|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-250 |
8.26e-155 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 430.27 E-value: 8.26e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILK 80
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGRFPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDMEVEI 240
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVEE 241
|
250
....*....|
gi 1821109780 241 IKGKKYCLYH 250
Cdd:COG4604 242 IDGKRICVYF 251
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-248 |
3.53e-107 |
|
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: 310.05 E-value: 3.53e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILK 80
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDMEV 238
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|..
gi 1821109780 239 EI--IKGKKYCL 248
Cdd:COG1120 242 IEdpVTGRPLVL 253
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-248 |
6.72e-77 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 232.98 E-value: 6.72e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILK 80
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:PRK11231 83 QHHLTPEGITVRELVAYGRSPWLSlwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDMEV 238
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEI 241
|
250
....*....|..
gi 1821109780 239 --EIIKGKKYCL 248
Cdd:PRK11231 242 hpEPVSGTPMCV 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-217 |
9.30e-74 |
|
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: 222.31 E-value: 9.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 qntyqvkmtvrellsfgrfpyskgrlttedyevidkVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-238 |
5.28e-71 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 218.10 E-value: 5.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQ 82
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRELLSFGRFPYSKGRltTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQ------DTDYI 156
Cdd:PRK13548 85 SSLSFPFTVEEVVAMGRAPHGLSR--AEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDM 236
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYGADV 242
|
..
gi 1821109780 237 EV 238
Cdd:PRK13548 243 LV 244
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-238 |
9.99e-71 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 217.29 E-value: 9.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILK 80
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGRFPYskGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQ---DTD--- 154
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH--GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwePVDggp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 155 -YILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFD 233
Cdd:COG4559 160 rWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYG 238
|
....*
gi 1821109780 234 VDMEV 238
Cdd:COG4559 239 ADLRV 243
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-238 |
1.15e-67 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 209.17 E-value: 1.15e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtdelaKEIAILKQ 81
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-----RRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTY--QVKMTVRELLSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:COG1121 83 RAEVdwDFPITVRDVVLMGRYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHsGTVDEVICSEHLKEVFDVDME 237
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENLSRAYGGPVA 240
|
.
gi 1821109780 238 V 238
Cdd:COG1121 241 L 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
12-223 |
1.28e-59 |
|
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: 187.92 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMT 90
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDDQlFAPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:COG1122 93 VEEDVAFG--PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 171 IVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-232 |
1.42e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 188.35 E-value: 1.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAILKQQ 82
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRELLSF-GRFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:COG1131 82 PALYPDLTVRENLRFfARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVIcSEHLKEVF 232
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK-ARLLEDVF 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-212 |
1.15e-56 |
|
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: 179.97 E-value: 1.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMT 90
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDDQfFGPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:cd03225 93 VEEEVAFG--LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1821109780 171 IVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:cd03225 171 RELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-236 |
5.81e-56 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 179.98 E-value: 5.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKMTVREL 94
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPY--SKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIV 172
Cdd:PRK10575 106 VAIGRYPWhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 173 VMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDM 236
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPM 249
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-233 |
1.31e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 178.33 E-value: 1.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNIC-ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK---EIA 77
Cdd:COG3638 4 ELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 78 ILKQQntYQV--KMTVRE-LLSfGRFPYSK------GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMI 148
Cdd:COG3638 84 MIFQQ--FNLvpRLSVLTnVLA-GRLGRTStwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 149 LVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEViCSEHL 228
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVL 239
|
....*
gi 1821109780 229 KEVFD 233
Cdd:COG3638 240 REIYG 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-215 |
1.50e-55 |
|
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: 177.34 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtdelaKEIAILKQQNTYQVKM--TVR 92
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQRRSIDRDFpiSVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:cd03235 89 DVVLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821109780 171 IVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICH 215
Cdd:cd03235 169 EDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-245 |
4.48e-55 |
|
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: 176.97 E-value: 4.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAILKQ 81
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTYQVKMTVRE-LLSFGRFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:COG4555 82 ERGLYDRLTVREnIRYFAEL---YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV---ICSEHLKEVFdvdme 237
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELreeIGEENLEDAF----- 232
|
....*...
gi 1821109780 238 VEIIKGKK 245
Cdd:COG4555 233 VALIGSEE 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-232 |
4.40e-54 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 175.17 E-value: 4.40e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKMTVREL 94
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIV 172
Cdd:PRK10253 102 VARGRYPHQPlfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 173 VMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVF 232
Cdd:PRK10253 182 LLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-213 |
4.54e-52 |
|
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: 168.44 E-value: 4.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCK----NICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA---- 73
Cdd:cd03255 2 ELKNLSKtyggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 74 KEIAILKQQNTYQVKMTVRELLSFGRFPysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDT 153
Cdd:cd03255 82 RHIGFVFQSFNLLPDLTALENVELPLLL--AGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 154 DYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFaAAYSDNIIAMKDGKI 213
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-222 |
7.20e-52 |
|
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: 168.52 E-value: 7.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICE-TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA---KEIA 77
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 78 ILKQQNTYQVKMTVRELLSFGRFPYSK------GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQ 151
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRRStwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 152 DTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-227 |
1.35e-50 |
|
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: 165.37 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDEL---AKEIAIL 79
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQNTYQVKMTVRELLSFgrFPYSKGRLTTEdyEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:cd03261 83 FQSGALFDSLTVFENVAF--PLREHTRLSEE--EIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEH 227
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-222 |
1.42e-50 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 165.55 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNI-CETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK---EI 76
Cdd:TIGR02315 2 LEVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKlrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 77 AILKQQNTYQVKMTVRELLSFGRFPYSK------GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILV 150
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 151 QDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-223 |
8.03e-49 |
|
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: 167.77 E-value: 8.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTD---ELAKEIAILkQQNTYQV---K 88
Cdd:COG1123 280 AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMV-FQDPYSSlnpR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFGrfPYSKGRLTTEdyEVIDKVLGYLDL----ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:COG1123 359 MTVGDIIAEP--LRLHGLLSRA--ERRERVAELLERvglpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSA 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 165 LDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1123 435 LDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-213 |
1.10e-48 |
|
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: 159.61 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILK 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:cd03259 79 QDYALFPHLTVAENIAFG--LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-227 |
2.31e-47 |
|
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: 157.06 E-value: 2.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA---KEIAI 78
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 79 LKQQN---TYqvkMTVRE-----LLSFGRFPYSkgrlttedyEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRAALAM 147
Cdd:COG1127 87 LFQGGalfDS---LTVFEnvafpLREHTDLSEA---------EIRELVLEKLElvgLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 148 ILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEH 227
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-213 |
3.29e-47 |
|
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: 154.48 E-value: 3.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAILKQ 81
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTYQVKMTVRELLsfgrfpyskgrlttedyevidkvlgyldlesygdryldTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03230 81 EPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
7-213 |
2.40e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.05 E-value: 2.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 7 CKNIC--------ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK---- 74
Cdd:COG1136 7 LRNLTksygtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlrrr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 75 EIAILKQQntYQV--KMTVRE---L-LSFGRFPYSkgrlttEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMI 148
Cdd:COG1136 87 HIGFVFQF--FNLlpELTALEnvaLpLLLAGVSRK------ERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 149 LVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDiNFAAAYSDNIIAMKDGKI 213
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
3-238 |
3.81e-46 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 158.47 E-value: 3.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQ 82
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRELLSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:PRK09536 86 TSLSFEFDVRQVVEMGRTPHRSrfDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDMEV 238
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAV 242
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-212 |
2.21e-45 |
|
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: 150.03 E-value: 2.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE--IAI 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 79 LKQQNTYQVKMTVRELLSFGrfpyskgrlttedyevidkvlgyldlesygdryldtLSGGQLQRAALAMILVQDTDYILL 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
15-213 |
1.16e-44 |
|
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: 149.58 E-value: 1.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA---KEIAILKQQ-----NTYq 86
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKirrKEIQMVFQDpmsslNPR- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 87 vkMTVRELLSFGRFPYSKGRLTTEDYEVIDKVL-GYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:cd03257 99 --MTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 166 DMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03257 177 DVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-222 |
1.49e-43 |
|
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: 147.20 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAilk 80
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIG--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 qqNTYQV-----KMTVRE-----LLSFGRFPYSKGRLTTEDYEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRAALAM 147
Cdd:cd03219 79 --RTFQIprlfpELTVLEnvmvaAQARTGSGLLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 148 ILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-213 |
1.62e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.11 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQ 81
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV-P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTYQVKMTVRELLsfgRFPYSKgRLTTEDYEVIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:COG4619 81 QEPALWGGTVRDNL---PFPFQL-RERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-223 |
3.31e-43 |
|
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: 152.75 E-value: 3.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKD---SGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMT 90
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVFQDPMTQlNPVT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:COG1123 101 VGDQIAEA--LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQ 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 171 IVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1123 179 AEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-212 |
3.84e-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: 143.54 E-value: 3.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 qntyqvkmtvrellsfgrfpyskgrlttedyevidkvlgyldlesygdryldtLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
19-221 |
4.32e-43 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 145.67 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 19 INLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILKQQNTYQVKMTVRELLSFG 98
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 99 RFPysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD--MKQSIvvMQT 176
Cdd:COG3840 96 LRP--GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpaLRQEM--LDL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821109780 177 IRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-239 |
4.88e-43 |
|
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: 146.38 E-value: 4.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSG-HVLIKGKEITKWRTDELAKEIAIL--KQQNTYQVK 88
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVspALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELL------SFGRFPyskgRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:COG1119 95 ETVLDVVlsgffdSIGLYR----EPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 163 NNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDMEVE 239
Cdd:COG1119 171 AGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGLPVEVE 247
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-194 |
2.08e-42 |
|
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: 143.39 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAILK 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFgrfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:COG4133 82 HADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1821109780 161 PLNNLDmKQSI-VVMQTIRNMADElGKTILVVLHD 194
Cdd:COG4133 158 PFTALD-AAGVaLLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
16-222 |
7.97e-42 |
|
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: 143.26 E-value: 7.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAilkqqNTYQV-----KM 89
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIA-----RTFQNprlfpEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRE--------------LLSFGRFPYSKGRLtTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDY 155
Cdd:COG0411 95 TVLEnvlvaaharlgrglLAALLRLPRARREE-REARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 156 ILLDEP---LNNLDMKQsivVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG0411 174 LLLDEPaagLNPEETEE---LAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
16-235 |
1.03e-41 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 142.67 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKdSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKMTVRELL 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGrfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQ-------DTDYILLDEPLNNLDMK 168
Cdd:COG4138 91 ALH---QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 169 QSIVVMQTIRNMAdELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVD 235
Cdd:COG4138 168 QQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVK 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-222 |
1.49e-41 |
|
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: 142.25 E-value: 1.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCK----NICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIA 77
Cdd:COG1124 3 EVRNLSVsygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 78 ILKQQNTYQV--KMTVRELLS----FGRFPYSKGRlttedyevIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMILV 150
Cdd:COG1124 83 MVFQDPYASLhpRHTVDRILAeplrIHGLPDREER--------IAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 151 QDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
12-222 |
1.65e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.98 E-value: 1.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEIT---KWRTDELAKEIAILKQQNTYQV- 87
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkKKKLKDLRKKVGLVFQFPEHQLf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLSFG--RFPYSKGRLTTEDYEVIDKVlGyLDlESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:TIGR04521 97 EETVYKDIAFGpkNLGLSEEEAEERVKEALELV-G-LD-EEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 166 DMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-227 |
8.07e-41 |
|
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: 140.51 E-value: 8.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKMTVREll 95
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHMTVEE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRFP----YSKGRLTTEDYEVIdKVLGyLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSI 171
Cdd:cd03295 95 NIALVPkllkWPKEKIRERADELL-ALVG-LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 172 VVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEH 227
Cdd:cd03295 173 QLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPA 228
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-206 |
1.52e-40 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 138.14 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGkeitkwrtdelAKEIAILKQQNTY--QVKMTVRE 93
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdSLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSFGRFPY--SKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSI 171
Cdd:NF040873 77 LVAMGRWARrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1821109780 172 VVMQTIRNMADElGKTILVVLHDINFAAAYSDNII 206
Cdd:NF040873 157 RIIALLAEEHAR-GATVVVVTHDLELVRRADPCVL 190
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-223 |
2.04e-40 |
|
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: 139.01 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETcILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILK 80
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGL--KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-232 |
1.48e-39 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 138.04 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKD--------SGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 87 VKMTVRELLSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQ---------DTDY 155
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 156 ILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVF 232
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-221 |
1.85e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 143.36 E-value: 1.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKqQNTYQVKMTVREL 94
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVP-QNPYLFAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLttedYEVIDKVlGYLDLESYGDRYLDT--------LSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:COG4988 431 LRLGRPDASDEEL----EAALEAA-GLDEFVAALPDGLDTplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 167 MKQSIVVMQTIRNMADelGKTILVVLHDINFAAAYsDNIIAMKDGKICHSGTVDE 221
Cdd:COG4988 506 AETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEE 557
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-223 |
2.06e-39 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 143.37 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVV-PQRPHLFDTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfpyskGRLTTED-YEVIDKV-LGYLdLESYGDRyLDT--------LSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:COG4987 429 LRLAR-----PDATDEElWAALERVgLGDW-LAALPDG-LDTwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 165 LDMKQSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG4987 502 LDAATEQALLADLLEALA--GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-213 |
2.58e-39 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 135.46 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWrtdELAKEIAILKQQNTYQVKM-TVRE 93
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQDVDYQLFTdSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSFGRfpyskgRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVV 173
Cdd:cd03226 92 ELLLGL------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1821109780 174 MQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03226 166 GELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-212 |
3.43e-39 |
|
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: 133.66 E-value: 3.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV-PQDPFLFSGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LsfgrfpyskgrlttedyevidkvlgyldlesygdryldtLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:cd03228 96 I---------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALIL 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1821109780 175 QTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGK 212
Cdd:cd03228 137 EALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-223 |
9.26e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 134.74 E-value: 9.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTD--ELAKEIAIL 79
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQ-NTYQvKMTVRELLSFGrfPYSKGRLTTEdyEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRA----ALAMilvq 151
Cdd:COG1126 83 FQQfNLFP-HLTVLENVTLA--PIKVKKMSKA--EAEERAMELLErvgLADKADAYPAQLSGGQQQRVaiarALAM---- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 152 DTDYILLDEPLNNLD--MKQsiVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1126 154 EPKVMLFDEPTSALDpeLVG--EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-217 |
1.34e-38 |
|
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: 133.47 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGtVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAILKQ 81
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTYQVKMTVRELLSFgrFPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03264 80 EFGVYPNFTVREFLDY--IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 162 LNNLDMKQSIVVmqtiRNMADELGKTILVVL--HDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03264 158 TAGLDPEERIRF----RNLLSELGEDRIVILstHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-213 |
1.42e-38 |
|
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: 133.53 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILK 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGRfpyskgRLTTEDYEVIDK----VLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGL------KLRKVPKDEIDErvreVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
15-222 |
2.03e-38 |
|
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: 133.33 E-value: 2.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAILKQ-QNTYQvKMTVR 92
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEgRRIFP-ELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFGRFPYSKGRLTtedyEVIDKVLGYL-DLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPlnNLDMKQSI 171
Cdd:cd03224 94 ENLLLGAYARRRAKRK----ARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP--SEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 172 V--VMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:cd03224 168 VeeIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-163 |
2.62e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 130.85 E-value: 2.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKMTVRELL 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 96 SFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLD----TLSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
15-230 |
5.27e-38 |
|
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: 132.80 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAilkqqntyQV------ 87
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIG--------YVpegrri 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 --KMTVRELLSFGRFPyskGRLTTEDYEVIDKVLGYL-DLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPlnn 164
Cdd:COG0410 90 fpSLTVEENLLLGAYA---RRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEP--- 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 165 ldmkqS------IV--VMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKE 230
Cdd:COG0410 164 -----SlglaplIVeeIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVRE 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-222 |
1.02e-37 |
|
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: 131.92 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLL-----SKDSGHVLIKGKEITKWRTD--ELA 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 74 KEIAILKQQnTYQVKMTVRELLSFGrfPYSKGRLTTEDYEVID-KVLGYLDLESYGDRYLD--TLSGGQLQRAALAMILV 150
Cdd:cd03260 81 RRVGMVFQK-PNPFPGSIYDNVAYG--LRLHGIKLKEELDERVeEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 151 QDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELgkTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-236 |
4.81e-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: 129.90 E-value: 4.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCK----NICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrtdELAKEI 76
Cdd:cd03293 1 LEVRNVSKtyggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 77 AILKQQNTYQVKMTVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 157 LLDEPLNNLDmkqsivvMQTIRNMADEL-------GKTILVVLHDINFAAAYSDNIIAMKdgkiCHSGTVdevicsehlK 229
Cdd:cd03293 154 LLDEPFSALD-------ALTREQLQEELldiwretGKTVLLVTHDIDEAVFLADRVVVLS----ARPGRI---------V 213
|
....*..
