93e-19 |
|
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: 81.81 E-value: 9.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 15 YGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKqkhdwepeksakhIAMLPQ-----HST 88
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSgTVTVRGR-------------VSSLLGlgggfNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 89 LTfpflAREVVELGAIPLSLSNKETTKLA---LHYMEQTDVLHLAESLYpslSGGEKQRLHLArVMTQLhqsgEKRILML 165
Cdd:cd03220 99 LT----GRENIYLNGRLLGLSRKEIDEKIdeiIEFSELGDFIDLPVKTY---SSGMKARLAFA-IATAL----EPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 166 DEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDD 224
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-221 |
1.08e-18 |
|
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: 84.00 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 23 DINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEISSNHHITYFGKQKHDWEPEKsaKHIAMLPQHSTLtFPFL- 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglerpdSGRIRLGGEVLQDSARGIFLPPHR--RRIGYVFQEARL-FPHLs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 95 AREVVELGaipLSLSNKETTKLALHYMeqTDVLHLAESL--YP-SLSGGEKQRLHLAR-VMTQlhqsgeKRILMLDEPTS 170
Cdd:COG4148 94 VRGNLLYG---RKRAPRAERRISFDEV--VELLGIGHLLdrRPaTLSGGERQRVAIGRaLLSS------PRLLLMDEPLA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 171 ALDLAHQHNTL----KIARETakaqNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG4148 163 ALDLARKAEILpyleRLRDEL----DIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-253 |
1.32e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.12 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKsaKHIAML 83
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMLDGVDLSHVPPYQ--RPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLtFPFLAREV-VELGAIPLSLSNKETTK-----LALHYMEQtdvlhLAESLYPSLSGGEKQRLHLARVMTQlhqs 157
Cdd:PRK11607 97 FQSYAL-FPHMTVEQnIAFGLKQDKLPKAEIASrvnemLGLVHMQE-----FAKRKPHQLSGGQRQRVALARSLAK---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 158 gEKRILMLDEPTSALDLA----HQHNTLKIARETAkaqnAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPwnaltse 233
Cdd:PRK11607 167 -RPKLLLLDEPMGALDKKlrdrMQLEVVDILERVG----VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP------- 234
|
250 260
....*....|....*....|
gi 491527411 234 riEQVYgyrsivtKHPTLDF 253
Cdd:PRK11607 235 --EEIY-------EHPTTRY 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-223 |
1.43e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQkhdwePEKSAKH-IAMLPQHS 87
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREdTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLtFPFlaREVVElgAIPLSLSNKETTKlALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqLHQSgekRILMLDE 167
Cdd:PRK11247 91 RL-LPW--KKVID--NVGLGLKGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARAL--IHRP---GLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 168 PTSALD----LAHQHNTLKIAREtakaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:PRK11247 160 PLGALDaltrIEMQDLIESLWQQ----HGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-231 |
1.91e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.04 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMTY---------GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQ---KHDW 71
Cdd:PRK10419 2 TLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 72 EPEKS-AKHIAMLPQHSTLTF-PflAREVVELGAIPL----SLSNKETTKLALHYMEQTDV-LHLAESLYPSLSGGEKQR 144
Cdd:PRK10419 82 AQRKAfRRDIQMVFQDSISAVnP--RKTVREIIREPLrhllSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 145 LHLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDD 224
Cdd:PRK10419 160 VCLARAL-----AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
....*..
gi 491527411 225 TPWNALT 231
Cdd:PRK10419 235 PVGDKLT 241
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-177 |
2.61e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAml 83
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAgTIKLDGGDIDDPDVAEACHYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 pqHSTLTFPFLAreVVE--------LGAIPLSLSNkettklALHYMEQTDVLHLAeslYPSLSGGEKQRLHLARVMTqlh 155
Cdd:PRK13539 80 --HRNAMKPALT--VAEnlefwaafLGGEELDIAA------ALEAVGLAPLAHLP---FGYLSAGQKRRVALARLLV--- 143
|
170 180
....*....|....*....|..
gi 491527411 156 qSGeKRILMLDEPTSALDLAHQ 177
Cdd:PRK13539 144 -SN-RPIWILDEPTAALDAAAV 163
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-225 |
2.77e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.44 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSNHHITYfgKQKhdwepEKSAKHIAM-LPQHSTL--- 89
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTgilvptsGEVRVLGYVPF--KRR-----KEFARRIGVvFGQRSQLwwd 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 -----TFPFLaREVVElgaIPlslsnKETTKLALHYMeqTDVLHLAESLY-P--SLSGGEKQRLHLARVMtqLHQSgekR 161
Cdd:COG4586 111 lpaidSFRLL-KAIYR---IP-----DAEYKKRLDEL--VELLDLGELLDtPvrQLSLGQRMRCELAAAL--LHRP---K 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 162 ILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDT 225
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
3.32e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.33 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLsgKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL------------CGEISSNHHITyFGKQK 68
Cdd:PRK11264 1 MSAIEV--KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARS-LSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 69 hdwepeksaKHIAMLPQHSTLTFP----FLAR----EVVELGAIPLSLSNKETTKLALHYMEQTDvLHLAESLYPS-LSG 139
Cdd:PRK11264 78 ---------GLIRQLRQHVGFVFQnfnlFPHRtvleNIIEGPVIVKGEPKEEATARARELLAKVG-LAGKETSYPRrLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 140 GEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:PRK11264 148 GQQQRVAIARALAM-----RPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
..
gi 491527411 220 LV 221
Cdd:PRK11264 222 IV 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-226 |
5.10e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.96 E-value: 5.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFgkqkhDWE--PEKS-------AKH 79
Cdd:PRK11831 11 RGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-----DGEniPAMSrsrlytvRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtfpFLAREVVELGAIPLslsnKETTKLALHYMEQTDVLHL-------AESLYPS-LSGGEKQRLHLARVM 151
Cdd:PRK11831 86 MSMLFQSGAL---FTDMNVFDNVAYPL----REHTQLPAPLLHSTVMMKLeavglrgAAKLMPSeLSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK11831 159 AL-----EPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-226 |
6.01e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.42 E-value: 6.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKqkhdwepeksakH 79
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKpTGGTILLRGQ------------H 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTL------TFP----FLAREVVE-----------------LGAIP-LSLSNKETTKLALHYMEQTDVLHLAE 131
Cdd:PRK11300 69 IEGLPGHQIArmgvvrTFQhvrlFREMTVIEnllvaqhqqlktglfsgLLKTPaFRRAESEALDRAATWLERVGLLEHAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 132 SLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADR 211
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVT-----QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDR 223
|
250
....*....|....*
gi 491527411 212 LVLLHNGKLVCDDTP 226
Cdd:PRK11300 224 IYVVNQGTPLANGTP 238
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-235 |
1.22e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.44 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGNRV-----VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKhdwEPE--KSAKHIAM 82
Cdd:PRK13645 11 NVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYA---IPAnlKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLTFPF----LAREVVE----LGAIPLSLSNKETTKlalHYMEQTDVLHLAESLYP----SLSGGEKQRLHLARV 150
Cdd:PRK13645 88 LRKEIGLVFQFpeyqLFQETIEkdiaFGPVNLGENKQEAYK---KVPELLKLVQLPEDYVKrspfELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 151 MTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNAL 230
Cdd:PRK13645 165 IAM-----DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
....*
gi 491527411 231 TSERI 235
Cdd:PRK13645 240 SNQEL 244
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-226 |
1.24e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.09 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKST-------LLKLLCGEISSNH-HITyfGKQKHDWEPEKSAKHIAMLPQHStl 89
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTliqhlngLLKPTSGKIIIDGvDIT--DKKVKLSDIRKKVGLVFQYPEYQ-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 tfpfLAREVVE----LGAIPLSLSNKETTKLALHYMEQT--DVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRIL 163
Cdd:PRK13637 96 ----LFEETIEkdiaFGPINLGLSEEEIENRVKRAMNIVglDYEDYKDKSPFELSGGQKRRVAIAGVVAM-----EPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 164 MLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13637 167 ILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-202 |
1.31e-17 |
|
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: 79.72 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 29 RAGEVTALLGPNGAGKSTLLKLLCGEISSNhhityFGKqkHDWEPE---------KSAKHI------------AMLPQHS 87
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPN-----LGK--FDDPPDwdeildefrGSELQNyftkllegdvkvIVKPQYV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLTFPFLAREVVELgaiplsLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDE 167
Cdd:cd03236 97 DLIPKAVKGKVGEL------LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALAR-----DADFYFFDE 165
|
170 180 190
....*....|....*....|....*....|....*
gi 491527411 168 PTSALDLAHQHNTLKIARETAKAQNaAVVVVLHDL 202
Cdd:cd03236 166 PSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDL 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-226 |
1.38e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.92 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHI-------TYFGKQKHDwe 72
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGlEKPTEGQIfidgedvTHRSIQQRD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 73 peksakhIAMLPQHSTLtFPFLA-REVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVM 151
Cdd:PRK11432 80 -------ICMVFQSYAL-FPHMSlGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK11432 152 IL-----KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-223 |
1.73e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.69 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTY----GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-CGEISSNHHITYFGKQKHDWEPEKSAK-- 78
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgCLDKPTSGTYRVAGQDVATLDADALAQlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 --HIAMLPQHSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQtdvLHLAE--SLYPS-LSGGEKQRLHLARVmtq 153
Cdd:PRK10535 85 reHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQR---LGLEDrvEYQPSqLSGGQQQRVSIARA--- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 154 LHQSGEkrILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCD 223
Cdd:PRK10535 159 LMNGGQ--VILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-213 |
2.10e-17 |
|
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: 78.99 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 27 DIRAGEVTALLGPNGAGKSTLLKLLCGEISSNhhityfgkqkhDWEPEKSAKHIAMLPQHSTLTFPFLAREVvelgaipl 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPD-----------EGDIEIELDTVSYKPQYIKADYEGTVRDL-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 107 sLSNKETTKLALHYMeQTDVLH------LAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNT 180
Cdd:cd03237 82 -LSSITKDFYTHPYF-KTEIAKplqieqILDREVPELSGGELQRVAIAACLSK-----DADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|...
gi 491527411 181 LKIARETAKAQNAAVVVVLHDLNLASQYADRLV 213
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
9-221 |
2.42e-17 |
|
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: 78.43 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKQKHDWEPEKSAKHIAMLP 84
Cdd:cd03251 4 KNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfyDVDSG-RILIDGHDVRDYTLASLRRQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLtFPFLAREVVELGAIPLSLSNKETTKLALHYME---------QTDVlhlaESLYPSLSGGEKQRLHLARVMTQlh 155
Cdd:cd03251 83 QDVFL-FNDTVAENIAYGRPGATREEVEEAARAANAHEfimelpegyDTVI----GERGVKLSGGQRQRIAIARALLK-- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 156 qsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:cd03251 156 ---DPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-255 |
4.17e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSA--- 77
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAgSILYLGKEVTFNGPKSSQeag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 -----KHIAMLPQHSTLTFPFLAREVVE-LGAIPLSLSNKETTKLalhyMEQTDVLHLAESLYPSLSGGEKQRLHLARVM 151
Cdd:PRK10762 81 igiihQELNLIPQLTIAENIFLGREFVNrFGRIDWKKMYAEADKL----LARLNLRFSSDKLVGELSIGEQQMVEIAKVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 152 tqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVcDDTPWNALT 231
Cdd:PRK10762 157 -----SFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI-AEREVADLT 229
|
250 260
....*....|....*....|....*
gi 491527411 232 SER-IEQVYGyRSIVTKHPTLDFPQ 255
Cdd:PRK10762 230 EDSlIEMMVG-RKLEDQYPRLDKAP 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-243 |
4.20e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE-ISSNHHITYFGKQKHdWEPEKSAKH--IAM 82
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQEMR-FASTTAALAagVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLTfPFLAreVVE---LGAIP--LSLSNKETtkLALHYMEQTDvlHLAESLYPS-----LSGGEKQRLHLARVMT 152
Cdd:PRK11288 84 IYQELHLV-PEMT--VAEnlyLGQLPhkGGIVNRRL--LNYEAREQLE--HLGVDIDPDtplkyLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 153 QlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALTS 232
Cdd:PRK11288 157 R-----NARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDR 230
|
250 260
....*....|....*....|
gi 491527411 233 ER---------IEQVYGYRS 243
Cdd:PRK11288 231 DQlvqamvgreIGDIYGYRP 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-222 |
4.91e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKQKHDWEPEKSAKH-IAMLPQ 85
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGihEPTKG-TITINNINYNKLDHKLAAQLgIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPFLAREVVELGAIPLS-------LSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsg 158
Cdd:PRK09700 88 ELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML----- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 159 EKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVC 222
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-221 |
7.32e-17 |
|
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: 77.14 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYG--NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLtFPFLAREVVELGAIPLSLSN-KETTKLA-LHYMeqtdVLHLAESlY--------PSLSGGEKQRLHLARVMTQlh 155
Cdd:cd03252 84 ENVL-FNRSIRDNIALADPGMSMERvIEAAKLAgAHDF----ISELPEG-YdtivgeqgAGLSGGQRQRIAIARALIH-- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 156 qsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNlASQYADRLVLLHNGKLV 221
Cdd:cd03252 156 ---NPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-221 |
8.11e-17 |
|
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: 79.46 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFgKQKHDW---------EPEKS 76
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV-RVGDEWvdmtkpgpdGRGRA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 77 AKHIAMLPQHSTLtFPFlaREVVE--LGAIPLSLSNKETTKLALHYMEQTDVLH-LAESL---YPS-LSGGEKQRLHLAR 149
Cdd:TIGR03269 364 KRYIGILHQEYDL-YPH--RTVLDnlTEAIGLELPDELARMKAVITLKMVGFDEeKAEEIldkYPDeLSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 150 VMTQlhqsgEKRILMLDEPTSALD----LAHQHNTLKiARETAkaqNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:TIGR03269 441 VLIK-----EPRIVILDEPTGTMDpitkVDVTHSILK-AREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-242 |
8.39e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 8.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVlSGKNISMTY--GNRVvLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSA 77
Cdd:PRK13647 1 MDNII-EVEDLHFRYkdGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 KHIAMLPQH-STLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhq 156
Cdd:PRK13647 79 SKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 157 sgEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPwNALTSERIE 236
Cdd:PRK13647 156 --DPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDIV 231
|
....*.