gi 1821109780 230 EVFDVDM 236
Cdd:cd03293 214 AEVEVDL 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-213 |
1.93e-36 |
|
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: 128.03 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTD--ELAKEIAIL 79
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQNTYQVKMTVRELLSFGrfP-YSKGRlttEDYEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRAALAMILVQDTDY 155
Cdd:cd03262 82 FQQFNLFPHLTVLENITLA--PiKVKGM---SKAEAEERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 156 ILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-222 |
3.54e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.96 E-value: 3.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrtDELAKE--IAIL 79
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT----DLPPKDrnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQntYQV--KMTVRELLSFG----RFPysKgrlttedyEVIDK----VLGYLDLESYGDRYLDTLSGGQLQRAALAMIL 149
Cdd:COG3839 81 FQS--YALypHMTVYENIAFPlklrKVP--K--------AEIDRrvreAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 150 VQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
8-246 |
4.99e-36 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 128.13 E-value: 4.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 8 KNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKdSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQV 87
Cdd:PRK03695 4 NDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLSFGRfpySKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQ-------DTDYILLDE 160
Cdd:PRK03695 83 AMPVFQYLTLHQ---PDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMAdELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDMEVEI 240
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLD 238
|
....*.
gi 1821109780 241 IKGKKY 246
Cdd:PRK03695 239 VEGHPM 244
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-222 |
5.51e-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: 130.60 E-value: 5.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILKQQ 82
Cdd:COG3842 8 LENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 -----NtyqvkMTVRELLSFG-RFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:COG3842 86 yalfpH-----LTVAENVAFGlRM---RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 157 LLDEPLNNLDMK---QsivvMQT-IRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG3842 158 LLDEPLSALDAKlreE----MREeLRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-221 |
6.07e-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: 126.85 E-value: 6.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCK--NICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAI 78
Cdd:cd03263 1 LQIRNLTKtyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 79 LKQQNTYQVKMTVRELLSF-GRFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:cd03263 80 CPQFDALFDELTVREHLRFyARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMADelGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-235 |
2.21e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.74 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrtdELAKEIAILKQQNTyqvkMTV 91
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPDRGVVFQEPAllpwLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFG-RFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDmkqs 170
Cdd:COG1116 98 LDNVALGlEL---RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD---- 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 171 ivvMQTIRNMADEL-------GKTILVVLHDINFAAAYSDNIIAMKDGKichsGTVdevicsehlKEVFDVD 235
Cdd:COG1116 171 ---ALTRERLQDELlrlwqetGKTVLFVTHDVDEAVFLADRVVVLSARP----GRI---------VEEIDVD 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-222 |
4.01e-35 |
|
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: 125.53 E-value: 4.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILK 80
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGRFPYSKGRLTTEDyEVIDKV---LGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVKPRSERPPEA-EIRAKVhelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-221 |
5.60e-35 |
|
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: 124.40 E-value: 5.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAILKQQ 82
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRE-LLSFGRFPYSKGRLTTEDyevIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03265 82 LSVDDELTGWEnLYIHARLYGVPGAERRER---IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-222 |
7.24e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 127.57 E-value: 7.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEitkWRTDELAKE--IAILK 80
Cdd:COG1118 5 VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD---LFTNLPPRErrVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQntYQV--KMTVRELLSFG--RFPYSKGrlttedyEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRAALAMILVQDT 153
Cdd:COG1118 82 QH--YALfpHMTVAENIAFGlrVRPPSKA-------EIRARVEELLElvqLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 154 DYILLDEPLNNLDMKqsivVMQTIR----NMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG1118 153 EVLLLDEPFGALDAK----VRKELRrwlrRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-221 |
1.62e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 126.76 E-value: 1.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 5 NLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILKQQNT 84
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 85 YQVKMTVRELLSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK11432 89 LFPHMSLGENVGYGL--KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 165 LDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-230 |
1.12e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 5 NLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE--LAKEIAILKQQ 82
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRELLSFGrfPYSKGRLTTEDYEVIDK-VLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:PRK09493 86 FYLFPHLTALENVMFG--PLRVRGASKEEAEKQAReLLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI---CSEHLKE 230
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIknpPSQRLQE 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-213 |
1.54e-33 |
|
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: 120.40 E-value: 1.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwrTDELAKEIAILKQ 81
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTYQVKMTVRELLsfgrfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03268 80 APGFYPNLTARENL------RLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-232 |
3.35e-33 |
|
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: 120.34 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAILK 80
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRE--LLSFGRFPYSKGRLTTEdyevIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:cd03218 82 QEASIFRKLTVEEniLAVLEIRGLSKKEREEK----LEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADeLGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVF 232
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
4.26e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.49 E-value: 4.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICE-TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTD--ELAKEIA 77
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 78 ILKQQNTYQV-KMTVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:PRK13636 86 MVFQDPDNQLfSASVYQDVSFG--AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-225 |
8.20e-33 |
|
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: 120.44 E-value: 8.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDEL----AKEIAILKQQNTYQVKMTV 91
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDmkqsi 171
Cdd:cd03294 120 LENVAFGL--EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD----- 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 172 vvmQTIRN-MADEL-------GKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICS 225
Cdd:cd03294 193 ---PLIRReMQDELlrlqaelQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-223 |
1.03e-32 |
|
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: 125.72 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVV-LQDVFLFSGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLTT--EDYEVIDKV----LGYldlesygdrylDT--------LSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:COG2274 569 ITLGDPDATDEEIIEaaRLAGLHDFIealpMGY-----------DTvvgeggsnLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG2274 638 ATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-217 |
2.91e-32 |
|
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: 117.21 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwrTDELAKEIAILKQQNTYQVKMTVRELLSF 97
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVSMLFQENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 98 GRFPysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTI 177
Cdd:cd03298 94 GLSP--GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1821109780 178 RNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-222 |
4.15e-32 |
|
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: 117.34 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwrtdelakeIAILKQ 81
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN---------LPPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 Q-NT----YQV--KMTVRELLSFG-RFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDT 153
Cdd:cd03300 73 PvNTvfqnYALfpHLTVFENIAFGlRL---KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 154 DYILLDEPLNNLDMK--QSivvMQ-TIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:cd03300 150 KVLLLDEPLGALDLKlrKD---MQlELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-223 |
2.89e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.04 E-value: 2.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV-PQDTFLFSGTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSkgrltteDYEVID--KVLGYLD-LESYGDRYlDT--------LSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:COG1132 434 IRYGRPDAT-------DEEVEEaaKAAQAHEfIEALPDGY-DTvvgergvnLSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 164 NLDMKQSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1132 506 ALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELL 562
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-222 |
5.75e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.50 E-value: 5.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMTVREL 94
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPDNQfVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:PRK13635 103 VAFGL--ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 175 QTIRNMADELGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13635 181 ETVRQLKEQKGITVLSITHDLD-EAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-222 |
6.30e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.56 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTD--ELAKEIAILKQQNTYQV-KM 89
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIVFQNPDDQLfAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQ 169
Cdd:PRK13639 95 TVEEDVAFG--PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 170 SIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-213 |
7.56e-31 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 113.80 E-value: 7.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 20 NLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwRTDELAKEIAILKQQNTYQVKMTVRELLSFGR 99
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT--GLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 100 FPYSKgrLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRN 179
Cdd:TIGR01277 96 HPGLK--LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....
gi 1821109780 180 MADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-222 |
1.05e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 115.21 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwrtdelakeiailKQQNT----------Y 85
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------------EDRRRigylpeerglY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 86 QvKMTVRE-LLSFGRFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:COG4152 84 P-KMKVGEqLVYLARL---KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 165 LDmkqSI---VVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG4152 160 LD---PVnveLLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-217 |
1.94e-30 |
|
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: 112.37 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEItkwrTDELAKEIAILK 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRE-LLSFGRFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:cd03269 77 EERGLYPKMKVIDqLVYLAQL---KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 160 EPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
18-217 |
1.95e-30 |
|
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: 112.39 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGtVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGkeiTKWRTDELA-------KEIAILKQQNTYQVKMT 90
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRKKinlppqqRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGrfpySKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:cd03297 92 VRENLAFG----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1821109780 171 IVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-222 |
2.44e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 112.62 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAILK 80
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGrFPYSKGRLTtedyEVIDKVLGYLD-LESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:TIGR03410 82 QGREIFPRLTVEENLLTG-LAALPRRSR----KIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 160 EPLNNLdmKQSIV--VMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR03410 157 EPTEGI--QPSIIkdIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
16-228 |
9.69e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.59 E-value: 9.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQV-KMTVREL 94
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIfSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:PRK13652 100 IAFG--PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 175 QTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHL 228
Cdd:PRK13652 178 DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
16-217 |
1.07e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 110.92 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKeIAILKQQNTYQVKMTVRE-L 94
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTGLYDRLTAREnL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRlttEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:cd03266 100 EYFAGLYGLKGD---ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1821109780 175 QTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03266 177 EFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-217 |
1.87e-29 |
|
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: 110.44 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLST-MCRLLSKD--SGHVLIKGKEITKwrtDELAKEIAILKQQNTYQVKMTV 91
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAiSGRVEGGGttSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFgrfpYSKGRLTTE------DYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:cd03234 99 RETLTY----TAILRLPRKssdairKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 166 DMKQSIVVMQTIRNMADElGKTILVVLH----DInfaaaYS--DNIIAMKDGKICHSG 217
Cdd:cd03234 175 DSFTALNLVSTLSQLARR-NRIVILTIHqprsDL-----FRlfDRILLLSSGEIVYSG 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
2.39e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.95 E-value: 2.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCK-----NICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE 75
Cdd:COG1101 2 LELKNLSKtfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 76 IAilkqqntyQV----------KMTVRELLSF-----GRFPYSKGrLTTEDYEVID---KVLGyLDLEsygDRyLDT--- 134
Cdd:COG1101 82 IG--------RVfqdpmmgtapSMTIEENLALayrrgKRRGLRRG-LTKKRRELFRellATLG-LGLE---NR-LDTkvg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 135 -LSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:COG1101 148 lLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-213 |
3.03e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 109.76 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK---EIAILKQqnTYQV--KM 89
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGVVFQ--DFRLlpDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLSFGRfpyskgRLTTEDYEVIDK----VLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:COG2884 95 TVYENVALPL------RVTGKSRKEIRRrvreVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1821109780 166 DMKQSIVVMQTIR--NmadELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:COG2884 169 DPETSWEIMELLEeiN---RRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-222 |
3.71e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 110.21 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDelakEIAIL----KQQN-TYQVKMT 90
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEH----EIARLgigrKFQKpTVFEELT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRE--LLSFGR----FPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPlnn 164
Cdd:COG4674 102 VFEnlELALKGdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEP--- 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 165 ldmkqsivV--------MQT---IRNMADElgKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG4674 179 --------VagmtdaetERTaelLKSLAGK--HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
16-217 |
7.86e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.83 E-value: 7.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQV-KMTVREL 94
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPDDQVfSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:PRK13647 101 VAFG--PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1821109780 175 qTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK13647 179 -EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-233 |
8.44e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.72 E-value: 8.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDS---GHVLIKGKEITkwRTDELAKEI- 76
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQ--REGRLARDIr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 77 -------AILKQQNTYQvKMTVRE---LLSFGRFPYSKGRL---TTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRA 143
Cdd:PRK09984 83 ksrantgYIFQQFNLVN-RLSVLEnvlIGALGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 144 ALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGtvdevi 223
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG------ 235
|
250
....*....|.
gi 1821109780 224 CSEHL-KEVFD 233
Cdd:PRK09984 236 SSQQFdNERFD 246
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-222 |
1.30e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEIT--KWRTDELAKEIAILKQQNTYQV-K 88
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPEYQLfE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFGrfpysKGRLTTEDYEVIDKV-----LGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK13637 99 ETIEKDIAFG-----PINLGLSEEEIENRVkramnIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 164 NLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-223 |
1.96e-28 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 109.41 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEI--AIlkQQ-----Nty 85
Cdd:COG1125 15 TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRRRIgyVI--QQiglfpH-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 86 qvkMTVRE-------LLSfgrfpYSKGRLTTEDYEVIDKVlGyLDLESYGDRYLDTLSGGQLQRA----ALAMilvqDTD 154
Cdd:COG1125 91 ---MTVAEniatvprLLG-----WDKERIRARVDELLELV-G-LDPEEYRDRYPHELSGGQQQRVgvarALAA----DPP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 155 YILLDEPLNNLDmkqSIV--VMQT-IRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1125 157 ILLMDEPFGALD---PITreQLQDeLLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEIL 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-222 |
2.95e-28 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 109.51 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 32 IGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELaKEIAILKQQNTYQVKMTVRELLSFGRfpyskgRLTTED 111
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN-VPPHL-RHINMVFQSYALFPHMTVEENVAFGL------KMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 112 YEVID----KVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKT 187
Cdd:TIGR01187 74 RAEIKprvlEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGIT 153
|
170 180 190
....*....|....*....|....*....|....*
gi 1821109780 188 ILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR01187 154 FVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-226 |
5.87e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.59 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 20 NLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwRTDELAKEIAILKQQNTYQVKMTVRELLSFGR 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 100 FPyskG-RLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD--MKQSIvvMQT 176
Cdd:PRK10771 97 NP---GlKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQEM--LTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1821109780 177 IRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSE 226
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-243 |
6.77e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 6.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElaKEIAILKQQ 82
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRELLSFG--RFPyskgRLTTEDYEVID-KVLGYLD---LESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:PRK10851 83 YALFRHMTVFDNIAFGltVLP----RRERPNAAAIKaKVTQLLEmvqLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVDM 236
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMG 238
|
....*..
gi 1821109780 237 EVEIIKG 243
Cdd:PRK10851 239 EVNRLQG 245
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-223 |
7.75e-28 |
|
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: 106.13 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDEL---AKEIAILKQQ-NTYQVKmTV 91
Cdd:cd03258 21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHfNLLSSR-TV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFgrfP-----YSKgrltTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:cd03258 100 FENVAL---PleiagVPK----AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 167 MKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:cd03258 173 PETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-202 |
2.15e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 104.49 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKD---SGHVLIKGKEITKWRTdeLAKEIA 77
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 78 ILKQQNTYQVKMTVRELLSFGrFPYSKGRltTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:COG4136 80 ILFQDDLLFPHLSVGENLAFA-LPPTIGR--AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYS 202
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG 201
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-212 |
3.51e-27 |
|
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: 104.80 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGT-----VTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEItkwrtdelakeiAILKQQNTYQVKMT 90
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSfgrfpySKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:cd03237 78 VRDLLS------SITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1821109780 171 IVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMkDGK 212
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVF-EGE 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-223 |
5.29e-27 |
|
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: 104.16 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYqVKMTVREL 94
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVL-FDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPyskgRLTTEDYEVIDKVLGYLDLESYGDRYlDT--------LSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:cd03249 97 IRYGKPD----ATDEEVEEAAKKANIHDFIMSLPDGY-DTlvgergsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 167 MKQSIVVMQTIRNMAdeLGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:cd03249 172 AESEKLVQEALDRAM--KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
15-194 |
1.01e-26 |
|
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: 107.83 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC-AQDAHLFDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfpyskGRLTTEDyevIDKVLGYLDLESYGDRY---LDT--------LSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:TIGR02868 429 LRLAR-----PDATDEE---LWAALERVGLADWLRALpdgLDTvlgeggarLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|.
gi 1821109780 164 NLDMKQSIVVMQTIRNmADElGKTILVVLHD 194
Cdd:TIGR02868 501 HLDAETADELLEDLLA-ALS-GRTVVLITHH 529
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-205 |
1.09e-26 |
|
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: 103.99 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 26 GTVTAFIGPNGAGKST--------LLSTMCRLLSKDSGHVLIK---GKEITKWRTDELAKEI-AILKQQNT----YQVKM 89
Cdd:cd03236 26 GQVLGLVGPNGIGKSTalkilagkLKPNLGKFDDPPDWDEILDefrGSELQNYFTKLLEGDVkVIVKPQYVdlipKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLSfgrfpyskgrlTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQ 169
Cdd:cd03236 106 KVGELLK-----------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1821109780 170 SIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNI 205
Cdd:cd03236 175 RLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-217 |
1.11e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.78 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLI---------KGKEITKWRTD---------------E 71
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEKVLEKlviqktrfkkikkikE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 72 LAKEIAILKQQNTYQV-KMTVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMIL 149
Cdd:PRK13651 103 IRRRVGVVFQFAEYQLfEQTIEKDIIFG--PVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 150 VQDTDYILLDEPLNNLDmKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLD-PQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
1.12e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.68 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTdelakeiaiLK 80
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARS---------LS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQntyqvKMTVREL--------LSFGRFPYS-------------KGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQ 139
Cdd:PRK11264 75 QQ-----KGLIRQLrqhvgfvfQNFNLFPHRtvleniiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 140 LQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
12-217 |
1.32e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 101.62 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAILKQQnTYQVKMTV 91
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQR-PYLFDTTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLsfgrfpyskgrlttedyevidkvlgyldlesyGDRyldtLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSI 171
Cdd:cd03247 92 RNNL--------------------------------GRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1821109780 172 VVMQTIRNMADElgKTILVVLHDINfAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03247 136 QLLSLIFEVLKD--KTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-231 |
1.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 103.91 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKW-RTDELAKEIAILKQQNTYQ-VKMT 90
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGIVFQNPETQfVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:PRK13644 95 VEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 171 IVVMQTIRNMaDELGKTILVVLHDINFAAAySDNIIAMKDGKICHSGTVDEVICSEHLKEV 231
Cdd:PRK13644 173 IAVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-213 |
1.51e-26 |
|
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: 102.49 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK---EIAILKQQNTYQVKMTVR 92
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFG-RFPYSKGRLTTEDyevIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSI 171
Cdd:cd03292 97 ENVAFAlEVTGVPPREIRKR---VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1821109780 172 VVMqTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03292 174 EIM-NLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-235 |
1.60e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.92 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLC--KNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAIL 79
Cdd:PRK13632 9 KVENVSfsYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQNTYQ-VKMTVRELLSFG----RFPYSKGRlttedyEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTD 154
Cdd:PRK13632 89 FQNPDNQfIGATVEDDIAFGlenkKVPPKKMK------DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 155 YILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDV 234
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGKPKEILNNKEILEKAKI 241
|
.
gi 1821109780 235 D 235
Cdd:PRK13632 242 D 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
18-222 |
1.72e-26 |
|
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: 105.19 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGkeiTKWRTDE----LAKE---IAILKQQNTYQVKMT 90
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG---RTLFDSRkgifLPPEkrrIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGRfpyskgRLTTEDYEVI--DKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK 168
Cdd:TIGR02142 92 VRGNLRYGM------KRARPSERRIsfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 169 QSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-222 |
2.25e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 103.95 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE----LAKEIAILKQQNTYQV-KMT 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkpLRKKVGIVFQFPEHQLfEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQ 169
Cdd:PRK13634 103 VEKDICFG--PMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 170 SIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-213 |
2.67e-26 |
|
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: 100.75 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNtyqvkmtvrEL 94
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD---------EL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSfgrfpyskGRLTtedyEVIdkvlgyldlesygdryldtLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:cd03246 88 FS--------GSIA----ENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1821109780 175 QTIRNMaDELGKTILVVLHDINFAAAySDNIIAMKDGKI 213
Cdd:cd03246 137 QAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-217 |
4.09e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.34 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 5 NLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwRTDELA---KEIAILKQ 81
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK-----RMNDVPpaeRGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTYQVKMTVRELLSFGRfpyskgRLTTEDYEVIDK----VLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:PRK11000 83 SYALYPHLSVAENMSFGL------KLAGAKKEEINQrvnqVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-223 |
4.65e-26 |
|
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: 101.54 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKqQNTYQVKMTVREL 94
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP-QDTVLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFgrfpyskGRLTTEDYEVI---------DKVLGYLDleSY----GDRYLdTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03253 95 IRY-------GRPDATDEEVIeaakaaqihDKIMRFPD--GYdtivGERGL-KLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLS-TIVNADKIIVLKDGRIVERGTHEELL 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-218 |
8.22e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKG------KEITKWRTDELAKE 75
Cdd:COG4161 4 QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 76 IAILKQQNTYQVKMTVRELLSfgRFPYSKGRLTTED-YEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTD 154
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENLI--EAPCKVLGLSKEQaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 155 YILLDEPLNNLDMKQSIVVMQTIRNMAdELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGT 218
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-223 |
1.02e-25 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 100.76 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV-LQDTFLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfPYSkgrlTTEDYEVIDKVLGYLD----LESYGDRYL----DTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:cd03254 97 IRLGR-PNA----TDEEVIEAAKEAGAHDfimkLPNGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 167 MKQSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:cd03254 172 TETEKLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-223 |
1.05e-25 |
|
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: 100.77 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV-SQDVFLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRL-----TTEDYEVIDKVLGYLDlESYGDRYLdTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQ 169
Cdd:cd03251 96 IAYGRPGATREEVeeaarAANAHEFIMELPEGYD-TVIGERGV-KLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 170 SIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:cd03251 174 ERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-208 |
1.35e-25 |
|
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: 104.68 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQnTYQVKMTVRELL 95
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQH-PFLFAGTIAENI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRfPYSKGrltTEDYEVIDKVlGYLDLESYGDRYLDT--------LSGGQLQRAALAMILVQDTDYILLDEPLNNLDM 167
Cdd:TIGR02857 417 RLAR-PDASD---AEIREALERA-GLDEFVAALPQGLDTpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1821109780 168 KQSIVVMQTIRNMADelGKTILVVLHDINFAAAYsDNIIAM 208
Cdd:TIGR02857 492 ETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-223 |
1.86e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.52 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQnTYQVKMTV 91
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQR-VHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRFPYSKGRLTtedyEVIDKV-LGYLdLEsyGDRYLDT--------LSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:PRK11160 431 RDNLLLAAPNASDEALI----EVLQQVgLEKL-LE--DDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 163 NNLDMKQSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PRK11160 504 EGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELL 561
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-223 |
2.55e-25 |
|
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: 101.28 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSK---DSGHVLIKGKEITKWRTDEL----AKEIAILkQQNTYQV--- 87
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELrkirGREIQMI-FQDPMTSlnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLsfgRFPYSKGRLTTEDyEVIDKVLGYLDL------ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:COG0444 102 VMTVGDQI---AEPLRIHGGLSKA-EARERAIELLERvglpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 162 LNNLDMkqSIV--VMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG0444 178 TTALDV--TIQaqILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-218 |
2.66e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDelaKEIAILKQQntyqVKMTVRell 95
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKD---KYIRPVRKR----IGMVFQ--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 sfgrFPYSKGRLTTEDYEVI--DKVLGyLDLESYGDRYLDTL-----------------SGGQLQRAALAMILVQDTDYI 156
Cdd:PRK13646 93 ----FPESQLFEDTVEREIIfgPKNFK-MNLDEVKNYAHRLLmdlgfsrdvmsqspfqmSGGQMRKIAIVSILAMNPDII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGT 218
Cdd:PRK13646 168 VLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-222 |
5.78e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.56 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 5 NLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElakeiailKQQNT 84
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--------RHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 85 -YQV-----KMTVRELLSFG----RFPYSKGRLTTEDyevidkVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTD 154
Cdd:PRK09452 91 vFQSyalfpHMTVFENVAFGlrmqKTPAAEITPRVME------ALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 155 YILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
16-222 |
7.96e-25 |
|
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: 98.31 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELakeiaILKQQNTYQVKMTVRELL 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRFPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQ 175
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1821109780 176 TIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-223 |
1.38e-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: 101.75 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQntyqVKM---TV 91
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQD----VELfdgTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSfgRFPyskgrlTTEDYEVI---------DKVL----GYldlesygdrylDT--------LSGGQLQRAALAMILV 150
Cdd:COG4618 423 AENIA--RFG------DADPEKVVaaaklagvhEMILrlpdGY-----------DTrigeggarLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 151 QDTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-195 |
1.91e-24 |
|
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: 101.40 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 23 LEQGTVTAFIGPNGAGKSTLLstmcRLLS---------------KDSghVL--IKGKEITKWRTDELAKEI-AILKQQNT 84
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTAL----KILSgelkpnlgdydeepsWDE--VLkrFRGTELQDYFKKLANGEIkVAHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 85 YQ----VKMTVRELLSfgrfpyskgrlTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:COG1245 170 DLipkvFKGTVRELLE-----------KVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|....*
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDI 195
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDL 272
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
12-222 |
2.74e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMT 90
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDNQfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:PRK13650 99 VEDDVAFGL--ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 171 IVVMQTIRNMADELGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13650 177 LELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-213 |
5.11e-24 |
|
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: 95.73 E-value: 5.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVRELL 95
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYV-PQDVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRfPYSkgrlttEDYEVID--KVLGYLDLESYGDRYLDT--------LSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:cd03245 99 TLGA-PLA------DDERILRaaELAGVTDFVNKHPNGLDLqigergrgLSGGQRQAVALARALLNDPPILLLDEPTSAM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 166 DMKQSIVVMQTIRNMADelGKTILVVLHDINFaAAYSDNIIAMKDGKI 213
Cdd:cd03245 172 DMNSEERLKERLRQLLG--DKTLIIITHRPSL-LDLVDRIIVMDSGRI 216
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
16-206 |
5.12e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 100.27 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGT-----VTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwrtdelakeIAILKQQNTYQVKMT 90
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQYIKPDYDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFgrfpySKGRLTTEDY--EVIDKvlgyLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK 168
Cdd:PRK13409 417 VEDLLRS-----ITDDLGSSYYksEIIKP----LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190
....*....|....*....|....*....|....*...
gi 1821109780 169 QSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNII 206
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-232 |
5.24e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 97.26 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELakeIAILKQQNT--YQVKMTVRE 93
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEvdWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSFGRFPYSK--GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSI 171
Cdd:PRK15056 100 VVMMGRYGHMGwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 172 VVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKdGKICHSGTVDEVICSEHLKEVF 232
Cdd:PRK15056 180 RIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAF 238
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-218 |
5.26e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 5.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTmcrLLSKD-----SGHVLIKGKEITKWRTDELAKEI 76
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKV---LMGHPkyevtSGSILLDGEDILELSPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 77 AILKQQNTYQVK-MTVRELLsfgRFPYSKGRLTTED-YEVIDKVLGYLDL----ESYGDRYLD-TLSGGQLQRAALAMIL 149
Cdd:COG0396 79 IFLAFQYPVEIPgVSVSNFL---RTALNARRGEELSaREFLKLLKEKMKElgldEDFLDRYVNeGFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 150 VQDTDYILLDEPLNNLD---MKqsiVVMQTIRNMADElGKTILVVLHD---INFAAAysDNIIAMKDGKICHSGT 218
Cdd:COG0396 156 LLEPKLAILDETDSGLDidaLR---IVAEGVNKLRSP-DRGILIITHYqriLDYIKP--DFVHVLVDGRIVKSGG 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-217 |
5.68e-24 |
|
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: 95.68 E-value: 5.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeITkwrtdelakeiAILKQQNTYQVKMTVREL 94
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VS-----------SLLGLGGGFNPELTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSF-GRFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD---MKQS 170
Cdd:cd03220 105 IYLnGRL---LGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDaafQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1821109780 171 IVVMQTIRNMadelGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03220 182 QRRLRELLKQ----GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-227 |
6.70e-24 |
|
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: 96.80 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE---LAKEIAILKQQNTYQV--KM 89
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDSPSAVnpRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLsfgRFPYSkgRLT----TEDYEVIDKVLGYLDLES-YGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:TIGR02769 106 TVRQII---GEPLR--HLTsldeSEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 165 LDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEH 227
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKH 243
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-213 |
6.70e-24 |
|
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: 94.03 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKW-RTDELAKEIAILk 80
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIAMV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 qqntYQvkmtvrellsfgrfpyskgrlttedyevidkvlgyldlesygdryldtLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:cd03216 81 ----YQ------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-220 |
7.42e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.85 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEItKWRTDELAKEIAILK 80
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 -------QQNTYQVKMTVRELLSfgRFPYSKGRLT-TEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQD 152
Cdd:PRK11124 82 rnvgmvfQQYNLWPHLTVQQNLI--EAPCRVLGLSkDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 153 TDYILLDEPLNNLDMKQSIVVMQTIRNMAdELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVD 220
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
15-223 |
9.04e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 9.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwrtdelakeIAILKQQNT-YQVKMTVRE 93
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-------------VSALLELGAgFHPELTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLsfgrfpYSKGRL---TTEDY-EVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD--- 166
Cdd:COG1134 108 NI------YLNGRLlglSRKEIdEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDaaf 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 167 MKQSivvMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1134 182 QKKC---LARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-232 |
9.49e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.72 E-value: 9.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAIL 79
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREaVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQNTYQVKMTVRELLSFGRFPYSKgrltTEDYEVIDKVLG-YLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAER----DQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 159 DEPLNNLdmkQSIVVMQ---TIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVF 232
Cdd:PRK11614 162 DEPSLGL---APIIIQQifdTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-194 |
9.69e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 9.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkWRtdelakeIAILKQQ 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----LR-------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRE--LLSFGRF---------PYSKGRLTTEDYEVIDKVLGYLDL--------------------ESYGDRY 131
Cdd:COG0488 70 PPLDDDLTVLDtvLDGDAELraleaeleeLEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilsglgfpEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 132 LDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDmkqsivvMQTIRNMADEL---GKTILVVLHD 194
Cdd:COG0488 150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEEFLknyPGTVLVVSHD 208
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
15-212 |
1.24e-23 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 94.62 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK---EIAILKQQNTYQVKMTV 91
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrrRIGVVFQDFRLLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFgrfPYS-KGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:TIGR02673 97 YENVAL---PLEvRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1821109780 171 IVVMQTIRNMADeLGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:TIGR02673 174 ERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-205 |
1.34e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 99.11 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 23 LEQGTVTAFIGPNGAGKST--------LLSTMCRLLSKDSGHVLIK---GKEITKWRTDELAKEI-AILKQQntY----- 85
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTavkilsgeLIPNLGDYEEEPSWDEVLKrfrGTELQNYFKKLYNGEIkVVHKPQ--Yvdlip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 86 -QVKMTVRELLSfgrfpyskgrlTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK13409 174 kVFKGKVRELLK-----------KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1821109780 165 LDMKQSIVVMQTIRNMADelGKTILVVLHDINFAAAYSDNI 205
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNV 281
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
13-221 |
1.37e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKdSGHVLIKGKEI-----TKWRtdelaKEIAILKQqNTYQV 87
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELreldpESWR-----KHLSWVGQ-NPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLSFGRFPYSKGRLttedYEVIDK--VLGYLDLESYGdryLDT--------LSGGQLQRAALAMILVQDTDYIL 157
Cdd:PRK11174 436 HGTLRDNVLLGNPDASDEQL----QQALENawVSEFLPLLPQG---LDTpigdqaagLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMAdeLGKTILVVLHDINFAAAYsDNIIAMKDGKICHSGTVDE 221
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-228 |
1.64e-23 |
|
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: 94.86 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYqVKMTVREL 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL-FNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLT-----TEDYEVIDKV-LGYLDLesYGDRYLdTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK 168
Cdd:cd03252 96 IALADPGMSMERVIeaaklAGAHDFISELpEGYDTI--VGEQGA-GLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 169 QSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVICSEHL 228
Cdd:cd03252 173 SEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-193 |
1.81e-23 |
|
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: 93.77 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLST-MCRLLS-KDSGHVLIKGKEITKwrtDELAKEIAILKQQNTYQVKMT 90
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAlAGRRTGlGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFgrfpyskgrlTTEdyevidkvlgyldlesygdryLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:cd03213 99 VRETLMF----------AAK---------------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|...