gi 491527411 237 QVYGYR 242
Cdd:PRK13647 232 EQAGLR 237
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
9-221 |
9.06e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.38 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNR---VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLcgeisSNHHITYFGKQKHDWEPEKSAKHIamlpq 85
Cdd:TIGR00958 482 QDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL-----QNLYQPTGGQVLLDGVPLVQYDHH----- 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 hstltfpFLAREVVELGAIPL--SLSNKETTKLALHYMEQTDVLHLAE--------SLYPS------------LSGGEKQ 143
Cdd:TIGR00958 552 -------YLHRQVALVGQEPVlfSGSVRENIAYGLTDTPDEEIMAAAKaanahdfiMEFPNgydtevgekgsqLSGGQKQ 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 144 RLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHntlkIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:TIGR00958 625 RIAIARALVR-----KPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-221 |
1.07e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.27 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKqkhdwepEKSAKH 79
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAgEVHYRMR-------DGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTltfPFLARE---VVE----------------LGAIPLSLSNKETTKL---ALHYMEQTDV-LHLAESLYPS 136
Cdd:PRK11701 75 LYALSEAER---RRLLRTewgFVHqhprdglrmqvsaggnIGERLMAVGARHYGDIratAGDWLERVEIdAARIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 LSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLH 216
Cdd:PRK11701 152 FSGGMQQRLQIARNLVT-----HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
....*
gi 491527411 217 NGKLV 221
Cdd:PRK11701 227 QGRVV 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
2.62e-16 |
|
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: 77.80 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGN----RVVLDDINIDIRAGEVTALLGPNGAGKS----TLLKLLCGEISSNH-HITYFGKQKHDW 71
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSgSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 72 ePEKSAKH-----IAML---------PQHStltfpfLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESL--YP 135
Cdd:COG4172 82 -SERELRRirgnrIAMIfqepmtslnPLHT------IGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLdaYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 136 S-LSGGEKQRlhlarVMTQLHQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVL 214
Cdd:COG4172 155 HqLSGGQRQR-----VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAV 229
|
....*..
gi 491527411 215 LHNGKLV 221
Cdd:COG4172 230 MRQGEIV 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
20-220 |
2.91e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.59 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEK----SAKHIAMLPQHSTLTFPFL 94
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGlDDGSSGEVSLVGQPLHQMDEEAraklRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 95 AREVVELGAIPLSLSNKETTKLALHYMEQtdvLHLAESLY--PS-LSGGEKQRLHLARVMtqlhqSGEKRILMLDEPTSA 171
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQ---LGLGKRLDhlPAqLSGGEQQRVALARAF-----NGRPDVLFADEPTGN 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491527411 172 LDlahQHNTLKIAR---ETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKL 220
Cdd:PRK10584 177 LD---RQTGDKIADllfSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-220 |
3.08e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.62 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTY--GNRV--VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEK 75
Cdd:PRK11629 1 MNKILLQCDNLCKRYqeGSVQtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGlDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 SAK----HIAMLPQHSTLTFPFLAREVVelgAIPLSLSNK---ETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLA 148
Cdd:PRK11629 81 KAElrnqKLGFIYQFHHLLPDFTALENV---AMPLLIGKKkpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491527411 149 RVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYaDRLVLLHNGKL 220
Cdd:PRK11629 158 RALVN-----NPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-221 |
3.30e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 19 VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQHSTLtFPFLAREV 98
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQL-PHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 99 VELGAIPLSlsnKETTKLALhymEQTDVLHLAESL-----YP------SLSGGEKQRLHLARVMTQLHQsgekrILMLDE 167
Cdd:PRK11174 443 VLLGNPDAS---DEQLQQAL---ENAWVSEFLPLLpqgldTPigdqaaGLSVGQAQRLALARALLQPCQ-----LLLLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 168 PTSALDlAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYaDRLVLLHNGKLV 221
Cdd:PRK11174 512 PTASLD-AHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-201 |
3.99e-16 |
|
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: 77.28 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG---------EISSNHHITYFGKQKHDWEPE 74
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGqeqpdsgtiEIGETVKLAYVDQSRDALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 KSakhiamlpqhstltfpflAREVVELGAIPLSLSNKETTKLAlhYMEQ-----TDvlhlAESLYPSLSGGEKQRLHLAR 149
Cdd:TIGR03719 401 KT------------------VWEEISGGLDIIKLGKREIPSRA--YVGRfnfkgSD----QQKKVGQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491527411 150 VmtqLHQSGEkrILMLDEPTSALDLahqhNTLKIARETAKAQNAAVVVVLHD 201
Cdd:TIGR03719 457 T---LKSGGN--VLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-219 |
4.16e-16 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.43 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKqkhdwepeksakhIAMLPQHS-----TL---- 89
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSgSVSVPGS-------------IAYVSQEPwiqngTIreni 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 TF--PFLA---REVVELGAIPLSLSNkettklaLHYMEQTDV----LhlaeslypSLSGGEKQRLHLARVMTQlhqsgEK 160
Cdd:cd03250 87 LFgkPFDEeryEKVIKACALEPDLEI-------LPDGDLTEIgekgI--------NLSGGQKQRISLARAVYS-----DA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 161 RILMLDEPTSALDlAHqhntlkiareTAK-----------AQNAAVVVVLHDLNLASQyADRLVLLHNGK 219
Cdd:cd03250 147 DIYLLDDPLSAVD-AH----------VGRhifencilgllLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-226 |
4.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.93 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHH--------ITYFGKQKHDWEPEKSAKHIAMLPQhsTLTFP 92
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivVSSTSKQKEIKPVRKKVGVVFQFPE--SQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 93 FLAREVVELGAIPLSLSNKETTKLAlhyMEQTDVLHLAESLYP----SLSGGEKQRLHLARVMTQlhqsgEKRILMLDEP 168
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIA---AEKLEMVGLADEFWEkspfELSGGQMRRVAIAGILAM-----EPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 169 TSALDLAHQHNTLKIArETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13643 172 TAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
16-202 |
4.68e-16 |
|
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: 77.40 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 16 GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQHSTLtFPFL 94
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQgEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 95 AREVVELGAIPLS----LSNKETTKLALHYMEQTDVLHlaESLYP---SLSGGEKQRLHLARVMTQlhqsgEKRILMLDE 167
Cdd:TIGR02868 425 VRENLRLARPDATdeelWAALERVGLADWLRALPDGLD--TVLGEggaRLSGGERQRLALARALLA-----DAPILLLDE 497
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491527411 168 PTSALDlahqhntLKIARETAKAQNAA-----VVVVLHDL 202
Cdd:TIGR02868 498 PTEHLD-------AETADELLEDLLAAlsgrtVVLITHHL 530
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-221 |
4.75e-16 |
|
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: 77.06 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYG--NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSAKHIA 81
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRfyEPDSGQ-ILLDGHDLADYTLASLRRQVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHSTLTFPFLAREVV--ELGAIPlslsnKETTKLALHYMEQTDVLH-LAESLYPS-------LSGGEKQRLHLARVM 151
Cdd:TIGR02203 410 LVSQDVVLFNDTIANNIAygRTEQAD-----RAEIERALAAAYAQDFVDkLPLGLDTPigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDlaHQHNTLKIARETAKAQNAAVVVVLHDLNlASQYADRLVLLHNGKLV 221
Cdd:TIGR02203 485 LK-----DAPILILDEATSALD--NESERLVQAALERLMQGRTTLVIAHRLS-TIEKADRIVVMDDGRIV 546
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-251 |
5.32e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGkqkhdwEPEKSAK 78
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASgKISILG------QPTRQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 H---IAMLPQHSTL--TFPFLAREVVELGAIP----LSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLAR 149
Cdd:PRK15056 76 QknlVAYVPQSEEVdwSFPVLVEDVVMMGRYGhmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 150 VMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPwNA 229
Cdd:PRK15056 156 AIAQ-----QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE-TT 228
|
250 260
....*....|....*....|..
gi 491527411 230 LTSERIEQVYgyrSIVTKHPTL 251
Cdd:PRK15056 229 FTAENLELAF---SGVLRHVAL 247
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-200 |
8.97e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS---SNHHITYFGKQKHDWEPEKSA 77
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykiLEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 KHIAMLPQHSTLTFP------FL---------AREVVELGaiPLSLSNKETTKLALHYMEQTdvlHLAESLYPSLSGGEK 142
Cdd:CHL00131 83 HLGIFLAFQYPIEIPgvsnadFLrlaynskrkFQGLPELD--PLEFLEIINEKLKLVGMDPS---FLSRNVNEGFSGGEK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 143 QR---LHLARVMTQLHqsgekrilMLDEPTSALDLahqhNTLKIARE---TAKAQNAAVVVVLH 200
Cdd:CHL00131 158 KRneiLQMALLDSELA--------ILDETDSGLDI----DALKIIAEginKLMTSENSIILITH 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-226 |
1.01e-15 |
|
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: 76.59 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQHSTLTFPFLARE 97
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 98 VVELGAiPLSLSNKETTKLALHYM-EQTDVLHLAESLYPSLSGGEKQRLHLARVMTqlhqsGEKRILMLDEPTSALDLAH 176
Cdd:TIGR01257 1023 HILFYA-QLKGRSWEEAQLEMEAMlEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV-----GDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491527411 177 QHNTLKIARETAKAQnaAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-220 |
1.25e-15 |
|
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: 72.46 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISmtygNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSAKH 79
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGlrPPASGE-ITLDGKPVTRRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 -IAMLPQ--HSTLTFpflarevvelgaipLSLSNKETTKLALHymeqtdvlhlaeslypsLSGGEKQRLHLARVMTQlhq 156
Cdd:cd03215 76 gIAYVPEdrKREGLV--------------LDLSVAENIALSSL-----------------LSGGNQQKVVLARWLAR--- 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 157 sgEKRILMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:cd03215 122 --DPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-221 |
1.53e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 74.84 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY----GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGK---QKHDWEPEKSAKHI 80
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLlERPTSGRVLVDGQdltALSEKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHstltFPFLA-REVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAE--SLYPS-LSGGEKQRLHLARVMtqlhq 156
Cdd:PRK11153 85 GMIFQH----FNLLSsRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDkaDRYPAqLSGGQKQRVAIARAL----- 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 157 SGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-221 |
1.91e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSAKH-IAM 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGiVPPDSGTLEIGGNPCARLTPAKAHQLgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTLtFPFLA-REVVELG-AIPLSLSNKETTKLALhymeqtdvlhLAESLYPSLSGG-----EKQrlhLARVMTQLH 155
Cdd:PRK15439 91 VPQEPLL-FPNLSvKENILFGlPKRQASMQKMKQLLAA----------LGCQLDLDSSAGslevaDRQ---IVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 156 QsgEKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK15439 157 R--DSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
9-226 |
2.00e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYG-----NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQkhDWEPEKSAKHIAML 83
Cdd:PRK13649 6 QNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDT--LITSTSKNKDIKQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 84 PQHSTLTFPFLAREV--------VELGAIPLSLSNKETTKLALhymEQTDVLHLAESLYP----SLSGGEKQRLHLARVM 151
Cdd:PRK13649 84 RKKVGLVFQFPESQLfeetvlkdVAFGPQNFGVSQEEAEALAR---EKLALVGISESLFEknpfELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAqNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13649 161 AM-----EPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-235 |
2.24e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISsnhHITYFGKQKHDWEPEK------SAK 78
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP---HGSYEGEILFDGEVCRfkdirdSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 H--------IAMLPQHSTLTFPFLAREVVELGAIPLSLSNKETTKL----ALHYMEQTDVLHLaeslypslsGGEKQRL- 145
Cdd:NF040905 78 LgiviihqeLALIPYLSIAENIFLGNERAKRGVIDWNETNRRARELlakvGLDESPDTLVTDI---------GVGKQQLv 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 146 HLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGK----LV 221
Cdd:NF040905 149 EIAKAL-----SKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRtietLD 222
|
250
....*....|....