gi 1821109780 171 IVVMQTIRNMADElGKTILVVLH 193
Cdd:cd03213 148 LQVMSLLRRLADT-GRTIICSIH 169
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-223 |
1.99e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.69 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA---KEIAILKQQ-Ntyqvkmtv 91
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRaarRKIGMIFQHfN-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 reLLS----FG--RFP-----YSKGrlttedyEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:COG1135 93 --LLSsrtvAEnvALPleiagVPKA-------EIRKRVAELLElvgLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 158 LDEPLNNLDMK--QSIV-VMQTIRnmaDELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:COG1135 164 CDEATSALDPEttRSILdLLKDIN---RELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVF 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
6-222 |
2.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.54 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 6 LCKNIC----------ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKG----KEITKWrtdE 71
Cdd:PRK13633 6 KCKNVSykyesneestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsDEENLW---D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 72 LAKEIAILKQQNTYQVKMT-VRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILV 150
Cdd:PRK13633 83 IRNKAGMVFQNPDNQIVATiVEEDVAFG--PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 151 QDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYME-EAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-235 |
2.97e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLI----------KGKEITKWRtdelaKEIAILKQQNTY 85
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlkKIKEVKRLR-----KEIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 86 QV-KMTVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK13645 102 QLfQETIEKDIAFG--PVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 164 NLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFDVD 235
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEID 251
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-221 |
2.98e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIkGKEItkwrtdelakEIAILKQQ 82
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTY-QVKMTVRELLSfgrfpyskgRLTTEDYEVidKVLGYldLESYG------DRYLDTLSGGQLQRAALAMILVQDTDY 155
Cdd:COG0488 387 QEElDPDKTVLDELR---------DGAPGGTEQ--EVRGY--LGRFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 156 ILLDEPLNNLDmkqsivvMQTIRNMADELGK---TILVVLHDINFAAAYSDNIIAMKDGKI-CHSGTVDE 221
Cdd:COG0488 454 LLLDEPTNHLD-------IETLEALEEALDDfpgTVLLVSHDRYFLDRVATRILEFEDGGVrEYPGGYDD 516
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-212 |
3.82e-23 |
|
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: 92.92 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwrtdelakeIAILKQ----QNTyqvkmT 90
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQepwiQNG-----T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGRfPYSKgrlttEDYE-VID--------KVLGYLDLESYGDRYLdTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03250 82 IRENILFGK-PFDE-----ERYEkVIKacalepdlEILPDGDLTEIGEKGI-NLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 162 LNNLDMKQSIVVMQT-IRNMAdELGKTILVVLHDINFaAAYSDNIIAMKDGK 212
Cdd:cd03250 155 LSAVDAHVGRHIFENcILGLL-LNNKTRILVTHQLQL-LPHADQIVVLDNGR 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-217 |
4.57e-23 |
|
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: 93.55 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGkEITKWRTDELAKEIA-ILKQQNTYQVKMTVREL 94
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGvVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYskgRLTTEDY-EVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDmkqsIVV 173
Cdd:cd03267 116 FYLLAAIY---DLPPARFkKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD----VVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 174 MQTIRNMADEL----GKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:cd03267 189 QENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-231 |
5.35e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.43 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMTVREL 94
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQfVGSIVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFG----RFPYSKGrlttedYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:PRK13648 105 VAFGlenhAVPYDEM------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 171 IVVMQTIRNMADELGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI-CSEHLKEV 231
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITHDLS-EAMEADHVIVMNKGTVYKEGTPTEIFdHAEELTRI 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-222 |
8.43e-23 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 93.33 E-value: 8.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEItKWRTD---EL----AKE 75
Cdd:COG4598 11 VRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKPDrdgELvpadRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 76 IAILKQQ--------NTYQvKMTVRELLSFGrfP-YSKGRlttEDYEVIDKVLGYLD---LESYGDRYLDTLSGGQLQRA 143
Cdd:COG4598 90 LQRIRTRlgmvfqsfNLWS-HMTVLENVIEA--PvHVLGR---PKAEAIERAEALLAkvgLADKRDAYPAHLSGGQQQRA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 144 ALAMILVQDTDYILLDEPLNNLDmkQSIV--VMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALD--PELVgeVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
.
gi 1821109780 222 V 222
Cdd:COG4598 241 V 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-223 |
8.98e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 95.87 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDEL----AKEIAILKQQNTYQVKMTV 91
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD----- 166
Cdd:PRK10070 124 LDNTAFGM--ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirt 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 167 -MKQSIVVMQTIRNmadelgKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PRK10070 202 eMQDELVKLQAKHQ------RTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-222 |
2.62e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 2.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGH---VLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMT 90
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREKVGIVFQNPDNQfVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:PRK13640 102 VGDDVAFGL--ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 171 IVVMQTIRNMADELGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-213 |
2.88e-22 |
|
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: 91.34 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK----EIAILkQQNtYQV--K 88
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlrarHVGFV-FQS-FQLlpT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRE-----LLSFGRfPYSKGRLTTEdyevidkvlgyldLESYG-----DRYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:COG4181 105 LTALEnvmlpLELAGR-RDARARARAL-------------LERVGlghrlDHYPAQLSGGEQQRVALARAFATEPAILFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAySDNIIAMKDGKI 213
Cdd:COG4181 171 DEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-218 |
4.30e-22 |
|
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: 94.78 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAiLKQQNTYQVKMTVRELL 95
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVA-LVSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRfpyskgrLTTEDYEVIDKVLGYLDLESYGDRY---LDT--------LSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:TIGR02203 427 AYGR-------TEQADRAEIERALAAAYAQDFVDKLplgLDTpigengvlLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 165 LDMKQSIVVMQTIrnmaDEL--GKTILVVLHDINfAAAYSDNIIAMKDGKICHSGT 218
Cdd:TIGR02203 500 LDNESERLVQAAL----ERLmqGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGT 550
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-195 |
4.45e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 91.46 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDElakeiAILKQQNTYQVKMTVREL 94
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-----GVVFQKDALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFG-RFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDM---KQs 170
Cdd:COG4525 97 VAFGlRL---RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQ- 172
|
170 180
....*....|....*....|....*.
gi 1821109780 171 ivvMQT-IRNMADELGKTILVVLHDI 195
Cdd:COG4525 173 ---MQElLLDVWQRTGKGVFLITHSV 195
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-206 |
5.89e-22 |
|
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: 94.47 E-value: 5.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 22 ELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVlikgkeitkwrtdELAKEIAILKQQNTYQVKMTVRELLSFGrfp 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQYISPDYDGTVEEFLRSA--- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 102 ySKGRLTTEDY--EVIDKvlgyLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRN 179
Cdd:COG1245 426 -NTDDFGSSYYktEIIKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500
|
170 180
....*....|....*....|....*..
gi 1821109780 180 MADELGKTILVVLHDINFAAAYSDNII 206
Cdd:COG1245 501 FAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2-232 |
6.08e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.86 E-value: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE-IAILK 80
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRE-LLSFGRF-PYSKgrltTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:COG1137 85 QEASIFRKLTVEDnILAVLELrKLSK----KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 159 DEPLNNLDmkqSIVVMQtIRNMADEL-GKTILVVLHDINFAA-------AYsdnIIAmkDGKICHSGTVDEVICSEHLKE 230
Cdd:COG1137 161 DEPFAGVD---PIAVAD-IQKIIRHLkERGIGVLITDHNVREtlgicdrAY---IIS--EGKVLAEGTPEEILNNPLVRK 231
|
..
gi 1821109780 231 VF 232
Cdd:COG1137 232 VY 233
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-221 |
7.59e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.96 E-value: 7.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLST-MCRLL--SKDSGHVLIKGKEITKWrtdELAKEIAILKQQNTYQVKMTV 91
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNAlAFRSPkgVKGSGSVLLNGMPIDAK---EMRAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSF------GRFPYSKGRLttedyEVIDKVLGYLDLESYGD------RYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:TIGR00955 117 REHLMFqahlrmPRRVTKKEKR-----ERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 160 EPLNNLD--MKQSIVvmQTIRNMADElGKTILVVLH----DI--NFaaaysDNIIAMKDGKICHSGTVDE 221
Cdd:TIGR00955 192 EPTSGLDsfMAYSVV--QVLKGLAQK-GKTIICTIHqpssELfeLF-----DKIILMAEGRVAYLGSPDQ 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-233 |
8.22e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 8.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRL--LSKD---SGHVLIKGKEITKWRTD--ELAKEIAILKQQ-NTYqv 87
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQpNPF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLSFGRfpyskgRLT-TEDYEVIDKVL-----GYLDLESYGDRYLDT---LSGGQLQRAALAMILVQDTDYILL 158
Cdd:PRK14239 99 PMSIYENVVYGL------RLKgIKDKQVLDEAVekslkGASIWDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADELgkTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEVFD 233
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
16-223 |
8.80e-22 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 93.78 E-value: 8.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVRELL 95
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYV-PQDPRLFYGTLRDNI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRfPYskgrltTEDYEVIDK-----VLGYLDLESYGdryLDT--------LSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:TIGR03375 560 ALGA-PY------ADDEEILRAaelagVTEFVRRHPDG---LDMqigergrsLSGGQRQAVALARALLRDPPILLLDEPT 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 163 NNLDMKQSivvMQTIRNMADEL-GKTILVVLHDINFaAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:TIGR03375 630 SAMDNRSE---ERFKDRLKRWLaGKTLVLVTHRTSL-LDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-222 |
1.13e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.41 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILK 80
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTvrelLSFGRFP-YSKGRLTTEDYEVIDKVLG------------YLDL----ESYGDRYLDTLSGGQLQRA 143
Cdd:PRK10619 86 QLRLLRTRLT----MVFQHFNlWSHMTVLENVMEAPIQVLGlskqeareravkYLAKvgidERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 144 ALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-222 |
2.79e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLL-----SKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKM 89
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLSFG----RFPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:PRK14247 98 SIFENVALGlklnRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 166 DMKQSivvmQTIRNMADELGK--TILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK14247 178 DPENT----AKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-220 |
2.84e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDelakeiailkqq 82
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 ntyqVKMTVRE--LLsfgrfPYSKgrlttedyeVIDKV-LGYLD---------LESYG--DRYLD---TLSGGQLQRAAL 145
Cdd:PRK11247 83 ----TRLMFQDarLL-----PWKK---------VIDNVgLGLKGqwrdaalqaLAAVGlaDRANEwpaALSGGQKQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 146 AMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVD 220
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
15-223 |
3.48e-21 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 92.03 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQntyqVKM---TV 91
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQD----VELfpgTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLS-FGRFPyskgrlttEDYEVID--KVLG----YLDLESYGDRYL----DTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:TIGR01842 409 AENIArFGENA--------DPEKIIEaaKLAGvhelILRLPDGYDTVIgpggATLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNmADELGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKA-LKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-212 |
3.48e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.90 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEIT-KWRTDELAKEIAILKQQNTYQVKMTVREL 94
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLTTED--YEVIDKvLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIV 172
Cdd:PRK11288 100 LYLGQLPHKGGIVNRRLlnYEAREQ-LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1821109780 173 VMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:PRK11288 179 LFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
4.33e-21 |
|
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: 85.96 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwrtdelakeiailkq 81
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 qntyqvkmtvrelLSFGrfpyskgrlttedyevidkvlgyldlesygdrYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:cd03221 63 -------------VKIG--------------------------------YFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 162 LNNLDMkQSIvvmQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:cd03221 98 TNHLDL-ESI---EALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-222 |
5.33e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLI---------KGKEITKWRtdelaKEIAILKQQNTYQ 86
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIKPVR-----KKVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 87 V-KMTVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK13643 97 LfEETVLKDVAFG--PQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 165 LDMKQSIVVMQTIRNMaDELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13643 175 LDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-230 |
6.86e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA--KEIAILKQQNTYQVKMTVR 92
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlrQQVATVFQDPEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 EllsfGRFPYSKGRLTTEDYEV---IDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQ 169
Cdd:PRK13638 96 D----SDIAFSLRNLGVPEAEItrrVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 170 SIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI-CSEHLKE 230
Cdd:PRK13638 172 RTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAMEQ 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
12-222 |
1.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.35 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTD----ELAKEIAILKQQNTYQV 87
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 -KMTVRELLSFG--RFPYSKGRLTTEDYEVIDKVlgYLDlESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK13641 99 fENTVLKDVEFGpkNFGFSEDEAKEKALKWLKKV--GLS-EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 165 LDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-213 |
1.57e-20 |
|
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: 86.76 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKmTV 91
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRFPYSKGRLTtedyEVIDKVLGYLDLESYGDRYlDT--------LSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:cd03248 105 QDNIAYGLQSCSFECVK----EAAQKAHAHSFISELASGY-DTevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1821109780 164 NLDMKQSIVVMQTIRNmaDELGKTILVVLHDINfAAAYSDNIIAMKDGKI 213
Cdd:cd03248 180 ALDAESEQQVQQALYD--WPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-222 |
1.63e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrTDELAKEIAILKQQ--------NTYQV 87
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLIT---STSKNKDIKQIRKKvglvfqfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLSFGrfPYSKGrLTTEDYEVI--DKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:PRK13649 100 EETVLKDVAFG--PQNFG-VSQEEAEALarEKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 166 DMKQSIVVMQTIRNMaDELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK13649 177 DPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-200 |
1.76e-20 |
|
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: 86.01 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAILKQQNTYQVKMTVREL 94
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKgrlttedyEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:cd03231 94 LRFWHADHSD--------EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180
....*....|....*....|....*.
gi 1821109780 175 QTIRNMADELGKTILVVLHDINFAAA 200
Cdd:cd03231 166 EAMAGHCARGGMVVLTTHQDLGLSEA 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-226 |
2.63e-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: 85.66 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLST-MCRLLSK-DSGHVLIKGKEITKWRTDELAKEIAIL 79
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTiMGHPKYEvTEGEILFKGEDITDLPPEERARLGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQNTYQVKM-TVRELLsfgrfpyskgrlttedyevidkvlgyldlesygdRYLD-TLSGGQLQRAALAMILVQDTDYIL 157
Cdd:cd03217 82 AFQYPPEIPGvKNADFL----------------------------------RYVNeGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHD---INFAAAysDNIIAMKDGKICHSGTVDEVICSE 226
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYqrlLDYIKP--DRVHVLYDGRIVKSGDKELALEIE 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-219 |
3.05e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 3.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 4 NNLCKNICE----TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAK----E 75
Cdd:PRK11629 9 DNLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 76 IAILKQQNTYQVKMTVRE-----LLSFGRFPyskgrltTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILV 150
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALEnvampLLIGKKKP-------AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 151 QDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNiIAMKDGKICHSGTV 219
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLTAELSL 229
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1-220 |
6.63e-20 |
|
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: 85.39 E-value: 6.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTM-----CRLlskDSGHVLIKGKEITKWRTDELAKE 75
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpsYEV---TSGTILFKGQDLLELEPDERARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 76 IAILKQQNTYQV-----KMTVRELLSFGRFPYSKGRLTTEDY-EVIDKVLGYLDL-ESYGDRYLDT-LSGGQLQRAALAM 147
Cdd:TIGR01978 78 GLFLAFQYPEEIpgvsnLEFLRSALNARRSARGEEPLDLLDFeKLLKEKLALLDMdEEFLNRSVNEgFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 148 ILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDIN-FAAAYSDNIIAMKDGKICHSGTVD 220
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREP-DRSFLIITHYQRlLNYIKPDYVHVLLDGRIVKSGDVE 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-240 |
7.33e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 7.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAIL---KQQNTYQvkMTVR 92
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVfgqRSQLWWD--LPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 EllSFgrfpyskgRLTTEDYEV--------IDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:COG4586 115 D--SF--------RLLKAIYRIpdaeykkrLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 165 LDmkqsiVVMQT-----IRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEvicsehLKEVFDVDMEVE 239
Cdd:COG4586 185 LD-----VVSKEairefLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE------LKERFGPYKTIV 253
|
.