gi 491527411 222 CDDTPwnaLTSERI 235
Cdd:NF040905 223 CRADE---VTEDRI 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-210 |
2.54e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.28 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKL------LCGEISSNHHITYFGKQKHDWE--PE 74
Cdd:PRK14243 8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVEGKVTFHGKNLYAPDvdPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 KSAKHIAMLPQHSTlTFP--------FLAR---------EVVElgaiplslsnkETTKLALHYMEQTDVLHLAESlypSL 137
Cdd:PRK14243 88 EVRRRIGMVFQKPN-PFPksiydniaYGARingykgdmdELVE-----------RSLRQAALWDEVKDKLKQSGL---SL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 138 SGGEKQRLHLARVMtqlhqSGEKRILMLDEPTSALDLAhqhNTLKIaRETAK--AQNAAVVVVLHDLNLASQYAD 210
Cdd:PRK14243 153 SGGQQQRLCIARAI-----AVQPEVILMDEPCSALDPI---STLRI-EELMHelKEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-221 |
2.60e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH------HITYFGKQKH--DWEPEKSAKHIA 81
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearvegEVRLFGRNIYspDVDPIEVRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHSTltfPFLAREVVELGAIPLSLSN--------KETTKLALHYMEQTDVLHLAESLYPS-LSGGEKQRLHLARVMT 152
Cdd:PRK14267 89 MVFQYPN---PFPHLTIYDNVAIGVKLNGlvkskkelDERVEWALKKAALWDEVKDRLNDYPSnLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 153 QlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK14267 166 M-----KPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-221 |
4.40e-15 |
|
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: 71.52 E-value: 4.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMTYG----NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH----HITYFGKQKHDwEPEK 75
Cdd:cd03233 2 STLSWRNISFTTGkgrsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsvegDIHYNGIPYKE-FAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 SAKHIAMLPQH----STLTFpflarevvelgaiplslsnKETTKLALHyMEQTDVLHlaeslypSLSGGEKQRLHLARVM 151
Cdd:cd03233 81 YPGEIIYVSEEdvhfPTLTV-------------------RETLDFALR-CKGNEFVR-------GISGGERKRVSIAEAL 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 152 TqlhqsGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDlnlASQ--YA--DRLVLLHNGKLV 221
Cdd:cd03233 134 V-----SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQ---ASDeiYDlfDKVLVLYEGRQI 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-217 |
5.82e-15 |
|
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: 70.26 E-value: 5.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 17 NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSnhhityfgkqkhdwePEKSakHIAMLPQHSTL 89
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsGRIGM---------------PEGE--DLLFLPQRPYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 TFPFLaREVVelgaiplslsnkettklalhymeqtdvlhlaesLYPS---LSGGEKQRLHLARVMtqLHQSgekRILMLD 166
Cdd:cd03223 76 PLGTL-REQL---------------------------------IYPWddvLSGGEQQRLAFARLL--LHKP---KFVFLD 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491527411 167 EPTSALDlahqHNTLKIARETAKAQNAAVVVVLHDLNLaSQYADRLVLLHN 217
Cdd:cd03223 117 EATSALD----EESEDRLYQLLKELGITVISVGHRPSL-WKFHDRVLDLDG 162
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-221 |
5.92e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYGN----RVVLDDINIDIRAGEVTALLGPNGAGKS----TLLKLL--------CGEIssnhhitYF 64
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDI-------RF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 65 GKQKHDWEPEKSAKH-----IAMLPQHSTLTF-PF--LAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESL--Y 134
Cdd:PRK15134 74 HGESLLHASEQTLRGvrgnkIAMIFQEPMVSLnPLhtLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLtdY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 135 P-SLSGGEKQRLHLArvMTQLHQSgekRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLV 213
Cdd:PRK15134 154 PhQLSGGERQRVMIA--MALLTRP---ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVA 228
|
....*...
gi 491527411 214 LLHNGKLV 221
Cdd:PRK15134 229 VMQNGRCV 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-220 |
7.62e-15 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 73.67 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSnhhityfgkQKHDWEPEKSAKhIAMLP 84
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP---------VSGEIGLAKGIK-LGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTltfpflarEVVELGAIPLslsnKETTKLALHYMEQTDVLHLA---------ESLYPSLSGGEKQRLHLARVMTQlh 155
Cdd:PRK10636 382 QHQL--------EFLRADESPL----QHLARLAPQELEQKLRDYLGgfgfqgdkvTEETRRFSGGEKARLVLALIVWQ-- 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 156 qsgEKRILMLDEPTSALDLahqhNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:PRK10636 448 ---RPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-256 |
1.05e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.04 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLSGKNISMTYGN------RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYF-----GKQKHD 70
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 71 WEPEKSAKHIAMLPQHSTLTFpfLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARV 150
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVAT--IVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 151 MTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTPwnal 230
Cdd:PRK13633 159 LAM-----RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTP---- 228
|
250 260
....*....|....*....|....*.
gi 491527411 231 tSERIEQVYGYRSIvtkhpTLDFPQV 256
Cdd:PRK13633 229 -KEIFKEVEMMKKI-----GLDVPQV 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-202 |
1.49e-14 |
|
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: 72.89 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 29 RAGEVTALLGPNGAGKSTLLKLLCGEISSNhhityFGkqKHDWEPEKSA--KH-------------------IAMLPQHs 87
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPN-----LG--DYDEEPSWDEvlKRfrgtelqdyfkklangeikVAHKPQY- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 tltfpflarevVELgaIPLSLSNK-----ETT---KLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqlhqSGE 159
Cdd:COG1245 169 -----------VDL--IPKVFKGTvrellEKVderGKLDELAEKLGLENILDRDISELSGGELQRVAIAAAL-----LRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491527411 160 KRILMLDEPTSALDLAHQHNTLKIARETAKAqNAAVVVVLHDL 202
Cdd:COG1245 231 ADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-221 |
1.86e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.37 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKS-AKHIA 81
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASlIDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPqhstltfPFLAreVVE-LGAIPLSlsnkettklalhymeqTDVLHLAesLYPSLSGGEKQRLHLARVMTqlhqSGEK 160
Cdd:COG2401 108 RKG-------DFKD--AVElLNAVGLS----------------DAVLWLR--RFKELSTGQKFRFRLALLLA----ERPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 161 RILMlDEPTSALD------LAhqHNTLKIARETAKaqnaAVVVVLHDLNLASQYA-DRLVLLHNGKLV 221
Cdd:COG2401 157 LLVI-DEFCSHLDrqtakrVA--RNLQKLARRAGI----TLVVATHHYDVIDDLQpDLLIFVGYGGVP 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-213 |
2.51e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 28 IRAGEVTALLGPNGAGKSTLLKLLCGEISSNhhityfgKQKHDWEPEKSAKhiamlPQHSTLTFP-----FLAREVVELG 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPD-------EGEVDPELKISYK-----PQYIKPDYDgtvedLLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 103 AiplSLSNKETTK-LALHymeqtdvlHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTL 181
Cdd:PRK13409 430 S---SYYKSEIIKpLQLE--------RLLDKNVKDLSGGELQRVAIAACLSR-----DADLYLLDEPSAHLDVEQRLAVA 493
|
170 180 190
....*....|....*....|....*....|..
gi 491527411 182 KIARETAKAQNAAVVVVLHDLNLASQYADRLV 213
Cdd:PRK13409 494 KAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-237 |
3.64e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWepekSAKHIAMLP 84
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY----SKRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLTFPFLAREVVEL---GAIPLSLSN-----KETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhq 156
Cdd:PRK13638 77 QQVATVFQDPEQQIFYTdidSDIAFSLRNlgvpeAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 157 sgEKRILMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPWNALT-SERI 235
Cdd:PRK13638 154 --QARYLLLDEPTAGLDPAGRTQMIAIIRRIV-AQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAM 230
|
..
gi 491527411 236 EQ 237
Cdd:PRK13638 231 EQ 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-221 |
3.73e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.94 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLsgKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLcgeissNHHITYFGKQKHDWEPEKSAKHI 80
Cdd:PRK14247 1 MNKIEI--RDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVF------NRLIELYPEARVSGEVYLDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLP-----QHSTLTF----PFLAREVVELGAIPLSL-----SNKETTKLALHYMEQT----DVLHLAESLYPSLSGGEK 142
Cdd:PRK14247 73 FKMDvielrRRVQMVFqipnPIPNLSIFENVALGLKLnrlvkSKKELQERVRWALEKAqlwdEVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 143 QRLHLARVMtqlhqSGEKRILMLDEPTSALDlahQHNTLKIAR---ETAKaqNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:PRK14247 153 QRLCIARAL-----AFQPEVLLADEPTANLD---PENTAKIESlflELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
..
gi 491527411 220 LV 221
Cdd:PRK14247 223 IV 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-213 |
3.90e-14 |
|
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: 71.74 E-value: 3.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 27 DIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHhityfGkqkhdwEPEKSAKhIAMLPQHSTLTFPFLAREVvelgaipl 106
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDE-----G------EVDEDLK-ISYKPQYISPDYDGTVEEF-------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 107 sLSNKETTKLALHYmEQTDVL------HLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNT 180
Cdd:COG1245 422 -LRSANTDDFGSSY-YKTEIIkplgleKLLDKNVKDLSGGELQRVAIAACLSR-----DADLYLLDEPSAHLDVEQRLAV 494
|
170 180 190
....*....|....*....|....*....|...
gi 491527411 181 LKIARETAKAQNAAVVVVLHDLNLASQYADRLV 213
Cdd:COG1245 495 AKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
9-226 |
5.13e-14 |
|
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: 69.06 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN--RVVLDDINIDIRAGEVTALLGPNGAGKST----LLKLLcgEISSNHhITYFGkqkHDWE---PEKSAKH 79
Cdd:cd03244 6 KNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV--ELSSGS-ILIDG---VDISkigLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtF---------PFLAREVVELGAIPLSLSNKETTKlALHYMEQTDVLHLAESLypslSGGEKQRLHLARV 150
Cdd:cd03244 80 ISIIPQDPVL-FsgtirsnldPFGEYSDEELWQALERVGLKEFVE-SLPGGLDTVVEEGGENL----SVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 151 MtqLHQSgekRILMLDEPTSALDLAhqhnTLKIARETAKAQ--NAAVVVVLHDLNLASQYaDRLVLLHNGKLVCDDTP 226
Cdd:cd03244 154 L--LRKS---KILVLDEATASVDPE----TDALIQKTIREAfkDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-201 |
5.24e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.13 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI---SSNHH------ITYFGKQKHDWEPE 74
Cdd:PRK11147 318 IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLqadSGRIHcgtkleVAYFDQHRAELDPE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 75 KSA-KHIAMLPQHstltfpflarevVELGAIPlslsnkettKLALHYMEqtDVL-HLAESLYP--SLSGGEKQRLHLARV 150
Cdd:PRK11147 398 KTVmDNLAEGKQE------------VMVNGRP---------RHVLGYLQ--DFLfHPKRAMTPvkALSGGERNRLLLARL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491527411 151 MtqLHQSGekrILMLDEPTSALDLahqhNTLKIARETAKAQNAAVVVVLHD 201
Cdd:PRK11147 455 F--LKPSN---LLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-219 |
5.81e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.68 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC------GEISSNHHITYFGKQKHDWEP--EKSAKHI 80
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNIYERRVnlNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtFPFLAREVVELGAIPLSLSNK----ETTKLALHYMEQTD-VLHLAESLYPSLSGGEKQRLHLARVMtqlh 155
Cdd:PRK14258 91 SMVHPKPNL-FPMSVYDNVAYGVKIVGWRPKleidDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARAL---- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 156 qSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:PRK14258 166 -AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-221 |
7.25e-14 |
|
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: 70.87 E-value: 7.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEksakhiAMLP--QHSTLTF--PF--- 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRR------ALRPlrRRMQVVFqdPFgsl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 94 ----LAREVVE--LGAIPLSLSNKETTKLALHYMEQTdvlHLAESL---YPS-LSGGEKQRLHLARVMTqLhqsgEKRIL 163
Cdd:COG4172 376 sprmTVGQIIAegLRVHGPGLSAAERRARVAEALEEV---GLDPAArhrYPHeFSGGQRQRIAIARALI-L----EPKLL 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 164 MLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
23-221 |
1.01e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 23 DINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEISSNHHITYFGKQKHDWEPEKsaKHIAMLPQHSTLtFPFLa 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAIsgltrpqKGRIVLNGRVLFDAEKGICLPPEK--RRIGYVFQDARL-FPHY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 96 revvelgaiplslsnkeTTKLALHY-MEQTDVLHLA--------ESL---YP-SLSGGEKQRLHLARVMTQlhqsgEKRI 162
Cdd:PRK11144 92 -----------------KVRGNLRYgMAKSMVAQFDkivallgiEPLldrYPgSLSGGEKQRVAIGRALLT-----APEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 163 LMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-201 |
1.10e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.15 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEissnhhityfgkqkhdwepEKsakhiam 82
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ-------------------EQ------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 lPQHSTltfpflarevVELGaiplslsnkETTKLAlhYMEQT------------------DVLHLAESLYPS-------- 136
Cdd:PRK11819 376 -PDSGT----------IKIG---------ETVKLA--YVDQSrdaldpnktvweeisgglDIIKVGNREIPSrayvgrfn 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 137 ------------LSGGEKQRLHLARVmtqLHQSGEkrILMLDEPTSALDLahqhNTLKiARETAKAQNA-AVVVVLHD 201
Cdd:PRK11819 434 fkggdqqkkvgvLSGGERNRLHLAKT---LKQGGN--VLLLDEPTNDLDV----ETLR-ALEEALLEFPgCAVVISHD 501
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
9-221 |
1.59e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 69.75 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHhityfGKQKHDWEPEKSAKH------IA 81
Cdd:PRK10790 344 DNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE-----GEIRLDGRPLSSLSHsvlrqgVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHST-LTFPFLAR----------------EVVELGAIPLSLSNKETTKLAlhymEQTDvlhlaeslypSLSGGEKQR 144
Cdd:PRK10790 419 MVQQDPVvLADTFLANvtlgrdiseeqvwqalETVQLAELARSLPDGLYTPLG----EQGN----------NLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 145 LHLARVMTQLHQsgekrILMLDEPTSALD----LAHQHnTLKIAREtakaqNAAVVVVLHDLNLASQyADRLVLLHNGKL 220
Cdd:PRK10790 485 LALARVLVQTPQ-----ILILDEATANIDsgteQAIQQ-ALAAVRE-----HTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
.
gi 491527411 221 V 221
Cdd:PRK10790 553 V 553
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-202 |
1.74e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 28 IRAGEVTALLGPNGAGKSTLLKLLCGEISSNhhityFGKQKHDWEPEKSAKH-------------------IAMLPQHST 88
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEVLKRfrgtelqnyfkklyngeikVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 89 LTFPFLAREVVELgaiplsLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEKRILMLDEP 168
Cdd:PRK13409 171 LIPKVFKGKVREL------LKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAAL-----LRDADFYFFDEP 239
|
170 180 190
....*....|....*....|....*....|....
gi 491527411 169 TSALDLAHQHNTLKIARETAKaqNAAVVVVLHDL 202
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL 271
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-221 |
2.14e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.20 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC---GEISSNHH---ITYFGKQKHDW-EPEKSAK 78
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSGYRYsgdVLLGGRSIFNYrDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIAMLPQHSTlTFPFLAREVVELGAIPLSL-SNKETTKLALHYMEQTDVL-----HLAESLYpSLSGGEKQRLHLARVMt 152
Cdd:PRK14271 102 RVGMLFQRPN-PFPMSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWdavkdRLSDSPF-RLSGGQQQLLCLARTL- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 153 qlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAkaQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK14271 179 ----AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLV 241
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-205 |
3.07e-13 |
|
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: 66.61 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIssnhhityfgkqkhdwEPEksAKHIAMLPQ 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLL----------------RPD--SGEVRWNGT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPFLAREVVELG---AIPLSLSNKETTKL--ALHYMEQTDV---------LHLAESLYPSLSGGEKQRLHLARVM 151
Cdd:TIGR01189 63 PLAEQRDEPHENILYLGhlpGLKPELSALENLHFwaAIHGGAQRTIedalaavglTGFEDLPAAQLSAGQQRRLALARLW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 152 TQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLA 205
Cdd:TIGR01189 143 LS-----RRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-221 |
3.46e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.77 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI---------SSNHHITYFGkQKH------- 69
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELepdsgtvkwSENANIGYYA-QDHaydfend 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 70 ----DWEPE-KSAKHiamlpqHSTLTFPFLARevvelgaipLSLSNKETTKLAlhymeqtdvlhlaeslyPSLSGGEKQR 144
Cdd:PRK15064 399 ltlfDWMSQwRQEGD------DEQAVRGTLGR---------LLFSQDDIKKSV-----------------KVLSGGEKGR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 145 LHLARVMTQLHQsgekrILMLDEPTSALDLahqhntlkiarETAKAQNAA-------VVVVLHDLNLASQYADRLVLLHN 217
Cdd:PRK15064 447 MLFGKLMMQKPN-----VLVMDEPTNHMDM-----------ESIESLNMAlekyegtLIFVSHDREFVSSLATRIIEITP 510
|
....
gi 491527411 218 GKLV 221
Cdd:PRK15064 511 DGVV 514
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-173 |
8.14e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGeISSNhhitYFGKQKhdwePEKSAKhIA 81
Cdd:TIGR03719 2 QYIYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKD----FNGEAR----PQPGIK-VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 82 MLPQHSTLTFPFLAREVVELGAIPL--------SLSNK------ETTKLA--------------LHYMEQT-----DVLH 128
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEEGVAEIkdaldrfnEISAKyaepdaDFDKLAaeqaelqeiidaadAWDLDSQleiamDALR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491527411 129 LAESLYP--SLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALD 173
Cdd:TIGR03719 152 CPPWDADvtKLSGGERRRVALCRLLLS-----KPDMLLLDEPTNHLD 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
1.07e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.36 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQKHDWEPEKSAKHIAM 82
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHST-LTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKR 161
Cdd:PRK13652 83 VFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM-----EPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 162 ILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTV 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-226 |
1.23e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.96 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGN-----RVVLDDINIDIRAGEVTALLGPNGAGKSTL-------LKLLCGEISSNHhITYFGKQKHdwepeks 76
Cdd:PRK13646 6 DNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLiqninalLKPTTGTVTVDD-ITITHKTKD------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 77 aKHIAMLPQHSTLTFPF---------LAREVvELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYP-SLSGGEKQRLH 146
Cdd:PRK13646 78 -KYIRPVRKRIGMVFQFpesqlfedtVEREI-IFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 147 LARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13646 156 IVSILAM-----NPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
9-226 |
1.53e-12 |
|
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: 64.74 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRV--VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI-SSNHHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:cd03369 10 ENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLeAEEGKIEIDGIDISTIPLEDLRSSLTIIPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTfpflarevveLGAIPLSLSNkettklalhYMEQTDVlHLAESLYPS-----LSGGEKQRLHLARVMTqlhqsGEK 160
Cdd:cd03369 90 DPTLF----------SGTIRSNLDP---------FDEYSDE-EIYGALRVSegglnLSQGQRQLLCLARALL-----KRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETakAQNAAVVVVLHDLNLASQYaDRLVLLHNGKLVCDDTP 226
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREE--FTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-221 |
2.25e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 66.52 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGN-RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLcgeissnH--------HITYFGKQKHDWEPEKSAKHI 80
Cdd:PRK13657 339 DVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL-------QrvfdpqsgRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLtfpfLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYP--------SLSGGEKQRLHLARVMT 152
Cdd:PRK13657 412 AVVFQDAGL----FNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 153 QlhqsgEKRILMLDEPTSALDlAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:PRK13657 488 K-----DPPILILDEATSALD-VETEAKVKAALDELM-KGRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-221 |
3.94e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.50 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 14 TYGNRVVLDDINIDIRAGEVTALLGPNGAGKST----LLKLlcgeISSNHHITYFGKQKHDWEPEKsakhiaMLP----- 84
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRL----INSQGEIWFDGQPLHNLNRRQ------LLPvrhri 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 ------QHSTLTFPFLAREVVELGaipL-----SLSNKETTKLALHYMEQTDVLHLAESLYPS-LSGGEKQRLHLARVMT 152
Cdd:PRK15134 365 qvvfqdPNSSLNPRLNVLQIIEEG---LrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 153 QlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK15134 442 L-----KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
6-219 |
4.17e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTY----GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITyfGKQKHDWE-----PEKS 76
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIG--GSATFNGReilnlPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 77 -----AKHIAMLPQHS-TLTFPFL--AREVVELGAIPLSLSNKETTKLALHYMeqtDVLHLAES-----LYP-SLSGGEK 142
Cdd:PRK09473 91 lnklrAEQISMIFQDPmTSLNPYMrvGEQLMEVLMLHKGMSKAEAFEESVRML---DAVKMPEArkrmkMYPhEFSGGMR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 143 QRLHLArvMTQLHQSgekRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:PRK09473 168 QRVMIA--MALLCRP---KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-221 |
4.38e-12 |
|
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: 65.61 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEISSNHH-ITyfgkqkhDWEPEKSAKH 79
Cdd:COG5265 361 ENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtSGRILIDGQdIR-------DVTQASLRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLtF------------PFLAREVVELGAiplslsnkettKLA-LHymeqtdvlHLAESL---YPS------- 136
Cdd:COG5265 434 IGIVPQDTVL-FndtiayniaygrPDASEEEVEAAA-----------RAAqIH--------DFIESLpdgYDTrvgergl 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 -LSGGEKQRLHLARVMtqLHQSgekRILMLDEPTSALDLAHQHNTLKIARETakAQNAAVVVVLHDLnlaS--QYADRLV 213
Cdd:COG5265 494 kLSGGEKQRVAIARTL--LKNP---PILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRL---StiVDADEIL 563
|
....*...
gi 491527411 214 LLHNGKLV 221
Cdd:COG5265 564 VLEAGRIV 571
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-226 |
5.48e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.05 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFG----KQKHDWE-PEKSAKHI 80
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiAKISDAElREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLTFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEK 160
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARAL-----AINP 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 161 RILMLDEPTSALD-LAHQHNTLKIARETAKAQNaAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTP 226
Cdd:PRK10070 184 DILLMDEAFSALDpLIRTEMQDELVKLQAKHQR-TIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-235 |
5.55e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMT-YGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKH-I 80
Cdd:COG3845 256 VVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASgSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQ--HST---LTFPflareVVE---LGAI---PLS----LSNKETTKLALHYMEQTDVLhlAESLYP---SLSGGEK 142
Cdd:COG3845 336 AYIPEdrLGRglvPDMS-----VAEnliLGRYrrpPFSrggfLDRKAIRAFAEELIEEFDVR--TPGPDTparSLSGGNQ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 143 QRLHLARVMtqlhqSGEKRILMLDEPTSALDL---AHQHNTLKIAREtakaQNAAVVVVLHDLNLASQYADRLVLLHNGK 219
Cdd:COG3845 409 QKVILAREL-----SRDPKLLIAAQPTRGLDVgaiEFIHQRLLELRD----AGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
250
....*....|....*.