gi 1821109780 240 I 240
Cdd:COG4586 254 L 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-222 |
9.85e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 9.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkWRTDELAKE--IAILkqqntYQ----V-K 88
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRSPRDAQAagIAII-----HQelnlVpN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFGRFPYSKGRLtteDY--------EVIDKvLGY-LDLesygDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:COG1129 94 LSVAENIFLGREPRRGGLI---DWramrrrarELLAR-LGLdIDP----DTPVGDLSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 160 EPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-223 |
1.00e-19 |
|
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: 87.87 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQnTYQVKMTVREL 94
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQE-PYIFSGSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGrfpySKGRLTTEDY-------EVIDKV----LGY-LDLESYGDryldTLSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:TIGR01193 568 LLLG----AKENVSQDEIwaaceiaEIKDDIenmpLGYqTELSEEGS----SISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 163 NNLDMKQSIVVMQTIRNMADelgKTILVVLHDINFAAAySDNIIAMKDGKICHSGTVDEVI 223
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-220 |
1.00e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.77 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkWRT--DELAKEIAILKQ-----QNtyqvk 88
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSprDAIALGIGMVHQhfmlvPN----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFGRFPYSKGRLTTEdyEVIDKVlgyLDL-ESYG-----DRYLDTLSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:COG3845 95 LTVAENIVLGLEPTKGGRLDRK--AARARI---RELsERYGldvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 163 NNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKIchSGTVD 220
Cdd:COG3845 170 AVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKV--VGTVD 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-222 |
1.07e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.20 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEI---TKWRTDELAKEIAILKQQNTYQVK 88
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSfgrFPYskgRLTTEDYEVIDKVLGYLDLESYGDR-----YLDTLSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK11831 99 MNVFDNVA---YPL---REHTQLPAPLLHSTVMMKLEAVGLRgaaklMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 164 NLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
1.08e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNL-C----KNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIK----GKEITKWRTD- 70
Cdd:PRK13631 22 LRVKNLyCvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELIt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 71 -----------ELAKEIAILKQQNTYQV-KMTVRELLSFGrfPYSKGRLTTEDYEVIDKVLGYLDL-ESYGDRYLDTLSG 137
Cdd:PRK13631 102 npyskkiknfkELRRRVSMVFQFPEYQLfKDTIEKDIMFG--PVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 138 GQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNmADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
250
....*....|.
gi 1821109780 218 TVDEVICSEHL 228
Cdd:PRK13631 259 TPYEIFTDQHI 269
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
15-228 |
1.08e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAILKQQNTYQVKMTVRE- 93
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEFTVREn 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSFGRFpyskGRLTTEDYE-VIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIV 172
Cdd:PRK13536 135 LLVFGRY----FGMSTREIEaVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 173 VMQTIRNMAdELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVIcSEHL 228
Cdd:PRK13536 211 IWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI-DEHI 264
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-211 |
1.13e-19 |
|
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: 84.30 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGK---EITKWRTDELAKEIAILKQQNTYQVKMTVR 92
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFGRfPYSKGRLTTedyeVID--------KVLGYLDLESYGDRYLDtLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:cd03290 97 ENITFGS-PFNKQRYKA----VTDacslqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 165 LDMKQSIVVMQT-IRNMADELGKTILVVLHDINFaAAYSDNIIAMKDG 211
Cdd:cd03290 171 LDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-226 |
1.19e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.01 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAILK 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRE-LLSFGRFpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:PRK13537 87 QFDNLDPDFTVREnLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 160 EPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSE 226
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-223 |
1.32e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 87.38 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTV 91
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALV-SQNVHLFNDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRfpysKGRLTTEDYEVIDKVLGYLDLESYGDRYLDT--------LSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK11176 434 ANNIAYAR----TEQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 164 NLDMKQSIVVMQTIrnmaDELGK--TILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PRK11176 510 ALDTESERAIQAAL----DELQKnrTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-221 |
2.14e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.08 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV-GQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGrfpyskgrLT-TEDYEVID--KVLGYLDLESYGDRYLDT--------LSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:TIGR00958 575 IAYG--------LTdTPDEEIMAaaKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 164 NLDMkQSIVVMQTIRNMADelgKTILVVLHDINFAAAySDNIIAMKDGKICHSGTVDE 221
Cdd:TIGR00958 647 ALDA-ECEQLLQESRSRAS---RTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQ 699
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-227 |
2.16e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.04 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwRTDELAKEIAILK 80
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFG----RFPysKGRLTTEdyevIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGlkqdKLP--KAEIASR----VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVIcsEH 227
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY--EH 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-223 |
3.12e-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: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNIC--ETCILK---DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIK-GKE---ITKWRTDE 71
Cdd:TIGR03269 280 IKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 72 ---LAKEIAILKQQNTYQVKMTVRELLSFG---RFPYSKGRLTTedyeVID-KVLGYLD--LESYGDRYLDTLSGGQLQR 142
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPHRTVLDNLTEAiglELPDELARMKA----VITlKMVGFDEekAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 143 AALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
.
gi 1821109780 223 I 223
Cdd:TIGR03269 516 V 516
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-232 |
9.59e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 9.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE--------L 72
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArarrgigyL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 73 AKEIAILKQQNTYQVKMTVRELlsfgrfpysKGRLTTEDYEV-IDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQ 151
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQI---------RDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 152 DTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEHLKEV 231
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
.
gi 1821109780 232 F 232
Cdd:PRK10895 234 Y 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-166 |
9.69e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 9.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 7 CKNIC----ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrTDELAKEIAILKQQ 82
Cdd:PRK13539 5 GEDLAcvrgGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEACHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRELLSFGRFPYSKGRLTtedyevIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFLGGEELD------IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
....
gi 1821109780 163 NNLD 166
Cdd:PRK13539 156 AALD 159
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
12-192 |
1.14e-18 |
|
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: 81.25 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAILKQQNTYQVKMTV 91
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRFPYSKGRLTTEDyevidkVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDmKQSI 171
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIED------ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGV 163
|
170 180
....*....|....*....|.
gi 1821109780 172 VVMQTIrnMADELGKTILVVL 192
Cdd:TIGR01189 164 ALLAGL--LRAHLARGGIVLL 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
16-242 |
1.15e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQ-VKMTVREL 94
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfpYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:PRK13642 103 VAFGM--ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 175 QTIRNMADELGKTILVVLHDINFAAAySDNIIAMKDGKICHSGTVDEVIC-SEHLKEV-FDVDMEVEIIK 242
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAtSEDMVEIgLDVPFSSNLMK 249
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-222 |
2.00e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 19 INLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVK-MTVRELLSF 97
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFReMTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 98 GRFPYSK-----GRLTTEDY-----EVIDKVLGYLD---LESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK11300 104 AQHQQLKtglfsGLLKTPAFrraesEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 165 LDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK11300 184 LNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-222 |
2.74e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 81.24 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLL-----SKDSGHVLIKGKEITKWRTD--ELA 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDIYDPDVDvvELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 74 KEIAILKQqntyqvK-----MTVRELLSFG---RFPYSKGRL--TTEDY--------EVIDKvlgyldlesygdryLDT- 134
Cdd:COG1117 92 RRVGMVFQ------KpnpfpKSIYDNVAYGlrlHGIKSKSELdeIVEESlrkaalwdEVKDR--------------LKKs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 135 ---LSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELgkTILVVLHDINFAAAYSDNIIAMKDG 211
Cdd:COG1117 152 algLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLG 229
|
250
....*....|.
gi 1821109780 212 KICHSGTVDEV 222
Cdd:COG1117 230 ELVEFGPTEQI 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-211 |
3.06e-18 |
|
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: 79.59 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLstmcRLLS--KDSGHV----LIKGKEITKwrtdELAKEIAILKQQNTYQVK 88
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLL----DVLAgrKTAGVItgeiLINGRPLDK----NFQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFgrfpyskgrlttedyevidkvlgyldlesygDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK 168
Cdd:cd03232 94 LTVREALRF-------------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1821109780 169 QSIVVMQTIRNMADElGKTILVVLH----DInFaaAYSDNIIAMKDG 211
Cdd:cd03232 143 AAYNIVRFLKKLADS-GQAILCTIHqpsaSI-F--EKFDRLLLLKRG 185
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-222 |
5.04e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLL-----SKDSGHVLIKGKEITKWRTD--ELAKEIAILKQQNTYQV 87
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLSFG----RFPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK14267 99 HLTIYDNVAIGvklnGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 164 NLDMKQSIVVMQTIRNMADELgkTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
16-222 |
6.14e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.39 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKE---IAILKQQ-Ntyqvkmtv 91
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArrqIGMIFQHfN-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 reLLS----FGR--FPYskgRLTTEDYEVIDK-VLGYLD---LESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:PRK11153 93 --LLSsrtvFDNvaLPL---ELAGTPKAEIKArVTELLElvgLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 162 LNNLDMK--QSIvvMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK11153 168 TSALDPAttRSI--LELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-218 |
6.51e-18 |
|
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: 82.75 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKnICETC---ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAIL 79
Cdd:TIGR01257 931 VKNLVK-IFEPSgrpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQNTYQVKMTVRELLSFgrFPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILF--YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 160 EPLNNLDMKQSivvmqtiRNMADEL-----GKTILVVLHDINFAAAYSDNIIAMKDGKICHSGT 218
Cdd:TIGR01257 1087 EPTSGVDPYSR-------RSIWDLLlkyrsGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
15-227 |
9.12e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.12 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA---KEIAILKQQNTYQV--KM 89
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafrRDIQMVFQDSISAVnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLsfgRFPYSkgRLTT----EDYEVIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK10419 107 TVREII---REPLR--HLLSldkaERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 165 LDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEH 227
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSS 244
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-222 |
1.33e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 80.66 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrtDELAKE--IAILKQQNTYQVKMTVR 92
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN----ELEPADrdIAMVFQNYALYPHMSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFGRfpysKGRLT--TEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:PRK11650 95 ENMAYGL----KIRGMpkAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 171 IVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK11650 171 VQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-193 |
2.03e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 81.31 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSK---DSGHVLIKGKEitkwRTDELAKEIAILKQQNTYQVKMTV 91
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRP----LDSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFG---RFPYSKGRltTEDYEVIDKVLGYLDLESYGDRYLDT----LSGGQLQRAALAMILVQDTDYIL-LDEPLN 163
Cdd:TIGR00956 854 RESLRFSaylRQPKSVSK--SEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
|
170 180 190
....*....|....*....|....*....|
gi 1821109780 164 NLDMKQSIVVMQTIRNMADElGKTILVVLH 193
Cdd:TIGR00956 932 GLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-222 |
2.21e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLikgkeitkwRTDELakEIAILKQQNTYQVKMTvrel 94
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL--RIGYVPQKLYLDTTLP---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLTTEDyevIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:PRK09544 84 LTVNRFLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 175 QTIRNMADELGKTILVVLHDINFAAAYSDNIIAMkDGKICHSGTVDEV 222
Cdd:PRK09544 161 DLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-222 |
4.00e-17 |
|
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: 80.11 E-value: 4.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSkDSGHVLIKGKEITKWRTDELAKeiaiLKQQntYQV-------- 87
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRP----LRRR--MQVvfqdpfgs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 ---KMTVRELLSFG----RFPYSKgrltTEDYEVIDKVL---GyLDlESYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:COG4172 375 lspRMTVGQIIAEGlrvhGPGLSA----AERRARVAEALeevG-LD-PAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 158 LDEPLNNLDM---KQsivVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG4172 449 LDEPTSALDVsvqAQ---ILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-225 |
4.59e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.21 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGH-----VLIKGKEITKWR-TDELAK 74
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRdVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 75 EIAILKQQ-NTYQVKMT--------VRELLSFGRFP-YSKGRLTTedyevidkvLGYLDleSYGDRYLDT---LSGGQLQ 141
Cdd:PRK14271 102 RVGMLFQRpNPFPMSIMdnvlagvrAHKLVPRKEFRgVAQARLTE---------VGLWD--AVKDRLSDSpfrLSGGQQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 142 RAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELgkTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:PRK14271 171 LLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQ 248
|
....
gi 1821109780 222 VICS 225
Cdd:PRK14271 249 LFSS 252
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-218 |
4.67e-17 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 77.15 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKqQNTYQVKMTVREL 94
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIP-QDPVLFSGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 L-SFGRfpYSKGRL--TTED---YEVIDKVLGYLD--LESYGdrylDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:cd03244 98 LdPFGE--YSDEELwqALERvglKEFVESLPGGLDtvVEEGG----ENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 167 MKQSIVVMQTIR-NMADelgKTILVVLHDINfAAAYSDNIIAMKDGKICHSGT 218
Cdd:cd03244 172 PETDALIQKTIReAFKD---CTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDS 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-210 |
5.62e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.92 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtdelakEIAILKQqntyqvkmtvreL 94
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGR------EASLIDA------------I 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLTTedyevidkvLGYLDLESYGDRYlDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:COG2401 107 GRKGDFKDAVELLNA---------VGLSDAVLWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1821109780 175 QTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKD 210
Cdd:COG2401 177 RNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-222 |
5.67e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.62 E-value: 5.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKeiaiLKQ------QNTYQV---K 88
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRrmqmvfQDPYASlnpR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFgrfPYSKGRLTTEDyEVIDKVLGYLDL----ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:COG4608 112 MTVGDIIAE---PLRIHGLASKA-ERRERVAELLELvglrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 165 LDMkqSI--VVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:COG4608 188 LDV--SIqaQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-221 |
7.22e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 79.55 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVlikgkeitKWrtDELAKeIAILKQQ 82
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------KW--SENAN-IGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVK--MTVRELLsfgrfpySKGRLTTEDYEVIDKVLGYLdLESYGD--RYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:PRK15064 391 HAYDFEndLTLFDWM-------SQWRQEGDDEQAVRGTLGRL-LFSQDDikKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 159 DEPLNNLDMkQSIVVMqtirNMADELGK-TILVVLHDINFAAAYSDNIIAMKDGKICH-SGTVDE 221
Cdd:PRK15064 463 DEPTNHMDM-ESIESL----NMALEKYEgTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEE 522
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
16-222 |
8.33e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWrTDELAKE--IAILKQQNTYQVKMTVRE 93
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAAQlgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSFGRFP-----------YSKGRLTTEdyEVIDKVLGYLDLesygDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:PRK09700 100 NLYIGRHLtkkvcgvniidWREMRVRAA--MMLLRVGLKVDL----DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 163 NNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK09700 174 SSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-223 |
1.96e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.22 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVV-SQTPFLFSDTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfPYSkgrlTTEDYE-------VIDKVL----GYlDLEsYGDRYLdTLSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK10789 409 IALGR-PDA----TQQEIEhvarlasVHDDILrlpqGY-DTE-VGERGV-MLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 164 NLDMKQSIVVMQTIRNMADelGKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-225 |
2.24e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 76.24 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 10 ICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLS------KDSGHVLIKGKEITKWRTDELAKEIAILKQQN 83
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 84 TYQVKMTVRELLSFGRFPY---SKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHgikEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADELgkTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICS 225
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-222 |
2.30e-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: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLC----KNICETCILKDINLELEQGTVTAFIGPNGAGKS-TLLSTMcRLL----SKDSGHVLIKGKEITKWRTDE 71
Cdd:COG4172 7 LSVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLpdpaAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 72 LAK----EIAILkqqntYQVKMT-----------VRELLSFGRfPYSKGRLTTEDYEVIDKVlGYLDLESYGDRYLDTLS 136
Cdd:COG4172 86 LRRirgnRIAMI-----FQEPMTslnplhtigkqIAEVLRLHR-GLSGAAARARALELLERV-GIPDPERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 137 GGQLQRAALAMILVQDTDYILLDEPLNNLDM---KQsivVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQ---ILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
....*....
gi 1821109780 214 CHSGTVDEV 222
Cdd:COG4172 236 VEQGPTAEL 244
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-223 |
3.18e-16 |
|
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: 78.06 E-value: 3.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGkeitkwrtdelakEIAILKQQNTYQvKMTVRELL 95
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQ-NDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRfpyskgRLTTEDYEVIDKVLGYL-DLE--SYGDRYL-----DTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDM 167
Cdd:TIGR00957 720 LFGK------ALNEKYYQQVLEACALLpDLEilPSGDRTEigekgVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 168 KQSIVVMQ-TIRNMADELGKTILVVLHDINFAAAySDNIIAMKDGKICHSGTVDEVI 223
Cdd:TIGR00957 794 HVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-222 |
3.34e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrtdELAKEiaILKQQNTY--QVKM 89
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS-----TLKPE--IYRQQVSYcaQTPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 ----TVRELLSfgrFPYsKGRLTTEDYEVIDKVLGYLDL-ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK10247 92 lfgdTVYDNLI---FPW-QIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 165 LDMKQSIVVMQTIRNMADELGKTILVVLHDINfAAAYSDNIIAMKDgkicHSGTVDEV 222
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKVITLQP----HAGEMQEA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
16-221 |
3.42e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.91 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE---LAKEIAILKQQNTYQVKMTVR 92
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSfgrFPYSKGRLTTEDYE-----VIDKVlGYLDlesYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDM 167
Cdd:PRK10908 98 DNVA---IPLIIAGASGDDIRrrvsaALDKV-GLLD---KAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1821109780 168 KQSIVVMQTIRNMaDELGKTILVVLHDINFAAAYSDNIIAMKDGKIcHSGTVDE 221
Cdd:PRK10908 171 ALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL-HGGVGGE 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-213 |
3.68e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKeiaiLKQQNtyqvkmtvrel 94
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ----LRREH----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 lsFGrFPYSK--------------------GRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTD 154
Cdd:PRK10535 88 --FG-FIFQRyhllshltaaqnvevpavyaGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 155 YILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAySDNIIAMKDGKI 213
Cdd:PRK10535 165 VILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-198 |
5.12e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwRTDELAKEIAILKQQNTYQVKMTVREL 94
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVFQNEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLTTEdyEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDM---KQsi 171
Cdd:PRK11248 91 VAFGLQLAGVEKMQRL--EIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftrEQ-- 166
|
170 180
....*....|....*....|....*...
gi 1821109780 172 vvMQT-IRNMADELGKTILVVLHDINFA 198
Cdd:PRK11248 167 --MQTlLLKLWQETGKQVLLITHDIEEA 192
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-213 |
6.49e-16 |
|
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: 73.24 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE-LAKEIAIL----KQQNTYQvKMT 90
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVpedrKREGLVL-DLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGRFpyskgrlttedyevidkvlgyldlesygdryldtLSGGQLQRAALAMILVQDTDYILLDEPLNNLDM--K 168
Cdd:cd03215 95 VAENIALSSL----------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVgaK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821109780 169 QSIvvMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:cd03215 141 AEI--YRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-222 |
6.90e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.74 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKS----TLLSTMCRLLSKDSGHVLIKGKEITkwrTDELAKEIAILKQQNTYQVKMT 90
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGRKIATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 91 VRELLSFGRFP-YSKGRLTTED--YEVIDKVlGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDM 167
Cdd:PRK10418 95 LHTMHTHARETcLALGKPADDAtlTAALEAV-GLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 168 KQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
15-213 |
1.27e-15 |
|
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: 73.22 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYqVKMTVREL 94
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTL-FSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LS-FGRfpYSKgrlttedyeviDKVLGYLDLESYGdrylDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVV 173
Cdd:cd03369 102 LDpFDE--YSD-----------EEIYGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1821109780 174 MQTIRNMADelGKTILVVLHDINFAAAYsDNIIAMKDGKI 213
Cdd:cd03369 165 QKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2-193 |
2.92e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 2 KVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMC-RLLSKD-SGHVLIKGKEITKwrtdELAKEIAIL 79
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK----QILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 KQQNTYQVKMTVRELLSFG---RFPYSKGRltTEDYEVIDKVLGYLDLES-----YGDRYLDTLSGGQLQRAALAMILVQ 151
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCsllRLPKSLTK--QEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLI 223
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1821109780 152 DTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLH 193
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-222 |
4.18e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 17 KDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITK-----WRtdELAKEIAILKQQ--NTYQVKM 89
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddeWR--AVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLSFGRFPYsKGRLTTEdyEVIDKVLGYLD----LESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:PRK15079 116 TIGEIIAEPLRTY-HPKLSRQ--EVKDRVKAMMLkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 166 DMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-221 |
5.24e-15 |
|
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: 74.09 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLstmcRLLSK----DSGHVLIKGKEITKWRTDELAKEIAILKQQ----NTyq 86
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLA----RLLFRfydvTSGRILIDGQDIRDVTQASLRAAIGIVPQDtvlfND-- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 87 vkmTVRELLSFgrfpyskGRLTTEDYEVIDKV-LGYLD--LESYGDRYlDT--------LSGGQLQRAALAMILVQDTDY 155
Cdd:COG5265 447 ---TIAYNIAY-------GRPDASEEEVEAAArAAQIHdfIESLPDGY-DTrvgerglkLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 156 ILLDEPLNNLDMK--QSIvvMQTIRNMADelGKTILVVLH---DInfaaAYSDNIIAMKDGKICHSGTVDE 221
Cdd:COG5265 516 LIFDEATSALDSRteRAI--QAALREVAR--GRTTLVIAHrlsTI----VDADEILVLEAGRIVERGTHAE 578
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-200 |
6.93e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 6.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRtDELAKEIAILKQQNTYQVKMTVRELLSF 97
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 98 grfpYSK--GRLTTED-YEVIDKV--LGYLDLEsygdryLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDmKQSIV 172
Cdd:PRK13538 98 ----YQRlhGPGDDEAlWEALAQVglAGFEDVP------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-KQGVA 166
|
170 180 190
....*....|....*....|....*....|.
gi 1821109780 173 VMQTIrnMADELGKTILVVL---HDINFAAA 200
Cdd:PRK13538 167 RLEAL--LAQHAEQGGMVILtthQDLPVASD 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-212 |
1.35e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 5 NLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEIT-KWRTDELAKEIAILKQQN 83
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 84 TYQVKMTVRELLSFGRFPySKGRLTTED--YEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:PRK10982 83 NLVLQRSVMDNMWLGRYP-TKGMFVDQDkmYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-222 |
1.43e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.11 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDEL--AKEIAI 78
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 79 LK------QQNTYQ-VKMTV-------RELLSFGRFPYSKGRLTTEDYevIDKVlgyldlESYGDRYLD---TLSGGQLQ 141
Cdd:PRK11701 87 LRtewgfvHQHPRDgLRMQVsaggnigERLMAVGARHYGDIRATAGDW--LERV------EIDAARIDDlptTFSGGMQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 142 RAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQ 238
|
.
gi 1821109780 222 V 222
Cdd:PRK11701 239 V 239
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-203 |
1.49e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.97 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRL-----LSKDSGHVLIKGKEITKWRTD--ELAKEIAILKQQnTYQVK 88
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQK-PNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFG-RFPYSKGRLTtedyEVIDKVLGYLDL-ESYGDRYLDT---LSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK14243 105 KSIYDNIAYGaRINGYKGDMD----ELVERSLRQAALwDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1821109780 164 NLDMKQSIVVMQTIRNMADELgkTILVVLHDINFAAAYSD 203
Cdd:PRK14243 181 ALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSD 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-219 |
2.13e-14 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 72.57 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRllSKDSGHVL--IKGKEITKwRTDELAKEIAILKQQNTYQVKMTVR 92
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdIRISGFPK-KQETFARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELL---SFGRFPYSKGRltTEDYEVIDKVLGYLDLESYGDRY-----LDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PLN03140 972 ESLiysAFLRLPKEVSK--EEKMMFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 165 LDMKQSIVVMQTIRNMADElGKTILVVLH--DINFAAAYSDNIIAMKDGKICHSGTV 219
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDT-GRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSGPL 1105
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
8-217 |
3.34e-14 |
|
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: 69.21 E-value: 3.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 8 KNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKD---SGHVLIKGKEItkwrtDELAK----EIAILK 80
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-----KEFAEkypgEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQNTYQVKMTVRELLSFGrfpyskgrlttedyevidkvlgyldLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:cd03233 90 EEDVHFPTLTVRETLDFA-------------------------LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINfAAAYS--DNIIAMKDGKICHSG 217
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAS-DEIYDlfDKVLVLYEGRQIYYG 202
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-223 |
4.61e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.31 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMC-RLLSKDSGHVLIKGKeitkwrtdelakeIAILKQQnTYQVKMTVREL 94
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLgELPPRSDASVVIRGT-------------VAYVPQV-SWIFNATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfPYSKGRLttedYEVID--------KVLGYLDLESYGDRYLDtLSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:PLN03130 699 ILFGS-PFDPERY----ERAIDvtalqhdlDLLPGGDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 167 MKQSIVVMQTIrnMADEL-GKTILVVLHDINFaAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PLN03130 773 AHVGRQVFDKC--IKDELrGKTRVLVTNQLHF-LSQVDRIILVHEGMIKEEGTYEELS 827
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-222 |
7.10e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 7.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSK-DSGHVLIKGKeitkwrtdelakeIAILKQQnTYQVKMTVREL 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGS-------------VAYVPQV-SWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFG-RFP---YSKGRLTTEDYEVIDKVLGYlDLESYGDRYLDtLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:PLN03232 699 ILFGsDFEserYWRAIDVTALQHDLDLLPGR-DLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVA 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 171 IVVMQTIrnMADEL-GKTILVVLHDINFAAAYsDNIIAMKDGKICHSGTVDEV 222
Cdd:PLN03232 777 HQVFDSC--MKDELkGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
126-206 |
9.49e-14 |
|
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: 67.21 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 126 SYGDRYLDtLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNI 205
Cdd:cd03222 64 VYKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI 142
|
.
gi 1821109780 206 I 206
Cdd:cd03222 143 H 143
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
18-222 |
1.12e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE-LAKE---IAILKQQNTYQVKMTVRE 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEkrrIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSFGRFPYSKGRLttedyeviDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVV 173
Cdd:PRK11144 96 NLRYGMAKSMVAQF--------DKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1821109780 174 MQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK11144 168 LPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-223 |
1.36e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.60 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkqqntYQVKM----TV 91
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV-----FQDAGlfnrSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRfPYSkgrlTTEDYEVIDKVLGYLD-LESYGDRYlDT--------LSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:PRK13657 426 EDNIRVGR-PDA----TDEEMRAAAERAQAHDfIERKPDGY-DTvvgergrqLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 163 NNLDMKQSIVVMQTIrnmaDEL--GKTILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PRK13657 500 SALDVETEAKVKAAL----DELmkGRTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDELV 557
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-244 |
1.59e-13 |
|
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: 69.45 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLStMCRLLSK---DSGHVL------------------- 58
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMDQyepTSGRIIyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 59 ---------IKGKEITKWRTDE-----LAKEIAILKQQN--TYQVKMTVRELLSfgrfpySKGRLTTEDYEVIDKVLGYL 122
Cdd:TIGR03269 80 epcpvcggtLEPEEVDFWNLSDklrrrIRKRIAIMLQRTfaLYGDDTVLDNVLE------ALEEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 123 DLESYGDRYLDT---LSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAA 199
Cdd:TIGR03269 154 EMVQLSHRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1821109780 200 AYSDNIIAMKDGKICHSGTVDEVIcSEHLKEVFDVDMEVEIIKGK 244
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVV-AVFMEGVSEVEKECEVEVGE 277
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
1.70e-13 |
|
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: 69.47 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDS--GHVLIKGKEITKWR-TDELAKEIA 77
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 78 ILKQQNTYQVKMTVRELLSFGRFPYSKGRLTTED--YEVIDKVLGYLDLESYGD-RYLDTLSGGQLQRAALAMILVQDTD 154
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPGGRMAYNamYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 155 YILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKicHSGTVD 220
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKD 224
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
16-219 |
2.17e-13 |
|
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: 67.28 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTL----------------LSTMCR--LLSKDSGHV-LIKGkeitkwrtdeLAKEI 76
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARqfLGQMDKPDVdSIEG----------LSPAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 77 AIlKQ----QNTYQVKMTVRELLSFGRFPYSKGRLTTEDYEVIDKVLGYLDLesygDRYLDTLSGGQLQRAALAMILVQD 152
Cdd:cd03270 81 AI-DQkttsRNPRSTVGTVTEIYDYLRLLFARVGIRERLGFLVDVGLGYLTL----SRSAPTLSGGEAQRIRLATQIGSG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 153 TDYIL--LDEPLNNLDMKQSIVVMQTIRNMADeLGKTILVVLHDINFAAAySDNIIAMKDGKICHSGTV 219
Cdd:cd03270 156 LTGVLyvLDEPSIGLHPRDNDRLIETLKRLRD-LGNTVLVVEHDEDTIRA-ADHVIDIGPGAGVHGGEI 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-190 |
2.78e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEitkwrtdelakEIAILKQQnTYQVKMTVREL 94
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RVLFLPQR-PYLPLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFgrfPYSKGRLTTEDY-EVIDKV-LGYL----DLEsygDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK 168
Cdd:COG4178 446 LLY---PATAEAFSDAELrEALEAVgLGHLaerlDEE---ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180
....*....|....*....|..
gi 1821109780 169 QSIVVMQTIRnmaDELGKTILV 190
Cdd:COG4178 520 NEAALYQLLR---EELPGTTVI 538
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
6.17e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDS-----GHVLIKGKEITKWRT--DELA 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVnlNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 74 KEIAIL-KQQNTYqvKMTVRELLSFG-RFPYSKGRLTTEDyeVIDKVLGYLDL-----ESYGDRYLDtLSGGQLQRAALA 146
Cdd:PRK14258 88 RQVSMVhPKPNLF--PMSVYDNVAYGvKIVGWRPKLEIDD--IVESALKDADLwdeikHKIHKSALD-LSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 147 MILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDI-------NFAAAYSDNiiAMKDGKICHSGTV 219
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLhqvsrlsDFTAFFKGN--ENRIGQLVEFGLT 240
|
....*...
gi 1821109780 220 DEVICSEH 227
Cdd:PRK14258 241 KKIFNSPH 248
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-220 |
1.12e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKD--SGHVLIKGKEITKWRTDELAKEIAI 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 79 LKQQntYQVKMTVRELLSFGRFPYSKGR----LTTED----YEVIDKVLGYLDL-ESYGDRYL-DTLSGGQLQR-AALAM 147
Cdd:CHL00131 88 LAFQ--YPIEIPGVSNADFLRLAYNSKRkfqgLPELDplefLEIINEKLKLVGMdPSFLSRNVnEGFSGGEKKRnEILQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 148 ILVqDTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHdinfaaaYS--------DNIIAMKDGKICHSGTV 219
Cdd:CHL00131 166 ALL-DSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH-------YQrlldyikpDYVHVMQNGKIIKTGDA 236
|
.
gi 1821109780 220 D 220
Cdd:CHL00131 237 E 237
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
15-213 |
1.58e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwRTDELAKeiAILKQQN---TYQVKMTV 91
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLH--QMDEEAR--AKLRAKHvgfVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 REL--LSFGRFP-YSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK 168
Cdd:PRK10584 101 PTLnaLENVELPaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821109780 169 QSIVVMQTIRNMADELGKTILVVLHDINFAAAySDNIIAMKDGKI 213
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-167 |
1.71e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.48 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITkwrTDELAKEIAILKQQNTYQVKMTV 91
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT---RGDRSRFMAYLGHLPGLKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSF-----GRFPyskgrlttedYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:PRK13543 100 LENLHFlcglhGRRA----------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
.
gi 1821109780 167 M 167
Cdd:PRK13543 170 L 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-221 |
1.83e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWrTDELAKEIAI-- 78
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-TPAKAHQLGIyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 79 LKQQNTYQVKMTVRELLSFGrfpYSKGRLTTEDYEVIDKVLG-YLDLESygdryldtlSGGQLQRAALAMI-----LVQD 152
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG---LPKRQASMQKMKQLLAALGcQLDLDS---------SAGSLEVADRQIVeilrgLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 153 TDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDE 221
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-220 |
3.16e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDS--GHVLIKGKEItKWRT--DELAKEIAILKQQNTYQVKMTV 91
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEEL-QASNirDTERAGIAIIHQELALVKELSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLSFGRFPYSKGRLtteDYEVI----DKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDM 167
Cdd:PRK13549 100 LENIFLGNEITPGGIM---DYDAMylraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 168 KQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKicHSGTVD 220
Cdd:PRK13549 177 SETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR--HIGTRP 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-222 |
3.46e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKD---SGHVLIKGKEITKWRTDEL----AKEIAILKQQ-----NTY 85
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELnklrAEQISMIFQDpmtslNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 86 -QVKMTVRELLSFgrfpySKGRLTTEDYEVIDKVLGYLDLESYGDR---YLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:PRK09473 114 mRVGEQLMEVLML-----HKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-222 |
4.37e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLStmcrLLSK----DSGHVLIKGKEIT--KWRtDELAKEIAILKQ---QN 83
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLS----LIAGarkiQQGRVEVLGGDMAdaRHR-RAVCPRIAYMPQglgKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 84 TYQvKMTVRELLSFgrFpyskGRL----TTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:NF033858 89 LYP-TLSVFENLDF--F----GRLfgqdAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 160 EPLNNLD---MKQSIVVMQTIRnmADELGKTILVvlhdinfAAAYS------DNIIAMKDGKICHSGTVDEV 222
Cdd:NF033858 162 EPTTGVDplsRRQFWELIDRIR--AERPGMSVLV-------ATAYMeeaerfDWLVAMDAGRVLATGTPAEL 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-193 |
4.80e-12 |
|
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: 62.17 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEitkwrtdelakEIAILKQQnTYQVKMTVR 92
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLLFLPQR-PYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFgrfPYSkgrlttedyevidkvlgyldlesygdrylDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIV 172
Cdd:cd03223 82 EQLIY---PWD-----------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|.