gi 491527411 220 LVcDDTPWNALTSERI 235
Cdd:COG3845 480 IV-GEVPAAEATREEI 494
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-218 |
1.06e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 62.73 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQHSTLTFPFLAREVVE 100
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 101 LGAIPLSLSNKETTKL---ALHYMEQTDVLHLAESLY-----PSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSAL 172
Cdd:cd03290 97 ENITFGSPFNKQRYKAvtdACSLQPDIDLLPFGDQTEigergINLSGGQRQRICVARALYQ-----NTNIVFLDDPFSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491527411 173 DL-----AHQHNTLKIARETAKaqnaAVVVVLHDLNLASqYADRLVLLHNG 218
Cdd:cd03290 172 DIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-235 |
2.55e-11 |
|
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: 63.31 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYF--GKQKHDWEPEKSAKH-IAMLP------------- 84
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFinGKPVDIRNPAQAIRAgIAMVPedrkrhgivpilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 --QHSTLT----FPFLAR--EVVELGAIPLSLSNkettklaLHYMEQTDVLHLAeslypSLSGGEKQRLHLARVMtqlhq 156
Cdd:TIGR02633 356 vgKNITLSvlksFCFKMRidAAAELQIIGSAIQR-------LKVKTASPFLPIG-----RLSGGNQQKAVLAKML----- 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 157 SGEKRILMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLvCDDTPWNALTSERI 235
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGKL-KGDFVNHALTQEQV 495
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-173 |
3.40e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTYG-NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGeISSNhhitYFGKQKhdwePEKSAKh 79
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKE----FEGEAR----PAPGIK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQHSTLTFPFLAREVVELG------------------AIPLSLSNK---ETTKL-----AL------HYMEQT-DV 126
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVEEGvaevkaaldrfneiyaayAEPDADFDAlaaEQGELqeiidAAdawdldSQLEIAmDA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491527411 127 LHL--AESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALD 173
Cdd:PRK11819 152 LRCppWDAKVTKLSGGERRRVALCRLLLE-----KPDMLLLDEPTNHLD 195
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-173 |
3.87e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNhhiTYFGK-QKHDWEPEKSA-KHIAMLPQHSTLtFPFLA 95
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN---NFTGTiLANNRKPTKQIlKRTGFVTQDDIL-YPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 96 -REV---VELGAIPLSLSNKETTKLA--------LHYMEQTDVlhlAESLYPSLSGGEKQRLHLARVMTqLHQSgekrIL 163
Cdd:PLN03211 157 vRETlvfCSLLRLPKSLTKQEKILVAesviselgLTKCENTII---GNSFIRGISGGERKRVSIAHEML-INPS----LL 228
|
170
....*....|
gi 491527411 164 MLDEPTSALD 173
Cdd:PLN03211 229 ILDEPTSGLD 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
9-231 |
4.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.54 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRV-VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSAKHIAMLPQH 86
Cdd:PRK13644 5 ENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKgKVLVSGIDTGDFSKLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 87 STLTfPFLAREVVE---LGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRIL 163
Cdd:PRK13644 85 NPET-QFVGRTVEEdlaFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM-----EPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 164 MLDEPTSALDLAHQHNTL-KIARETAKAQNaaVVVVLHDLNlASQYADRLVLLHNGKLVCDDTPWNALT 231
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLeRIKKLHEKGKT--IVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
9-221 |
5.04e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 62.34 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNR--VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSAKHIAMLP 84
Cdd:PRK11176 345 RNVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRfyDIDEGE-ILLDGHDLRDYTLASLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 85 QHSTLTFPFLA------------REVVELGAiplslsnkettKLAlHYMEQTDvlHLAESLYP-------SLSGGEKQRL 145
Cdd:PRK11176 424 QNVHLFNDTIAnniayarteqysREQIEEAA-----------RMA-YAMDFIN--KMDNGLDTvigengvLLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 146 HLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaqNAAVVVVLHDLNLASQyADRLVLLHNGKLV 221
Cdd:PRK11176 490 AIARALLR-----DSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIV 557
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-221 |
5.12e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSgkNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYfgkqkhdwepEKSAKh 79
Cdd:PRK11147 1 MSLISIH--GAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLlDDGRIIY----------EQDLI- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAML----PQHSTLT-FPFLAREVVELGA-----------IPLSLSNKETTKLAlHYMEQTDVLHL-------------- 129
Cdd:PRK11147 68 VARLqqdpPRNVEGTvYDFVAEGIEEQAEylkryhdishlVETDPSEKNLNELA-KLQEQLDHHNLwqlenrinevlaql 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 130 ---AESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAhqhnTLKIARETAKAQNAAVVVVLHDLNLAS 206
Cdd:PRK11147 147 gldPDAALSSLSGGWLRKAALGRALVS-----NPDVLLLDEPTNHLDIE----TIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
250
....*....|....*
gi 491527411 207 QYADRLVLLHNGKLV 221
Cdd:PRK11147 218 NMATRIVDLDRGKLV 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-173 |
5.69e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 2 NQIVLsgKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE--ISSNHHITYFGKQKHD----WEPEk 75
Cdd:PRK10938 259 PRIVL--NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpQGYSNDLTLFGRRRGSgetiWDIK- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 saKHIAMLPqhSTLTFPF----LAREVVELG-----AIPLSLSNKEtTKLAlhyMEQTDVLHLAESL----YPSLSGGEk 142
Cdd:PRK10938 336 --KHIGYVS--SSLHLDYrvstSVRNVILSGffdsiGIYQAVSDRQ-QKLA---QQWLDILGIDKRTadapFHSLSWGQ- 406
|
170 180 190
....*....|....*....|....*....|..
gi 491527411 143 QRLHL-ARVMTQlHQSgekrILMLDEPTSALD 173
Cdd:PRK10938 407 QRLALiVRALVK-HPT----LLILDEPLQGLD 433
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-235 |
6.95e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSA--KHIAMLPQH 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAleNGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 87 STLTfpfLAREVVE---LGAIPLS---LSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEK 160
Cdd:PRK10982 82 LNLV---LQRSVMDnmwLGRYPTKgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAF-----SYNA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLVcDDTPWNALTSERI 235
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI-ATQPLAGLTMDKI 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-221 |
1.00e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISmtygNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSAKH-I 80
Cdd:COG1129 255 VVLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGadPADSGE-IRLDGKPVRIRSPRDAIRAgI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLP----------QHS---TLTFPFLARevveLGAIPLsLSNKETTKLALHYMEQTDV-LHLAESLYPSLSGGEKQRLH 146
Cdd:COG1129 330 AYVPedrkgeglvlDLSireNITLASLDR----LSRGGL-LDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 147 LARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG1129 405 LAKWLAT-----DPKVLILDEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-221 |
1.49e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 23 DINIDIRAGEVTALLGPNGAGKS----TLLKLL---CGEISS--------NHHITYFGKQKHDWEPEKSAKHIAMLPQHS 87
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCdkmllrrrSRQVIELSEQSAAQMRHVRGADMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 88 TLT----FPfLAREVVELGAIPLSLSNKETTKLALHYMEQTDV--LHLAESLYP-SLSGGEKQRlhlarVMTQLHQSGEK 160
Cdd:PRK10261 114 MTSlnpvFT-VGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeAQTILSRYPhQLSGGMRQR-----VMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-226 |
2.30e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.72 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIvLSGKNISMTYGNRVVLDDIN---IDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSA 77
Cdd:PRK13642 1 MNKI-LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 KH-IAMLPQHSTLTF-PFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlh 155
Cdd:PRK13642 80 RRkIGMVFQNPDNQFvGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL-- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 156 qsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTP 226
Cdd:PRK13642 158 ---RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAP 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-53 |
2.43e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 2.43e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 491527411 10 NISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG 53
Cdd:NF033858 6 GVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAG 49
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-221 |
2.95e-10 |
|
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: 58.02 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMT----YGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-----GEISSNhhITYFGKQKhdwePEK 75
Cdd:cd03232 3 VLTWKNLNYTvpvkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVITGE--ILINGRPL----DKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 SAKHIAMLPQHSTLtFPFLA-REVVELGAiplslsnkettklalhymeqtdvlhlaesLYPSLSGGEKQRLHLARVMTQL 154
Cdd:cd03232 77 FQRSTGYVEQQDVH-SPNLTvREALRFSA-----------------------------LLRGLSVEQRKRLTIGVELAAK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 155 HQsgekrILMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLAS-QYADRLVLLH-NGKLV 221
Cdd:cd03232 127 PS-----ILFLDEPTSGLDSQAAYNIVRFLKKLA-DSGQAILCTIHQPSASIfEKFDRLLLLKrGGKTV 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-214 |
3.53e-10 |
|
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: 57.89 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 6 LSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIssnhhityfgkqkhdwepEKSAKHIAMLPQ 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLS------------------PPLAGRVLLNGG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPFLAREVVELGAIP-----LS----------LSNKETTKLALHYMEQTDVLHLAeslYPSLSGGEKQRLHLARV 150
Cdd:cd03231 63 PLDFQRDSIARGLLYLGHAPgikttLSvlenlrfwhaDHSDEQVEEALARVGLNGFEDRP---VAQLSAGQQRRVALARL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491527411 151 MTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVL 214
Cdd:cd03231 140 LLS-----GRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-221 |
4.49e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 58.82 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTY--------GNRVV--LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQ-- 67
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMiETPTGGELYYQGQDll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 68 KHDWEPEKSA-KHIAMLPQHstltfPFLA---REVVelGAI---PL----SLSNKETTKLALHYMEQTDVLHLAESLYPS 136
Cdd:PRK11308 81 KADPEAQKLLrQKIQIVFQN-----PYGSlnpRKKV--GQIleePLlintSLSAAERREKALAMMAKVGLRPEHYDRYPH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 L-SGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLL 215
Cdd:PRK11308 154 MfSGGQRQRIAIARALML-----DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVM 228
|
....*.
gi 491527411 216 HNGKLV 221
Cdd:PRK11308 229 YLGRCV 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-222 |
5.56e-10 |
|
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: 59.64 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS-SNHHITYFGKQkhdWEPEKSAKHIAM--LPQHSTLTFPFLARE 97
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTvTSGDATVAGKS---ILTNISDVHQNMgyCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 98 VVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTqlhqsGEKRILMLDEPTSALDLAHQ 177
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI-----GCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491527411 178 H---NTL-KIAREtakaqNAAVVVVLHDLNLASQYADRLVLLHNGKLVC 222
Cdd:TIGR01257 2107 RmlwNTIvSIIRE-----GRAVVLTSHSMEECEALCTRLAIMVKGAFQC 2150
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-221 |
7.86e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 58.38 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 16 GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHIT-----YFGKQKHDWEPEKS----AKHIAMLPQH 86
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTadrfrWNGIDLLKLSPRERrkiiGREIAMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 87 -STLTFPF--LAREVVElgAIPLS-LSN---------KETTKLALHYMEQTDVLHLAESlYP-SLSGGEKQRLHLArvMT 152
Cdd:COG4170 98 pSSCLDPSakIGDQLIE--AIPSWtFKGkwwqrfkwrKKRAIELLHRVGIKDHKDIMNS-YPhELTEGECQKVMIA--MA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 153 QLHQSgekRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:COG4170 173 IANQP---RLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-221 |
7.88e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 22 DDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEI-SSNHHITYFGK-----QKHDWEPEKsaKHIAMLPQHStltfpfLA 95
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVkATDGEVAWLGKdllgmKDDEWRAVR--SDIQMIFQDP------LA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 96 R-----EVVELGAIPLSLSNKETTKLALhyMEQTDVLHLAESLYPSL--------SGGEKQRLHLARVMTQlhqsgEKRI 162
Cdd:PRK15079 110 SlnprmTIGEIIAEPLRTYHPKLSRQEV--KDRVKAMMLKVGLLPNLinryphefSGGQCQRIGIARALIL-----EPKL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 163 LMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-221 |
8.74e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.88 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVL---------DDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSNHHITYFGKQK 68
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAgmieptsGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 69 HdwepekSAKHIAMLPQHSTLTFPFLAReVVELGAIPL----SLSNKETTKLALHYMEQTDVLHLAESLYPS-LSGGEKQ 143
Cdd:PRK15112 84 Y------RSQRIRMIFQDPSTSLNPRQR-ISQILDFPLrlntDLEPEQREKQIIETLRQVGLLPDHASYYPHmLAPGQKQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491527411 144 RLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK15112 157 RLGLARALIL-----RPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-200 |
1.08e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG----EISSNhHITYFGKQKHDWEPEKSAKHI 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGredyEVTGG-TVEFKGKDLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLTFP------FLAREVVEL----GAIPL---SLSNKETTKLALHYMEQtDVlhLAESLYPSLSGGEKQRLHL 147
Cdd:PRK09580 80 IFMAFQYPVEIPgvsnqfFLQTALNAVrsyrGQEPLdrfDFQDLMEEKIALLKMPE-DL--LTRSVNVGFSGGEKKRNDI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 148 ARvMTQLhqsgEKRILMLDEPTSALDLahqhNTLKIARE---TAKAQNAAVVVVLH 200
Cdd:PRK09580 157 LQ-MAVL----EPELCILDESDSGLDI----DALKIVADgvnSLRDGKRSFIIVTH 203
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-238 |
1.36e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.55 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLsgKNISMTYGNRV-VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKQKHDWEPekSA 77
Cdd:PRK11650 1 MAGLKL--QAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGleRITSG-EIWIGGRVVNELEP--AD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 KHIAMLPQHSTLtFPFLA-REVVELGaiplsLSNKETTKlalhymEQTD--VLHLAESL--------YPS-LSGGEKQRL 145
Cdd:PRK11650 76 RDIAMVFQNYAL-YPHMSvRENMAYG-----LKIRGMPK------AEIEerVAEAARILeleplldrKPReLSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 146 HLARVMTQlhqsgEKRILMLDEPTSALDLAhqhntLKIA-R-ETAKAQ---NAAVVVVLHDLNLASQYADRLVLLHNGkl 220
Cdd:PRK11650 144 AMGRAIVR-----EPAVFLFDEPLSNLDAK-----LRVQmRlEIQRLHrrlKTTSLYVTHDQVEAMTLADRVVVMNGG-- 211
|
250
....*....|....*...