gi 1821109780 173 VMQTIRnmadELGKTILVVLH 193
Cdd:cd03223 130 LYQLLK----ELGITVISVGH 146
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-226 |
5.33e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRL--------------------------------------------- 49
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 50 ---------LSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYqVKMTVRELLSFGrfpysKGRLTTEDYEVIDKvLG 120
Cdd:PTZ00265 1263 eggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFG-----KEDATREDVKRACK-FA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 121 YLD--LESYGDRYlDT--------LSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILV 190
Cdd:PTZ00265 1336 AIDefIESLPNKY-DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1821109780 191 VLHDINfAAAYSDNIIAM----KDGKICHS-GTVDEVICSE 226
Cdd:PTZ00265 1415 IAHRIA-SIKRSDKIVVFnnpdRTGSFVQAhGTHEELLSVQ 1454
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-214 |
8.15e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLlstmCRLLS----KDSGHVLIKGKEITkwrtdelakeiaiLKQQNTYqvkmtv 91
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTL----AMLLTglyqPQSGEILLDGKPVT-------------AEQPEDY------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 92 RELLS--------FGRFPYSKGrlTTEDYEVIDKVLGYLDLESY----GDRYLDT-LSGGQLQRAALAMILVQDTDYILL 158
Cdd:PRK10522 396 RKLFSavftdfhlFDQLLGPEG--KPANPALVEKWLERLKMAHKleleDGRISNLkLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDIN-FAAAysDNIIAMKDGKIC 214
Cdd:PRK10522 474 DEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHyFIHA--DRLLEMRNGQLS 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-217 |
1.01e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.41 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTmcrLLSKdsghvlikgKEITKWRTdELAKEIAILKQQnTYQVKMTVREL 94
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQS---LLSQ---------FEISEGRV-WAERSIAYVPQQ-AWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFgrfpyskgrLTTEDYEVIDKVLGYLDLES------------YGDRYLDtLSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:PTZ00243 741 ILF---------FDEEDAARLADAVRVSQLEAdlaqlgggleteIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 163 NNLDMKQSIVVMQTIRnMADELGKTILVVLHDINFaAAYSDNIIAMKDGKICHSG 217
Cdd:PTZ00243 811 SALDAHVGERVVEECF-LGALAGKTRVLATHQVHV-VPRADYVVALGDGRVEFSG 863
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-223 |
1.01e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITK------WRT-------DELA-------- 73
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdinlkwWRSkigvvsqDPLLfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 74 --------KEIAILKQQ---------------NTYQVKMT------VRELLSFGRFPYSKGRLTTEDYEVID---KVLGY 121
Cdd:PTZ00265 480 ikyslyslKDLEALSNYynedgndsqenknkrNSCRAKCAgdlndmSNTTDSNELIEMRKNYQTIKDSEVVDvskKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 122 LDLESYGDRYlDTL--------SGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLH 193
Cdd:PTZ00265 560 DFVSALPDKY-ETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
250 260 270
....*....|....*....|....*....|
gi 1821109780 194 DINfAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PTZ00265 639 RLS-TIRYANTIFVLSNRERGSTVDVDIIG 667
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-197 |
1.58e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLlSKDSGHVLIKGKEITkwrtdelakeIAILKQQNTYQVKMTVREL 94
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKDFNGEARPQPGIK----------VGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFG---------RFPYSKGRLTTEDY-------------EVIDKVLGYlDLESYGDRYLD------------TLSGGQL 140
Cdd:TIGR03719 89 VEEGvaeikdaldRFNEISAKYAEPDAdfdklaaeqaelqEIIDAADAW-DLDSQLEIAMDalrcppwdadvtKLSGGER 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 141 QRAALAMILVQDTDYILLDEPLNNLDmKQSIVVMQtiRNMADELGkTILVVLHDINF 197
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPG-TVVAVTHDRYF 220
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
15-195 |
1.84e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTdELAKEIAILKQQNTYQVKMTVREL 94
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC-TYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGrFPYSKGRLTtedyevIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVM 174
Cdd:PRK13540 95 CLYD-IHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170 180
....*....|....*....|.
gi 1821109780 175 QTIRNMADELGKTILVVLHDI 195
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQDL 188
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-211 |
3.26e-11 |
|
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: 61.30 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIK--GKEItkwrtdELAK----EIAILKQQ------- 82
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWV------DLAQasprEILALRRRtigyvsq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 --------NTYQVkmtVRE-LLSFGrfpyskgrltTEDYEVIDKV---LGYLDL-ESYGDRYLDTLSGGQLQRAALAMIL 149
Cdd:COG4778 101 flrviprvSALDV---VAEpLLERG----------VDREEARARArelLARLNLpERLWDLPPATFSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 150 VQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDG 211
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
16-213 |
3.81e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEItKWRT--DELAKEIAIL----KQQNTYQvKM 89
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV-RIRSprDAIRAGIAYVpedrKGEGLVL-DL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRE---------LLSFGRFPYSKGRLTTEDYevIDKvlgyLDLE-SYGDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:COG1129 346 SIREnitlasldrLSRGGLLDRRRERALAEEY--IKR----LRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 160 EPLNNLDM--KQSIvvMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:COG1129 420 EPTRGIDVgaKAEI--YRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-213 |
6.23e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 6.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwrtdelaKEIAILKQQNTYQVKMTVREL 94
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-----------VRMAVFSQHHVDGLDLSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGR----FPYSKGRLTTEDYevidKVLGYLDLESygdryLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK-- 168
Cdd:PLN03073 593 LYMMRcfpgVPEQKLRAHLGSF----GVTGNLALQP-----MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDav 663
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1821109780 169 ----QSIVVMQtirnmadelgKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:PLN03073 664 ealiQGLVLFQ----------GGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-197 |
7.57e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 7.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVlikgKEITKWrtdelakEIAILKQq 82
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKL-------EVAYFDQ- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 ntYQVKM----TVRELLSFGRfpyskgrlttEDYEVIDK---VLGYL-DLESYGDRYL---DTLSGGQLQRAALAMILVQ 151
Cdd:PRK11147 390 --HRAELdpekTVMDNLAEGK----------QEVMVNGRprhVLGYLqDFLFHPKRAMtpvKALSGGERNRLLLARLFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1821109780 152 DTDYILLDEPLNNLDmkqsIVVMQTIRNMADELGKTILVVLHDINF 197
Cdd:PRK11147 458 PSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-212 |
1.26e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEIT-KWRTDELAKEIAILKQQNTYQVKMTVREL 94
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSK-GRLT-TEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIV 172
Cdd:PRK10762 100 IFLGREFVNRfGRIDwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETES 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1821109780 173 VMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:PRK10762 180 LFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-223 |
1.79e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKMTVREL 94
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGRLTTEDYEVIDKVLGY---LDLE-SYGDrylDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQS 170
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALpdkLDHEcAEGG---ENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 171 IVVMQTIRNMADELgkTILVVLHDINFAAAYSdNIIAMKDGKICHSGTVDEVI 223
Cdd:TIGR00957 1458 NLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-225 |
2.67e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 59.03 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEIT----KWRTdelaKEIAILKQ--QNTYQVKM 89
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRS----QRIRMIFQdpSTSLNPRQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLSFgrfPYskgRLTTE---------DYEVIDKVLGYLDLESYgdrYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:PRK15112 105 RISQILDF---PL---RLNTDlepeqrekqIIETLRQVGLLPDHASY---YPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1821109780 161 PLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICS 225
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-212 |
2.96e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKS-TLLSTMcRLLSKD-----SGHVLIKGKEITKWRTDEL----AKEIAILKQ 81
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPpvvypSGDIRFHGESLLHASEQTLrgvrGNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNT------YQVKMTVRELLSFGRfpyskG-RLTTEDYEVIDKvlgyldLESYGDR--------YLDTLSGGQLQRAALA 146
Cdd:PRK15134 100 EPMvslnplHTLEKQLYEVLSLHR-----GmRREAARGEILNC------LDRVGIRqaakrltdYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 147 MILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGK 212
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-222 |
4.55e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKS-TLLSTMcRLLSKDSGHVLiKGKEITKWRTdelaKEIAILKQQNTYQVK------ 88
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQ-CDKMLLRRRS----RQVIELSEQSAAQMRhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 --MTVRELLSFGRFPYSKGRLTTEDY---------EVIDKVLGYLDL------ESYGDRYLDTLSGGQLQRAALAMILVQ 151
Cdd:PRK10261 106 maMIFQEPMTSLNPVFTVGEQIAESIrlhqgasreEAMVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 152 DTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-194 |
7.44e-10 |
|
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: 58.79 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIkGKEItkwrtdelakEIAILK 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQ-NTYQVKMTVRELLSFGrfpyskgrlttedYEVIDkvLGYLDLES--YGDRY----------LDTLSGGQLQRAALAM 147
Cdd:TIGR03719 392 QSrDALDPNKTVWEEISGG-------------LDIIK--LGKREIPSraYVGRFnfkgsdqqkkVGQLSGGERNRVHLAK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1821109780 148 ILVQDTDYILLDEPLNNLDmkqsIVVMQTIRNMADELGKTILVVLHD 194
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD 499
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
50-227 |
9.30e-10 |
|
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: 58.49 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 50 LSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKMTV-----RELLSfgrfpyskgRLTTedyeVIDKVLGYLDL 124
Cdd:TIGR00630 416 LKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTPEEKKIaeevlKEIRE---------RLGF----LIDVGLDYLSL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 125 EsygdRYLDTLSGGQLQRAALA------MILVQdtdYIlLDEPLNNLDMKQSIVVMQTIRNMADeLGKTILVVLHDINfA 198
Cdd:TIGR00630 483 S----RAAGTLSGGEAQRIRLAtqigsgLTGVL---YV-LDEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEHDED-T 552
|
170 180 190
....*....|....*....|....*....|....*
gi 1821109780 199 AAYSDNIIAM------KDGKICHSGTVDEVICSEH 227
Cdd:TIGR00630 553 IRAADYVIDIgpgageHGGEVVASGTPEEILANPD 587
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
50-223 |
9.33e-10 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 58.50 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 50 LSKDSGHVLIKGKEITkwrtdELakeiailkqqntyqVKMTVRELLSFgrfpYSKGRLTTEDYEVIDKV----------- 118
Cdd:COG0178 413 LKPEALAVKIGGKNIA-----EL--------------TALSIDEALEF----FENLELTEREAEIAERIlkeirsrlgfl 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 119 ----LGYLDLesygDRYLDTLSGGQLQRAALA----MILVqDTDYIlLDEPLNNL---DMKQSIvvmQTIRNMADeLGKT 187
Cdd:COG0178 470 vdvgLDYLTL----DRSAGTLSGGEAQRIRLAtqigSGLV-GVLYV-LDEPSIGLhqrDNDRLI---ETLKRLRD-LGNT 539
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821109780 188 ILVVLHD---InfAAAysDNIIAM------KDGKICHSGTVDEVI 223
Cdd:COG0178 540 VIVVEHDedtI--RAA--DYIIDIgpgageHGGEVVAQGTPEEIL 580
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-220 |
9.99e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELA------------KEIAILKqqn 83
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrlgvayipedrlGRGLVPD--- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 84 tyqvkMTVRE---LLSFGRFPYSKGRLttEDYEVIDKVLGYLdLESYG------DRYLDTLSGGQLQRAALAMILVQDTD 154
Cdd:COG3845 351 -----MSVAEnliLGRYRRPPFSRGGF--LDRKAIRAFAEEL-IEEFDvrtpgpDTPARSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 155 YILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKIchSGTVD 220
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI--VGEVP 485
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-232 |
1.26e-09 |
|
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: 58.49 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 26 GTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwRTDELAKEIAILKQQNTYQVKMTVRELLsfgrfpYSKG 105
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGREHL------YLYA 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 106 RLTTEDYEVIDKVLGY----LDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMA 181
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWsiqsLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 182 DElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVdevicsEHLKEVF 232
Cdd:TIGR01257 2118 RE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI------QHLKSKF 2161
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-237 |
1.76e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 12 ETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHV-LIKG--------KEITKWRTDELA-KEIAILKQ 81
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGiklgyfaqHQLEFLRADESPlQHLARLAP 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 82 QNTYQvkmTVRELLsfGRFPYsKGRLTTEDYEvidkvlgyldlesygdRYldtlSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:PRK10636 404 QELEQ---KLRDYL--GGFGF-QGDKVTEETR----------------RF----SGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 162 LN--NLDMKQSIVvmqtiRNMADELGkTILVVLHDINFAAAYSDNIIAMKDGKIchsgtvdevicsehlkEVFDVDME 237
Cdd:PRK10636 458 TNhlDLDMRQALT-----EALIDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV----------------EPFDGDLE 513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
15-181 |
2.06e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEItkwrtdelakeIAILKQQNTYQVKMTVREL 94
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI-----------VARLQQDPPRNVEGTVYDF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFG---------RFpYSKGRLTTEDY------------EVID------------KVLGYLDLEsyGDRYLDTLSGGQLQ 141
Cdd:PRK11147 87 VAEGieeqaeylkRY-HDISHLVETDPseknlnelaklqEQLDhhnlwqlenrinEVLAQLGLD--PDAALSSLSGGWLR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 142 RAALAMILVQDTDYILLDEPLNNLDM-------------KQSIVVMQT----IRNMA 181
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIetiewlegflktfQGSIIFISHdrsfIRNMA 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-167 |
2.51e-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: 57.23 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 13 TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeITkwrtdelakeiaiLKQQNTYQVKMTVR 92
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-IS-------------FSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFGrFPYSKGRLTT--------EDYEVI---DK-VLGYLDLesygdryldTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:TIGR01271 505 DNIIFG-LSYDEYRYTSvikacqleEDIALFpekDKtVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDS 574
|
....*..
gi 1821109780 161 PLNNLDM 167
Cdd:TIGR01271 575 PFTHLDV 581
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-226 |
3.70e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 32 IGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYqVKMTVRellsFGRFPYSKG------ 105
Cdd:PLN03232 1268 VGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL-FSGTVR----FNIDPFSEHndadlw 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 106 ----RLTTEDyeVIDKVLGYLDLESY--GDRYldtlSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRn 179
Cdd:PLN03232 1343 ealeRAHIKD--VIDRNPFGLDAEVSegGENF----SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR- 1415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 180 maDELGK-TILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVICSE 226
Cdd:PLN03232 1416 --EEFKScTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-218 |
4.51e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 56.26 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILkQQNTYQVKMTVREL 94
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV-QQDPVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRfPYSKGRL--TTEDYEVIDKVLGYLD-LESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSI 171
Cdd:PRK10790 435 VTLGR-DISEEQVwqALETVQLAELARSLPDgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1821109780 172 VVMQTIRNMADElgKTILVVLHDINfAAAYSDNIIAMKDGKICHSGT 218
Cdd:PRK10790 514 AIQQALAAVREH--TTLVVIAHRLS-TIVEADTILVLHRGQAVEQGT 557
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-222 |
9.16e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLlstmCRLLS----KDSGHVLIKGKEITKWRTDELA---KEIAILKQqNTY--- 85
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTmietPTGGELYYQGQDLLKADPEAQKllrQKIQIVFQ-NPYgsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 86 ----QVKMTVRELLSFGRfPYSKGRLTTEDYEVIDKVlGyLDLESYgDRYLDTLSGGQLQRAALAMILVQDTDYILLDEP 161
Cdd:PRK11308 106 nprkKVGQILEEPLLINT-SLSAAERREKALAMMAKV-G-LRPEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 162 LNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-178 |
1.15e-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: 55.30 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICE--TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDsGHVLIKGKE-----ITKWRtdela 73
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSwnsvtLQTWR----- 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 74 KEIAILKQQnTYQVKMTVRELLSfgrfPYSK------GRLTTED--YEVIDKVLGYLDLESYGDRYLdtLSGGQLQRAAL 145
Cdd:TIGR01271 1292 KAFGVIPQK-VFIFSGTFRKNLD----PYEQwsdeeiWKVAEEVglKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCL 1364
|
170 180 190
....*....|....*....|....*....|...
gi 1821109780 146 AMILVQDTDYILLDEPLNNLDMkqsiVVMQTIR 178
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDP----VTLQIIR 1393
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-217 |
1.19e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMC--RLLSKDSGHVLIKGKEITKWRTDELAKEIAI 78
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 79 LKQQ---------NTYQVKMTVRELLSFgRFPYSKGRLTTEDYevIDKVLGYLDL-ESYGDRYLDT-LSGGQLQRAALAM 147
Cdd:PRK09580 82 MAFQypveipgvsNQFFLQTALNAVRSY-RGQEPLDRFDFQDL--MEEKIALLKMpEDLLTRSVNVgFSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 148 ILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
114-222 |
1.23e-08 |
|
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: 53.10 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 114 VIDKVLGYLDLesygDRYLDTLSGGQLQRAALAMILVQDTDYIL--LDEPLNNLDMKQSIVVMQTIRNMADeLGKTILVV 191
Cdd:cd03238 71 LIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDINQLLEVIKGLID-LGNTVILI 145
|
90 100 110
....*....|....*....|....*....|.