gi 491527411 221 vcddtpwnaltseRIEQV 238
Cdd:PRK11650 212 -------------VAEQI 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-221 |
1.54e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-----HITYFGKQKHDWEPEKSAK---------HIAMLPQ 85
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigvegVITYDGITPEEIKKHYRGDvvynaetdvHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HSTLTFPFLAREVvelGAIPLSLSNKE-TTKLALHYMEQTDVLH-----LAESLYPSLSGGEKQRLHLARVMTqlhqsGE 159
Cdd:TIGR00956 156 GETLDFAARCKTP---QNRPDGVSREEyAKHIADVYMATYGLSHtrntkVGNDFVRGVSGGERKRVSIAEASL-----GG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 160 KRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDlnlASQYA----DRLVLLHNGKLV 221
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQ---CSQDAyelfDKVIVLYEGYQI 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-199 |
2.21e-09 |
|
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: 57.61 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAM 82
Cdd:TIGR01271 1217 QMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQhSTLTFPFLAREVVELGAiplSLSNKETTKLAlhymEQTDVLHLAESlYPS------------LSGGEKQRLHLARV 150
Cdd:TIGR01271 1297 IPQ-KVFIFSGTFRKNLDPYE---QWSDEEIWKVA----EEVGLKSVIEQ-FPDkldfvlvdggyvLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491527411 151 MTQlhqsgEKRILMLDEPTSALDLAhqhnTLKIARETAKAQNAAVVVVL 199
Cdd:TIGR01271 1368 ILS-----KAKILLLDEPSAHLDPV----TLQIIRKTLKQSFSNCTVIL 1407
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-221 |
2.25e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQiVLSGKNISMtYGNRVVLDDINIDIRAGEVTALLGPNGAGKS----TLLKLLCGEISSNHhityfGKQKHDWEPEKS 76
Cdd:PRK10418 1 MPQ-QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTA-----GRVLLDGKPVAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 77 A----KHIAMLPQHSTLTF-PF--LAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAEsLYP-SLSGGEKQRLhla 148
Cdd:PRK10418 74 CalrgRKIATIMQNPRSAFnPLhtMHTHARETCLALGKPADDATLTAALEAVGLENAARVLK-LYPfEMSGGMLQRM--- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 149 rvMTQLHQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK10418 150 --MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
26-210 |
3.17e-09 |
|
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: 55.31 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 26 IDIRAGeVTALLGPNGAGKSTL---LKLLC-GEISSNhhiTYFGKqkHDwepeksakhiamlpqhstltfPFLAREVVEL 101
Cdd:cd03240 18 IEFFSP-LTLIVGQNGAGKTTIieaLKYALtGELPPN---SKGGA--HD---------------------PKLIREGEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 102 GAIPLSLSNKETTKL----ALHYMEQTDVLHLAESLYP------SLSGGEKQ------RLHLARVMtqlhqSGEKRILML 165
Cdd:cd03240 71 AQVKLAFENANGKKYtitrSLAILENVIFCHQGESNWPlldmrgRCSGGEKVlasliiRLALAETF-----GSNCGILAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491527411 166 DEPTSALDLAHQHNTL-KIARETAKAQNAAVVVVLHDLNLAsQYAD 210
Cdd:cd03240 146 DEPTTNLDEENIEESLaEIIEERKSQKNFQLIVITHDEELV-DAAD 190
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
134-221 |
4.78e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 55.90 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 134 YP-SLSGGEKQRlhlarVMTQLHQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRL 212
Cdd:PRK11022 150 YPhQLSGGMSQR-----VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
....*....
gi 491527411 213 VLLHNGKLV 221
Cdd:PRK11022 225 IVMYAGQVV 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-235 |
5.06e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNIS---MTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYF--GKQKHDWEPEKSAK 78
Cdd:PRK13549 258 VILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFidGKPVKIRNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 H-IAMLP---------------QHSTL------TFPFLAREVVELGAIplslsNKETTKLALhymeQTDVLHLAESlypS 136
Cdd:PRK13549 338 QgIAMVPedrkrdgivpvmgvgKNITLaaldrfTGGSRIDDAAELKTI-----LESIQRLKV----KTASPELAIA---R 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 LSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLH 216
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLL-----NPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVMH 479
|
250
....*....|....*....
gi 491527411 217 NGKLvCDDTPWNALTSERI 235
Cdd:PRK13549 480 EGKL-KGDLINHNLTQEQV 497
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-226 |
5.25e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYG---NRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE--------ISSNHHITyfgkQKHDWEPEKsa 77
Cdd:PRK13650 8 KNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLleaesgqiIIDGDLLT----EENVWDIRH-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 78 kHIAMLPQHSTLTFPFLAREV-VELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTQlhq 156
Cdd:PRK13650 82 -KIGMVFQNPDNQFVGATVEDdVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM--- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 157 sgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASqYADRLVLLHNGKLVCDDTP 226
Cdd:PRK13650 158 --RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTP 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-221 |
6.19e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 24 INIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSAKH-IAMLPQHstltfpflaREvvEL 101
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGaTRRTAGQVYLDGKPIDIRSPRDAIRAgIMLCPED---------RK--AE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 102 GAIPLS--------------------LSNKETTKLALHYMEQTDV-LHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEK 160
Cdd:PRK11288 341 GIIPVHsvadninisarrhhlragclINNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWL-----SEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELA-AQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-218 |
7.61e-09 |
|
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: 55.25 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHhityfGKQKHdwepeksAKHIAMLPQHSTLtFPFLAREVV 99
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSE-----GKIKH-------SGRISFSSQFSWI-MPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 100 ELGAIPLSLSNKETTKLAlhyMEQTDVLHLAESLYP-------SLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSAL 172
Cdd:cd03291 119 IFGVSYDEYRYKSVVKAC---QLEEDITKFPEKDNTvlgeggiTLSGGQRARISLARAVYK-----DADLYLLDSPFGYL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491527411 173 DLAHQHNTLKIARETAKAQNAAVVVVLHDLNLasQYADRLVLLHNG 218
Cdd:cd03291 191 DVFTEKEIFESCVCKLMANKTRILVTSKMEHL--KKADKILILHEG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
10-204 |
8.41e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 10 NISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLpQHSTL 89
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFV-GHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 TFPFLAREVVELGAIPLSLSNKETTKLAL-----HYMEqtdvlhlaeslYPS--LSGGEKQRLHLARvmtqLHQSGEKrI 162
Cdd:PRK13540 85 INPYLTLRENCLYDIHFSPGAVGITELCRlfsleHLID-----------YPCglLSSGQKRQVALLR----LWMSKAK-L 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491527411 163 LMLDEPTSALD-LAHQHNTLKIarETAKAQNAAVVVVLH-DLNL 204
Cdd:PRK13540 149 WLLDEPLVALDeLSLLTIITKI--QEHRAKGGAVLLTSHqDLPL 190
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-221 |
8.83e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.49 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEISSnHHITYFGKQKHDWEpeksaKHIAMLPQHstltfP 92
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQrhfdvseGDIRF-HDIPLTKLQLDSWR-----SRLAVVSQT-----P 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 93 FLAREVVelgAIPLSLSNKETTKLALHYMEQ-----TDVLHLAESlYPS--------LSGGEKQRLHLARVMTQlhqsgE 159
Cdd:PRK10789 399 FLFSDTV---ANNIALGRPDATQQEIEHVARlasvhDDILRLPQG-YDTevgergvmLSGGQKQRISIARALLL-----N 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491527411 160 KRILMLDEPTSALDLAHQHNTLKIARETakAQNAAVVVVLHDLNlASQYADRLVLLHNGKLV 221
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQW--GEGRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-216 |
1.04e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.34 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 27 DIRAGEVTALLGPNGAGKSTLLKLLCGEISSNhhityfgKQKHDWEPEKsakhIAMLPQhstltfpflarevvelgaipl 106
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPN-------GDNDEWDGIT----PVYKPQ--------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 107 slsnkettklalhymeqtdvlhlaeslYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARE 186
Cdd:cd03222 69 ---------------------------YIDLSGGELQRVAIAAALLR-----NATFYLFDEPSAYLDIEQRLNAARAIRR 116
|
170 180 190
....*....|....*....|....*....|
gi 491527411 187 TAKAQNAAVVVVLHDLNLASQYADRLVLLH 216
Cdd:cd03222 117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-221 |
2.42e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 13 MTYGNRV-VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYFGKQKHDWE-----PEKSAK----HIAM 82
Cdd:PRK15093 14 KTSDGWVkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDllrlsPRERRKlvghNVSM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 L---PQHSTLTFPFLAREVVElgAIP-----------LSLSNKETTKLaLHYMEQTDVLHLAESLYPSLSGGEKQRlhla 148
Cdd:PRK15093 94 IfqePQSCLDPSERVGRQLMQ--NIPgwtykgrwwqrFGWRKRRAIEL-LHRVGIKDHKDAMRSFPYELTEGECQK---- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491527411 149 rVMTQLHQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK15093 167 -VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
9-234 |
2.43e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNhHITYFGKqkhdwepEKSAKHIAM---- 82
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGllPASEG-EAWLFGQ-------PVDAGDIATrrrv 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 --LPQ----HSTLTfpflAREVVELGA----IPLSLSNKETTKLalhyMEQTDVLHLAESLYPSLSGGEKQRLHLARVMt 152
Cdd:NF033858 342 gyMSQafslYGELT----VRQNLELHArlfhLPAAEIAARVAEM----LERFDLADVADALPDSLPLGIRQRLSLAVAV- 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 153 qLHqsgEKRILMLDEPTSALDlahqhntlKIAR--------ETAKAQNAAVVVVLHDLNLAsQYADRLVLLHNGK-LVCd 223
Cdd:NF033858 413 -IH---KPELLILDEPTSGVD--------PVARdmfwrlliELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRvLAS- 478
|
250
....*....|.
gi 491527411 224 DTPwNALTSER 234
Cdd:NF033858 479 DTP-AALVAAR 488
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
15-223 |
2.45e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 15 YGNRVVLDDINIDIRAGEVTALLGPNGAG--KSTLLKLLCGEISSNHHITYFgkqkhDWEPEKSAKHIAM---LPQHSTL 89
Cdd:NF000106 23 FGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*-----TWCANRRALRRTIg*hRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 TFPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVMTqlhqsGEKRILMLDEPT 169
Cdd:NF000106 98 RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI-----GRPAVLYLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 170 SALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCD 223
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVIDRGRVIAD 225
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
5-53 |
3.07e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 3.07e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG 53
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG 49
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-220 |
3.45e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 23 DINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEIS-SNHHITYFGKQkhdwepEKSAKHIAMLP---QHSTLTF 91
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLyglrparGGRIMlNGKEINALSTA------QRLARGLVYLPedrQSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 92 --PfLAREVVEL--GAIPLSLSNKETTKLALHYMEQTDV-LHLAESLYPSLSGGEKQRLHLARVMtqlhqSGEKRILMLD 166
Cdd:PRK15439 355 daP-LAWNVCALthNRRGFWIKPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCL-----EASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491527411 167 EPTSALDLAHQHNTLKIARETAkAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-220 |
4.51e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTY-GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHHITYfgkqkhdwepeKSAK-HIAM 82
Cdd:PLN03073 508 IISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKvRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 LPQHSTltfpflarEVVELGAIPLslsnkettklaLHYM-------EQTDVLHLA----------ESLYpSLSGGEKQRL 145
Cdd:PLN03073 577 FSQHHV--------DGLDLSSNPL-----------LYMMrcfpgvpEQKLRAHLGsfgvtgnlalQPMY-TLSGGQKSRV 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 146 HLARVMTQlhqsgEKRILMLDEPTSALDLahqhNTLKIARETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:PLN03073 637 AFAKITFK-----KPHILLLDEPSNHLDL----DAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-220 |
5.01e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 16 GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEIS--SNHHITYFGKqkhdwepeksakhIAMLPQHSTLtFPF 93
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPprSDASVVIRGT-------------VAYVPQVSWI-FNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 94 LAREVVELGAiPLSlsnkettklALHYMEQTDVLHLAE--SLYP------------SLSGGEKQRLHLARVMTqlhqsGE 159
Cdd:PLN03130 694 TVRDNILFGS-PFD---------PERYERAIDVTALQHdlDLLPggdlteigergvNISGGQKQRVSMARAVY-----SN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491527411 160 KRILMLDEPTSALDlAHqhntlkIARET------AKAQNAAVVVVLHDLNLASQyADRLVLLHNGKL 220
Cdd:PLN03130 759 SDVYIFDDPLSALD-AH------VGRQVfdkcikDELRGKTRVLVTNQLHFLSQ-VDRIILVHEGMI 817
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-218 |
7.69e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHhityfGKQKHdwepeksAKHIAMLPQHSTLtFPFLAREVV 99
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE-----GKIKH-------SGRISFSPQTSWI-MPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 100 ELGaiplsLSNKEttklaLHYMEQTDVLHLAE--SLYP------------SLSGGEKQRLHLARVMTQlhqsgEKRILML 165
Cdd:TIGR01271 508 IFG-----LSYDE-----YRYTSVIKACQLEEdiALFPekdktvlgeggiTLSGGQRARISLARAVYK-----DADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491527411 166 DEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLasQYADRLVLLHNG 218
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHL--KKADKILLLHEG 623
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
9-235 |
8.09e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 53.03 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTY--GNRVVLDDINIDIRAGEVTALLGPNGAGKSTL-LKLLCGEISSNHHITYFGKQKHDWEPEKSAKHIAMLPQ 85
Cdd:TIGR00957 1288 RNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 86 HstltfPFLAREVVELGAIPLSLSNKETTKLALHYMEqtdvLHLAESLYP------------SLSGGEKQRLHLARVMTQ 153
Cdd:TIGR00957 1368 D-----PVLFSGSLRMNLDPFSQYSDEEVWWALELAH----LKTFVSALPdkldhecaeggeNLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 154 lhqsgEKRILMLDEPTSALDLahqhNTLKIARETAKAQ--NAAVVVVLHDLNLASQYAdRLVLLHNGKLVCDDTPWNALT 231
Cdd:TIGR00957 1439 -----KTKILVLDEATAAVDL----ETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
....
gi 491527411 232 SERI 235
Cdd:TIGR00957 1509 QRGI 1512
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-220 |
2.34e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.48 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISS-NHHITYFGKqkhdwepeksakhIAMLPQHSTLTFPFLaREVV 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKvEGHVHMKGS-------------VAYVPQQAWIQNDSL-RENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 100 ELGAiPLSLSNKETTKLA------LHYMEQTDVLHLAESLYpSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALD 173
Cdd:TIGR00957 720 LFGK-ALNEKYYQQVLEAcallpdLEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYS-----NADIYLFDDPLSAVD 792
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491527411 174 lAH--QHNTLKIARETAKAQNAAVVVVLHDLNLASQyADRLVLLHNGKL 220
Cdd:TIGR00957 793 -AHvgKHIFEHVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKI 839
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-176 |
3.43e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEissnhhityFGKQKHDWEPEKSakhIAMLPQHstltfPFLARE 97
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQ---------FEISEGRVWAERS---IAYVPQQ-----AWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 98 VVElGAIpLSLSNKETTKLA----LHYMEqTDVLHLAESLYP-------SLSGGEKQRLHLARVMTqlhqsGEKRILMLD 166
Cdd:PTZ00243 736 TVR-GNI-LFFDEEDAARLAdavrVSQLE-ADLAQLGGGLETeigekgvNLSGGQKARVSLARAVY-----ANRDVYLLD 807
|
170
....*....|
gi 491527411 167 EPTSALDlAH 176
Cdd:PTZ00243 808 DPLSALD-AH 816
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-213 |
3.61e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLkLLCGEISsnhhityfGKQKHDWEPEKSAKH-IAMLPQHSTLTfpflarevv 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-NEGLYAS--------GKARLISFLPKFSRNkLIFIDQLQFLI--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 100 elgaiplslsnkettKLALHYmeqtdvLHLAESLyPSLSGGEKQRLHLArvmTQLHQSGEKRILMLDEPTSALDlahqHN 179
Cdd:cd03238 73 ---------------DVGLGY------LTLGQKL-STLSGGELQRVKLA---SELFSEPPGTLFILDEPSTGLH----QQ 123
|
170 180 190
....*....|....*....|....*....|....*..
gi 491527411 180 TLKIARETAKA---QNAAVVVVLHDLNLaSQYADRLV 213
Cdd:cd03238 124 DINQLLEVIKGlidLGNTVILIEHNLDV-LSSADWII 159
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-230 |
4.53e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 28 IRAGEVTALLGPNGAGKSTLLKLLCGEISSNhhITYFGKQKHDWEP--EKSAKHIAMLPQHSTLTFPFL-AREVVELGAI 104
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKG--VKGSGSVLLNGMPidAKEMRAISAYVQQDDLFIPTLtVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 105 pLSLSNKETTKLALHYMEQT-DVLHL---------AESLYPSLSGGEKQRLHLA-RVMTQLHqsgekrILMLDEPTSALD 173
Cdd:TIGR00955 126 -LRMPRRVTKKEKRERVDEVlQALGLrkcantrigVPGRVKGLSGGERKRLAFAsELLTDPP------LLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491527411 174 LAHQHNTLKIARETAKaQNAAVVVVLHD--LNLASQYaDRLVLLHNGKLVCDDTPWNAL 230
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQ-KGKTIICTIHQpsSELFELF-DKIILMAEGRVAYLGSPDQAV 255
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-53 |
4.72e-07 |
|
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: 50.18 E-value: 4.72e-07
10 20 30
....*....|....*....|....*....|
gi 491527411 24 INIDIRAGEVTALLGPNGAGKSTLLKLLCG 53
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTG 380
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-218 |
4.93e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 16 GNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-----GEISSNHHITYFGKQkhDWEPEKSAKHIAMLPQHS-TL 89
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervttGVITGGDRLVNGRPL--DSSFQRSIGYVQQQDLHLpTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 TfpflAREVVELGAIpLSLSNKETTKLALHYMEQT-DVLHLaESLYPSLSG--GE------KQRLHLARVMTqlhqSGEK 160
Cdd:TIGR00956 852 T----VRESLRFSAY-LRQPKSVSKSEKMEYVEEViKLLEM-ESYADAVVGvpGEglnveqRKRLTIGVELV----AKPK 921
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 161 RILMLDEPTSALDLAHQHNTLKIARETAKAqNAAVVVVLH--DLNLASQYaDRLVLLHNG 218
Cdd:TIGR00956 922 LLLFLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHqpSAILFEEF-DRLLLLQKG 979
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
135-222 |
5.80e-07 |
|
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: 49.18 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 135 PSLSGGEKQRLHLArvmTQLHQSGEKRILMLDEPTSALdlaHQHNTLKIaRETAKAQNAA---VVVVLHDLNLASQyADR 211
Cdd:cd03270 136 PTLSGGEAQRIRLA---TQIGSGLTGVLYVLDEPSIGL---HPRDNDRL-IETLKRLRDLgntVLVVEHDEDTIRA-ADH 207
|
90
....*....|....*..
gi 491527411 212 LVLL------HNGKLVC 222
Cdd:cd03270 208 VIDIgpgagvHGGEIVA 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-233 |
1.24e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.20 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLC-------GEIS-SNHHITYFGKQkhdwepeKSAKHIAMLPQHstltf 91
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFrivelekGRIMiDDCDVAKFGLT-------DLRRVLSIIPQS----- 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 92 PFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVLH-----LAESLY---PSLSGGEKQRLHLARVMtqLHQSgekRIL 163
Cdd:PLN03232 1319 PVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDrnpfgLDAEVSeggENFSVGQRQLLSLARAL--LRRS---KIL 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 164 MLDEPTSALDLAHQHNTLKIARETAKAqnAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTPWNALTSE 233
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-221 |
1.47e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 48.57 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 1 MNQIVLSGKNISMTY---------GNRVV--LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQ 67
Cdd:COG4608 3 MAEPLLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRleEPTSGE-ILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 68 KHDWEPEKSA---KHIAML---PQHS---------TLTFPFLAREVvelgaiplsLSNKETTKLALHYMEQT--DVLHLA 130
Cdd:COG4608 82 ITGLSGRELRplrRRMQMVfqdPYASlnprmtvgdIIAEPLRIHGL---------ASKAERRERVAELLELVglRPEHAD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 131 EslYP-SLSGGEKQRLHLARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNLASQYA 209
Cdd:COG4608 153 R--YPhEFSGGQRQRIGIARAL-----ALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHIS 225
|
250
....*....|..
gi 491527411 210 DRLVLLHNGKLV 221
Cdd:COG4608 226 DRVAVMYLGKIV 237
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-213 |
1.73e-06 |
|
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: 46.97 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 18 RVVLDDINIDIRAGEVTALLGPNGAGKSTLLK---LLCGEISSNHHITYFGKQKHdWEPEKSAKHIAMLPQhstltfpfl 94
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAGC-IVAAVSAELIFTRLQ--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 95 arevvelgaiplslsnkettklalhymeqtdvlhlaeslypsLSGGEKQRLHLARVMtQLHQSGEKRILMLDEPTSALDL 174
Cdd:cd03227 78 ------------------------------------------LSGGEKELSALALIL-ALASLKPRPLYILDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|....*....
gi 491527411 175 AHQHNTLKIARETAKaQNAAVVVVLHDLNLAsQYADRLV 213
Cdd:cd03227 115 RDGQALAEAILEHLV-KGAQVIVITHLPELA-ELADKLI 151
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-174 |
2.10e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 4 IVLSGKNISMtyGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEPEKSakhiam 82
Cdd:PRK10636 2 IVFSSLQIRR--GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGgSYTFPGNWQLAWVNQET------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 83 lpqhSTLTFPFLA------REVVELGAiPLSLSNKETTKLAL-HYMEQTDVLHL------AESLYPSL------------ 137
Cdd:PRK10636 74 ----PALPQPALEyvidgdREYRQLEA-QLHDANERNDGHAIaTIHGKLDAIDAwtirsrAASLLHGLgfsneqlerpvs 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 491527411 138 --SGGEKQRLHLARVMTqlhqsGEKRILMLDEPTSALDL 174
Cdd:PRK10636 149 dfSGGWRMRLNLAQALI-----CRSDLLLLDEPTNHLDL 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-217 |
6.43e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRV---VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHHITYFGKQKHDWEPEK-------- 75
Cdd:PTZ00265 1169 MDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfyDLKNDHHIVFKNEHTNDMTNEQdyqgdeeq 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 76 ----------SAKHIAMLPQHSTL------------------------TFPFLAREvvelgAIPLSLSNKETTKLALHYM 121
Cdd:PTZ00265 1249 nvgmknvnefSLTKEGGSGEDSTVfknsgkilldgvdicdynlkdlrnLFSIVSQE-----PMLFNMSIYENIKFGKEDA 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 122 EQTDVLHLA---------ESL----------Y-PSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTL 181
Cdd:PTZ00265 1324 TREDVKRACkfaaidefiESLpnkydtnvgpYgKSLSGGQKQRIAIARALLR-----EPKILLLDEATSSLDSNSEKLIE 1398
|
250 260 270
....*....|....*....|....*....|....*..
gi 491527411 182 KIARETAKAQNAAVVVVLHdlNLAS-QYADRLVLLHN 217
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITIAH--RIASiKRSDKIVVFNN 1433
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
9-234 |
8.03e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRV--VLDDINIDIRAGEVTALLGPNGAGKSTLLKLL-------CGEIS-SNHHITYFGKQkhDWEpeksaK 78
Cdd:PLN03130 1241 EDVVLRYRPELppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALfriveleRGRILiDGCDISKFGLM--DLR-----K 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 79 HIAMLPQHstltfPFLAREVVELGAIPLSLSNKETTKLALHYMEQTDVL---------HLAESlYPSLSGGEKQRLHLAR 149
Cdd:PLN03130 1314 VLGIIPQA-----PVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIrrnslgldaEVSEA-GENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 150 VMtqLHQSgekRILMLDEPTSALDLAHQHNTLKIARETAKAqnAAVVVVLHDLNLASQyADRLVLLHNGKLVCDDTPWNA 229
Cdd:PLN03130 1388 AL--LRRS---KILVLDEATAAVDVRTDALIQKTIREEFKS--CTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
....*
gi 491527411 230 LTSER 234
Cdd:PLN03130 1460 LSNEG 1464
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-174 |
1.36e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNH-HITYFGKQKHDWEpekSAKHIAMLPQHSTLTFPFLAREV 98
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESgQIQIDGKTATRGD---RSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491527411 99 VELGAIPLSLSNKETTKLALHYMEQTDvlhLAESLYPSLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDL 174
Cdd:PRK13543 103 LHFLCGLHGRRAKQMPGSALAIVGLAG---YEDTLVRQLSAGQKKRLALARLWLS-----PAPLWLLDEPYANLDL 170
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
137-217 |
1.45e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 LSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLHDLNlASQYADRLVLLH 216
Cdd:PTZ00265 580 LSGGQKQRISIARAIIR-----NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLS 653
|
.
gi 491527411 217 N 217
Cdd:PTZ00265 654 N 654
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
14-172 |
1.59e-05 |
|
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: 45.90 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 14 TYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLcGEISSnhhiTYFGKQKhdwEPEKSAkhIAMLPQHSTLTFPF 93
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWP----VYGGRLT---KPAKGK--LFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 94 LAREVVelgaIPLS--------LSNKETTK----LALHYMEQTDV-LHLAESLYPSLSGGEKQRLHLARVMtqLHQSgek 160
Cdd:TIGR00954 531 LRDQII----YPDSsedmkrrgLSDKDLEQildnVQLTHILEREGgWSAVQDWMDVLSGGEKQRIAMARLF--YHKP--- 601
|
170
....*....|..
gi 491527411 161 RILMLDEPTSAL 172
Cdd:TIGR00954 602 QFAILDECTSAV 613
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-193 |
2.68e-05 |
|
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: 43.13 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 31 GEVTALLGPNGAGKSTLLKLLCGEISSNHHItyfgkqkhdwepeksakhiamlpqhstltfpflareVVELGAIPLslsn 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGG------------------------------------VIYIDGEDI---- 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 111 kettklaLHYMEQTDVLHLAESLYPSLSGGEKQRLHLARVmtqlhQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKA 190
Cdd:smart00382 42 -------LEEVLDQLLLIIVGGKKASGSGELRLRLALALA-----RKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
...
gi 491527411 191 QNA 193
Cdd:smart00382 110 LLK 112
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-220 |
2.84e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSNHhityfGKQKHDWEpeksakhIAMLPQHSTLTFPFLAREVVE 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV-----GKVDRNGE-------VSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 101 LGAIPLSLSNKETTKLALHYMEQTDvlhLAESLYPSL---SGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQ 177
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSE---LGEFIYQPVkkySSGMRAKLGFSINITV-----NPDILVIDEALSVGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491527411 178 HNTLKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:PRK13546 180 QKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-221 |
5.88e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 5.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGEISSN----HHITYFGKQKHDWEPEKSAK-------HIAMLPQHST 88
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvsGEITYNGYRLNEFVPRKTSAyisqndvHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 89 LTFPF--------------LAREVVELGAIP-----------------LSLSNKETTK-LALHYMEQTDVlhlAESLYPS 136
Cdd:PLN03140 260 LDFSArcqgvgtrydllseLARREKDAGIFPeaevdlfmkatamegvkSSLITDYTLKiLGLDICKDTIV---GDEMIRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 LSGGEKQRLHLARVMTqlhqsGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNAAVVVVLhdLNLASQ---YADRLV 213
Cdd:PLN03140 337 ISGGQKKRVTTGEMIV-----GPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSL--LQPAPEtfdLFDDII 409
|
....*...
gi 491527411 214 LLHNGKLV 221
Cdd:PLN03140 410 LLSEGQIV 417
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-220 |
1.06e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNisMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG--EISSNHhITYFGKQKHDWEPEKSAKH- 79
Cdd:PRK10982 248 EVILEVRN--LTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGirEKSAGT-ITLHGKKINNHNANEAINHg 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 80 IAMLPQH--STLTFPFLAREVVEL--------GAIPLsLSN---KETTKLALHYMEQTDVLHlaESLYPSLSGGEKQRLH 146
Cdd:PRK10982 325 FALVTEErrSTGIYAYLDIGFNSLisnirnykNKVGL-LDNsrmKSDTQWVIDSMRVKTPGH--RTQIGSLSGGNQQKVI 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491527411 147 LAR-VMTQlhqsgeKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:PRK10982 402 IGRwLLTQ------PEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
125-226 |
1.43e-04 |
|
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: 42.22 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 125 DVLHLAESLyPSLSGGEKQRLHLARVMtqLHQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNaAVVVVLHDLNL 204
Cdd:cd03271 159 GYIKLGQPA-TTLSGGEAQRIKLAKEL--SKRSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDV 234
|
90 100
....*....|....*....|....*...
gi 491527411 205 ASQyADRLVLL------HNGKLVCDDTP 226
Cdd:cd03271 235 IKC-ADWIIDLgpeggdGGGQVVASGTP 261
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
135-226 |
1.49e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 135 PSLSGGEKQRLHLARVMTQlhQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKAQNaAVVVVLHDLNLASQyADRLVL 214
Cdd:TIGR00630 828 TTLSGGEAQRIKLAKELSK--RSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKT-ADYIID 903
|
90
....*....|....*...
gi 491527411 215 L------HNGKLVCDDTP 226
Cdd:TIGR00630 904 LgpeggdGGGTVVASGTP 921
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-54 |
1.52e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 1.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 491527411 5 VLSGKNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE 54
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGD 50
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-220 |
2.37e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 21 LDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGeissnhhITYFGKQKHDWepEKSAKHIAMlpqHSTLTFPFLAREVVE 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAG-------VTMPNKGTVDI--KGSAALIAI---SSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 101 LGAIPLSLSNKETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLArvmtqLHQSGEKRILMLDEPTSALDLAHQHNT 180
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFA-----ISVHINPDILVIDEALSVGDQTFTKKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491527411 181 LKIARETaKAQNAAVVVVLHDLNLASQYADRLVLLHNGKL 220
Cdd:PRK13545 183 LDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-53 |
3.59e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.50 E-value: 3.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 491527411 6 LSGKNISMTYGNR-VVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG 53
Cdd:PRK10522 323 LELRNVTFAYQDNgFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTG 371
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
20-173 |
4.24e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 20 VLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE-----ISSNHHITYFGKQKHDWEP-----EKSAKHIAMLPQHSTL 89
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRktggyIEGDIRISGFPKKQETFARisgycEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 90 TFPFLARevvelgaIPLSLSNKETTKLALHYMEQTDVLHLAESLY-----PSLSGGEKQRLHLARVMTqlhqsGEKRILM 164
Cdd:PLN03140 975 IYSAFLR-------LPKEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELV-----ANPSIIF 1042
|
....*....
gi 491527411 165 LDEPTSALD 173
Cdd:PLN03140 1043 MDEPTSGLD 1051
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-221 |
4.82e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.15 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 25 NIDIRAGEVTALLGPNGAGKSTLLKLLCGEI--------SSNHHITY--FGKQKHDWEPEKSAKHIAMLPQHSTlTFPFL 94
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELpllsgerqSQFSHITRlsFEQLQKLVSDEWQRNNTDMLSPGED-DTGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 95 AREVVELGAiplslsnkETTKLALHYMEQTDVLHLAESLYPSLSGGEKQRLHLAR-VMTQlhqsgeKRILMLDEPTSALD 173
Cdd:PRK10938 102 TAEIIQDEV--------KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQaLMSE------PDLLILDEPFDGLD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491527411 174 LAHQHNTLKIArETAKAQNAAVVVVLHDLNLASQYADRLVLLHNGKLV 221
Cdd:PRK10938 168 VASRQQLAELL-ASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLA 214
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-226 |
6.14e-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: 40.77 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 136 SLSGGEKQRLHLArvmTQLhQSGEKRIL-MLDEPTSALdlaHQH------NTLKIAREtakaQNAAVVVVLHDLNLASQy 208
Cdd:TIGR00630 488 TLSGGEAQRIRLA---TQI-GSGLTGVLyVLDEPSIGL---HQRdnrrliNTLKRLRD----LGNTLIVVEHDEDTIRA- 555
|
90 100
....*....|....*....|....
gi 491527411 209 ADRLVLL------HNGKLVCDDTP 226
Cdd:TIGR00630 556 ADYVIDIgpgageHGGEVVASGTP 579
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-51 |
6.49e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 6.49e-04
10 20 30
....*....|....*....|....*....|..
gi 491527411 21 LDDINIDIRAGE-VTALLGPNGAGKSTLLKLL 51
Cdd:COG3950 14 FEDLEIDFDNPPrLTVLVGENGSGKTTLLEAI 45
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
21-52 |
8.31e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 8.31e-04
10 20 30
....*....|....*....|....*....|..
gi 491527411 21 LDDINIDIRAGeVTALLGPNGAGKSTLLKLLC 52
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAIK 39
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-226 |
8.40e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 135 PSLSGGEKQRLHLArvmTQLhQSGekriLM-----LDEPTSALdlaHQH------NTLKIARE---TakaqnaaVVVVLH 200
Cdd:COG0178 484 GTLSGGEAQRIRLA---TQI-GSG----LVgvlyvLDEPSIGL---HQRdndrliETLKRLRDlgnT-------VIVVEH 545
|
90 100 110
....*....|....*....|....*....|....
gi 491527411 201 DLN--LAsqyADRLVLL------HNGKLVCDDTP 226
Cdd:COG0178 546 DEDtiRA---ADYIIDIgpgageHGGEVVAQGTP 576
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
30-54 |
8.54e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 39.30 E-value: 8.54e-04
10 20
....*....|....*....|....*
gi 491527411 30 AGEVTALLGPNGAGKSTLLKLLCGE 54
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPE 108
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
30-69 |
8.80e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.06 E-value: 8.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491527411 30 AGEVTALLGPNGAGKSTLLKLLC-------GEISSNHhityfGKQKH 69
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLpeldlrtGEISEKL-----GRGRH 146
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-219 |
1.87e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 137 LSGGEKQRLHLA-RVMTQLHQSGEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQyADRL--V 213
Cdd:PRK03918 789 LSGGERIALGLAfRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLR-KIPQVIIVSHDEELKDA-ADYVirV 866
|
....*.
gi 491527411 214 LLHNGK 219
Cdd:PRK03918 867 SLEGGV 872
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
25-51 |
1.94e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.14 E-value: 1.94e-03
10 20
....*....|....*....|....*..
gi 491527411 25 NIDIRAGEVTALLGPNGAGKSTLLKLL 51
Cdd:COG4637 15 DLELPLGPLTVLIGANGSGKSNLLDAL 41
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-48 |
2.04e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 2.04e-03
10 20
....*....|....*....|....*..
gi 491527411 22 DDINIDIRAGEVTALLGPNGAGKSTLL 48
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-235 |
2.14e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.00 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 3 QIVLSGKNISMTYGNRVvlDDINIDIRAGEVTALLGPNGAGKSTLLKLLCG-EISSNHHITYFGKQKHDWEPEKSAKH-I 80
Cdd:PRK09700 263 ETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGvDKRAGGEIRLNGKDISPRSPLDAVKKgM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 81 AMLPQHSTLTFPFLAREVVELGAIPLSLSN---KETTKLALHYME------QTDVL----HLAESLYPSLSGGEKQRLHL 147
Cdd:PRK09700 341 AYITESRRDNGFFPNFSIAQNMAISRSLKDggyKGAMGLFHEVDEqrtaenQRELLalkcHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 148 ARVMtqlhqSGEKRILMLDEPTSALDLAHQHNTLKIARETAKaQNAAVVVVLHDLNLASQYADRLVLLHNGKLVCDDTPW 227
Cdd:PRK09700 421 SKWL-----CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNR 494
|
....*...
gi 491527411 228 NALTSERI 235
Cdd:PRK09700 495 DDMSEEEI 502
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
135-172 |
2.75e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.85 E-value: 2.75e-03
10 20 30
....*....|....*....|....*....|....*....
gi 491527411 135 PSLSGGEKQRLHLARvmtQLHQSGEKRIL-MLDEPTSAL 172
Cdd:COG0178 825 TTLSGGEAQRVKLAS---ELSKRSTGKTLyILDEPTTGL 860
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
30-69 |
3.01e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 38.26 E-value: 3.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491527411 30 AGEVTALLGPNGAGKSTLLKLL-------CGEISSNHhityfGKQKH 69
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLLNALapdlelkTGEISEAL-----GRGKH 204
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-51 |
3.49e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.14 E-value: 3.49e-03
|
| COG1373 |
COG1373 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
13-64 |
4.99e-03 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440984 [Multi-domain] Cd Length: 405 Bit Score: 37.62 E-value: 4.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 491527411 13 MTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLcgeISSNHHITYF 64
Cdd:COG1373 2 MIMIKRKILDKLLKLLDNRKAVVITGPRQVGKTTLLKQL---AKELENILYI 50
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-204 |
5.64e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 125 DVLHLAESLYpSLSGGEKQRLHLARVMtqLHQSGEKRILMLDEPTSALdlaHQHN--TLKIARETAKAQNAAVVVVLHDL 202
Cdd:PRK00635 799 DYLPLGRPLS-SLSGGEIQRLKLAYEL--LAPSKKPTLYVLDEPTTGL---HTHDikALIYVLQSLTHQGHTVVIIEHNM 872
|
..
gi 491527411 203 NL 204
Cdd:PRK00635 873 HV 874
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
26-48 |
6.00e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.91 E-value: 6.00e-03
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-238 |
6.22e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 9 KNISMTYGNRVVLDDINIDIRAGEVTALLGPNGAGKSTLLKLLCGE----ISSNHHITYFGKQ-------------KHDW 71
Cdd:PLN03073 181 ENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHaidgIPKNCQILHVEQEvvgddttalqcvlNTDI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 72 EPEK-SAKHIAMLPQHSTLTFPflarEVVELGAIPLSLSNKE---TTKLALHY--MEQTDVlHLAESLYPSL-------- 137
Cdd:PLN03073 261 ERTQlLEEEAQLVAQQRELEFE----TETGKGKGANKDGVDKdavSQRLEEIYkrLELIDA-YTAEARAASIlaglsftp 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 138 ----------SGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLahqHNTLKIARETAKAQNaAVVVVLHDLNLASQ 207
Cdd:PLN03073 336 emqvkatktfSGGWRMRIALARALFI-----EPDLLLLDEPTNHLDL---HAVLWLETYLLKWPK-TFIVVSHAREFLNT 406
|
250 260 270
....*....|....*....|....*....|.
gi 491527411 208 YADRLVLLHNGKLVCDDTPWNALTSERIEQV 238
Cdd:PLN03073 407 VVTDILHLHGQKLVTYKGDYDTFERTREEQL 437
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-51 |
6.86e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 37.29 E-value: 6.86e-03
10 20 30
....*....|....*....|....*....|.
gi 491527411 21 LDDINIDIRAGeVTALLGPNGAGKSTLLKLL 51
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEAL 43
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
136-233 |
8.07e-03 |
|
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: 36.81 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491527411 136 SLSGGEKQRLHLARVMTQlhqsgEKRILMLDEPTSALDLAHQhNTLKIARETAKAqNAAVVVVLHDLNLASQyADRLVLL 215
Cdd:cd03288 156 NFSVGQRQLFCLARAFVR-----KSSILIMDEATASIDMATE-NILQKVVMTAFA-DRTVVTIAHRVSTILD-ADLVLVL 227
|
90
....*....|....*...
gi 491527411 216 HNGKLVCDDTPWNALTSE 233
Cdd:cd03288 228 SRGILVECDTPENLLAQE 245
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
31-54 |
9.22e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 36.84 E-value: 9.22e-03
10 20
....*....|....*....|....
gi 491527411 31 GEVTALLGPNGAGKSTLLKLLCGE 54
Cdd:PRK01889 195 GKTVALLGSSGVGKSTLVNALLGE 218
|
|
| |