gi 1821109780 192 LHDINFaAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:cd03238 146 EHNLDV-LSSADWIIDFGPGSGKSGGKVVFS 175
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-213 |
1.51e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 17 KDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEIT-KWRTDELAKEIAIL---KQQNTYQVKMTVR 92
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYItesRRDNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFGRFpYSKGRL--------TTEDYEVIDKVLGYLDLESYG-DRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLN 163
Cdd:PRK09700 360 QNMAISRS-LKDGGYkgamglfhEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1821109780 164 NLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
104-206 |
1.72e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.83 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 104 KGRLTTedyeVIDKVLGYLDLEsygdRYLDTLSGGQLQRAALAMIL---VQDTDYIlLDEPLNNLDMKQSIVVMQTIRNM 180
Cdd:PRK00635 454 KSRLSI----LIDLGLPYLTPE----RALATLSGGEQERTALAKHLgaeLIGITYI-LDEPSIGLHPQDTHKLINVIKKL 524
|
90 100
....*....|....*....|....*....
gi 1821109780 181 ADElGKTILVVLHD---INFAaaysDNII 206
Cdd:PRK00635 525 RDQ-GNTVLLVEHDeqmISLA----DRII 548
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-222 |
5.48e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 19 INLELEQGTVTAFIGPNGAGKS-TLLSTMCRL-----LSKDS----GHVLIKGKEitKWRTDELAKEIAILKQ------Q 82
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIdypgrVMAEKlefnGQDLQRISE--KERRNLVGAEVAMIFQdpmtslN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 NTYQVKMTVRELLSFgrfpYSKGRLTTEDYEVID--KVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDE 160
Cdd:PRK11022 104 PCYTVGFQIMEAIKV----HQGGNKKTRRQRAIDllNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1821109780 161 PLNNLDMK-QSIVV-----MQTIRNMAdelgktILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK11022 180 PTTALDVTiQAQIIellleLQQKENMA------LVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-167 |
9.94e-08 |
|
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: 51.78 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwrtdelakeiAILKQQNTYQVKMTVREL 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGrfpyskgrLTTEDYE---VIDKVLGYLDLESYGDRylD---------TLSGGQLQRAALAMILVQDTDYILLDEPL 162
Cdd:cd03291 118 IIFG--------VSYDEYRyksVVKACQLEEDITKFPEK--DntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
....*
gi 1821109780 163 NNLDM 167
Cdd:cd03291 188 GYLDV 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-214 |
1.47e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNIcetciLKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEI-TKWRTDELAKEIAIL 79
Cdd:PRK10762 258 LKVDNLSGPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 80 ---KQQNTYQVKMTVRE---LLSFGRFPYSKGRLTTED-YEVIDKVLGYLDLESYG-DRYLDTLSGGQLQRAALAMILVQ 151
Cdd:PRK10762 333 sedRKRDGLVLGMSVKEnmsLTALRYFSRAGGSLKHADeQQAVSDFIRLFNIKTPSmEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 152 DTDYILLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKIC 214
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-213 |
1.96e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 19 INLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEItKWRTDELAKEIAIL------KQQNTYQVKmTVR 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAIRAGIMlcpedrKAEGIIPVH-SVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 93 ELLSFG-RFPYSKGRL----TTEDyEVIDKVLGYLDLES-YGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:PRK11288 350 DNINISaRRHHLRAGClinnRWEA-ENADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1821109780 167 M--KQSIvvMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:PRK11288 429 VgaKHEI--YNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-178 |
2.87e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 50.24 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICE--TCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDsGHVLIKGKE-----ITKWRtdela 73
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSwnsvpLQKWR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 74 KEIAILKQQnTYQVKMTVRELLSfgrfPYSKG------RLTTED--YEVIDKVLGYLDLESYGDRYLdtLSGGQLQRAAL 145
Cdd:cd03289 77 KAFGVIPQK-VFIFSGTFRKNLD----PYGKWsdeeiwKVAEEVglKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCL 149
|
170 180 190
....*....|....*....|....*....|...
gi 1821109780 146 AMILVQDTDYILLDEPLNNLDMKQSIVVMQTIR 178
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK 182
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
21-195 |
4.59e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.85 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 21 LELEQGtVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQVKmtvRELLSFGRF 100
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEHGGKRYRIE---RRQGEFAEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 101 PYSKGR---------LTTEDYEVIDKVLGYL------------DLESYGDRYL---------DTLSGGQLQRAALAMILV 150
Cdd:COG0419 95 LEAKPSerkealkrlLGLEIYEELKERLKELeealesaleelaELQKLKQEILaqlsgldpiETLSGGERLRLALADLLS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1821109780 151 qdtdyILLDepLNNLDmkqsivvMQTIRNMADELgKTILVVLHDI 195
Cdd:COG0419 175 -----LILD--FGSLD-------EERLERLLDAL-EELAIITHVI 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-222 |
7.72e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 1 MKVNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLlSTMCRLLSKDSGHvliKGKEITKWRTDELAKEIAILK 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 81 QQntyQVKMTVRELLSFGRFPYSKGR---LTTEDYEV-IDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYI 156
Cdd:NF000106 90 HR---PVR*GRRESFSGRENLYMIGR*ldLSRKDARArADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 157 LLDEPLNNLDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
15-166 |
8.95e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLlskDsghvlikgKEIT-KWRTDELAKeIAILKQQNTYQVKMTVRE 93
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---D--------KEFEgEARPAPGIK-VGYLPQEPQLDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSFG---------RFPYSKGRLTTEDY-------------EVIDKVLGYlDLESY------------GDRYLDTLSGGQ 139
Cdd:PRK11819 90 NVEEGvaevkaaldRFNEIYAAYAEPDAdfdalaaeqgelqEIIDAADAW-DLDSQleiamdalrcppWDAKVTKLSGGE 168
|
170 180
....*....|....*....|....*..
gi 1821109780 140 LQRAALAMILVQDTDYILLDEPLNNLD 166
Cdd:PRK11819 169 RRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-216 |
1.08e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.89 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 17 KDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRT-DELAKEIAIL---KQQN--------T 84
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLARGLVYLpedRQSSglyldaplA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 85 YQVKMTVRELLSFGRFPySKGRLTTEDYEvidKVLGyLDLeSYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:PRK15439 360 WNVCALTHNRRGFWIKP-ARENAVLERYR---RALN-IKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 165 LDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHS 216
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGA 484
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-222 |
1.16e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTmcrLLSKDSGHVLIKGKEIT--KWRTDELAK----EIAILKQQNTYQVK 88
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKT---IASNTDGFHIGVEGVITydGITPEEIKKhyrgDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSFG---RFPYSKGR-LTTEDY--EVIDKVLGYLDLE-----SYGDRYLDTLSGGQLQRAALAMILVQDTDYIL 157
Cdd:TIGR00956 153 LTVGETLDFAarcKTPQNRPDgVSREEYakHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 158 LDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINfAAAYS--DNIIAMKDGKICHSGTVDEV 222
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCS-QDAYElfDKVIVLYEGYQIYFGPADKA 298
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-237 |
1.32e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwrtdelAKEIAILKQQNTYQVKMTVREL- 94
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS----------AALIAISSGLNGQLTGIENIELk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 -LSFGrfpyskgrLTTEDY-EVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIV 172
Cdd:PRK13545 110 gLMMG--------LTKEKIkEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1821109780 173 VMQTIrNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVIC--SEHLKEVFDVDME 237
Cdd:PRK13545 182 CLDKM-NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDhyDEFLKKYNQMSVE 247
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
25-211 |
1.35e-06 |
|
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: 46.98 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 25 QGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIailkqqntyqvkmtvrellsfgrfpysk 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLI---------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 105 grlttedyevidkvlgyldlesYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIR-----N 179
Cdd:smart00382 53 ----------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllL 110
|
170 180 190
....*....|....*....|....*....|....*..
gi 1821109780 180 MADELGKTILVVLHDINF-----AAAYSDNIIAMKDG 211
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLI 147
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-217 |
1.44e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKdSGHVLIKGKEITKWRTDEL---AKEIAILKQ--QNTYQVKM 89
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 90 TVRELLSFGRFPYSKgRLTTEDYE--VIDKV--LGyLDLESYgDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL 165
Cdd:PRK15134 380 NVLQIIEEGLRVHQP-TLSAAQREqqVIAVMeeVG-LDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1821109780 166 DMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-197 |
1.67e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 32 IGPNGAGKSTLLSTMCRLLSKDSGHVLI-KGKEITKWRTDELAKE------IAILKQQNTYQVKmTVRELLsfgrfpYSK 104
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLGKLRQDQFAFEeftvldTVIMGHTELWEVK-QERDRI------YAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 105 GRLTTEDYEvidKVLgylDLES-YG--DRYLDTLSGGQLQ-----------------------RAALAMILVQDTDYILL 158
Cdd:PRK15064 106 PEMSEEDGM---KVA---DLEVkFAemDGYTAEARAGELLlgvgipeeqhyglmsevapgwklRVLLAQALFSNPDILLL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1821109780 159 DEPLNNLDmkqsivvMQTIRNMADELGK---TILVVLHDINF 197
Cdd:PRK15064 180 DEPTNNLD-------INTIRWLEDVLNErnsTMIIISHDRHF 214
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-200 |
2.12e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 28 VTAFIGPNGAGKSTLL-----STMCRL-LSKDSGHVLIKgkeitkwrtdelakeiAILKQQNTYQVKMTVREllsfgrfp 101
Cdd:cd03240 24 LTLIVGQNGAGKTTIIealkyALTGELpPNSKGGAHDPK----------------LIREGEVRAQVKLAFEN-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 102 YSKGRLT-TEDYEVIDKVLgYL---DLESYGDRYLDTLSGGQ------LQRAALAMILVQDTDYILLDEPLNNLD---MK 168
Cdd:cd03240 80 ANGKKYTiTRSLAILENVI-FChqgESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDeenIE 158
|
170 180 190
....*....|....*....|....*....|..
gi 1821109780 169 QSIVvmQTIRNMADELGKTILVVLHDINFAAA 200
Cdd:cd03240 159 ESLA--EIIEERKSQKNFQLIVITHDEELVDA 188
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
5-223 |
2.38e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 5 NLCKNICETC---------------ILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKD---SGHVLIKGkeitk 66
Cdd:PLN03140 155 NAARNIAESAlgmlginlakktkltILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG----- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 67 WRTDELA--KEIAILKQQNTYQVKMTVRELLSF------------------------GRFPYS--------------KGR 106
Cdd:PLN03140 230 YRLNEFVprKTSAYISQNDVHVGVMTVKETLDFsarcqgvgtrydllselarrekdaGIFPEAevdlfmkatamegvKSS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 107 LTTeDYEVidKVLGyLDL---ESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMK---QSIVVMQTIRNM 180
Cdd:PLN03140 310 LIT-DYTL--KILG-LDIckdTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSttyQIVKCLQQIVHL 385
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1821109780 181 ADelgKTILV-VLHDINFAAAYSDNIIAMKDGKICHSGTVDEVI 223
Cdd:PLN03140 386 TE---ATVLMsLLQPAPETFDLFDDIILLSEGQIVYQGPRDHIL 426
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
89-223 |
2.41e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 89 MTVRELLSF-GRFPYSKGRLTTedyeVIDKVLGYLDLesygDRYLDTLSGGQLQRAALAMILVQ----DTDYIlLDEPLN 163
Cdd:TIGR00630 791 MTVEEAYEFfEAVPSISRKLQT----LCDVGLGYIRL----GQPATTLSGGEAQRIKLAKELSKrstgRTLYI-LDEPTT 861
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1821109780 164 NL---DMKQSIVVMQTIRnmadELGKTILVVLHDINFAAAySDNII------AMKDGKICHSGTVDEVI 223
Cdd:TIGR00630 862 GLhfdDIKKLLEVLQRLV----DKGNTVVVIEHNLDVIKT-ADYIIdlgpegGDGGGTVVASGTPEEVA 925
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-227 |
2.59e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 32 IGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYqVKMTVRellsFGRFPYSKG------ 105
Cdd:PLN03130 1271 VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVL-FSGTVR----FNLDPFNEHndadlw 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 106 ----RLTTEDyeVIDKVLGYLDLE-SYGDrylDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRnm 180
Cdd:PLN03130 1346 esleRAHLKD--VIRRNSLGLDAEvSEAG---ENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR-- 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 181 aDELGK-TILVVLHDINfAAAYSDNIIAMKDGKICHSGTVDEVICSEH 227
Cdd:PLN03130 1419 -EEFKScTMLIIAHRLN-TIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-176 |
2.59e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKwrtdeLAKE-IAILKQQNTYQVKMTVREL 94
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-----IAKPyCTYIGHNLGLKLEMTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 95 LSFGRFPYSKGrlttedyEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNL-----DMKQ 169
Cdd:PRK13541 91 LKFWSEIYNSA-------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLskenrDLLN 163
|
....*..
gi 1821109780 170 SIVVMQT 176
Cdd:PRK13541 164 NLIVMKA 170
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-217 |
4.26e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKeitkwRTDELAkeiailkqqnTYQVKMTVRELL 95
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQ-----RIDTLS----------PGKLQALRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 96 SFGRFPYSK--GRLTTeDYEVID--KVLGYLD-----------LESYGD------RYLDTLSGGQLQRAALAMILVQDTD 154
Cdd:PRK10261 405 FIFQDPYASldPRQTV-GDSIMEplRVHGLLPgkaaaarvawlLERVGLlpehawRYPHEFSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1821109780 155 YILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSG 217
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-166 |
5.79e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 3 VNNLCKNICETCILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIkGKEItkwrtdelakEIAILKQQ 82
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 83 -NTYQVKMTVRELLSFGrfpyskgrlttedYEVIDkvLGYLDLES--Y--------GD--RYLDTLSGGQLQRAALAMIL 149
Cdd:PRK11819 396 rDALDPNKTVWEEISGG-------------LDIIK--VGNREIPSraYvgrfnfkgGDqqKKVGVLSGGERNRLHLAKTL 460
|
170
....*....|....*..
gi 1821109780 150 VQDTDYILLDEPLNNLD 166
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLD 477
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-166 |
6.15e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLELEQGTVTAFIGPNGAGKSTLLStmcrLLSKD-----SGHVLIKGKEI----TKWrtdELAKEIAILKQQ--N 83
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITGDhpqgySNDLTLFGRRRgsgeTIW---DIKKHIGYVSSSlhL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 84 TYQVKMTVRELLSFGRFPySKGRlttedYE-VID----KVLGYLDLESYGDRYLD----TLSGGQlQRAAL-AMILVQDT 153
Cdd:PRK10938 348 DYRVSTSVRNVILSGFFD-SIGI-----YQaVSDrqqkLAQQWLDILGIDKRTADapfhSLSWGQ-QRLALiVRALVKHP 420
|
170
....*....|...
gi 1821109780 154 DYILLDEPLNNLD 166
Cdd:PRK10938 421 TLLILDEPLQGLD 433
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-205 |
6.41e-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: 45.04 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 14 CILKDINLELEQGTVTAFIGPNGAGKSTLLSTMCRllskdsghvlikgkeitkwrtdelakeIAILKQQNTYQVKMTVRE 93
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGL---------------------------ALGGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 94 LLSfgrfPYSKGRLTTEdyevidkvlgyldlesygdryLDTLSGGQLQRAALAMIL----VQDTDYILLDEPLNNLDMKQ 169
Cdd:cd03227 62 CIV----AAVSAELIFT---------------------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|....*.
gi 1821109780 170 SIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNI 205
Cdd:cd03227 117 GQALAEAILEHLVK-GAQVIVITHLPELAELADKLI 151
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-213 |
7.32e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 15 ILKDINLE-----------LEQGTVT-------AFIGPNGAGKSTLLSTM-----------CRLLskdsgHV--LIKGKE 63
Cdd:PLN03073 174 AIKDIHMEnfsisvggrdlIVDASVTlafgrhyGLVGRNGTGKTTFLRYMamhaidgipknCQIL-----HVeqEVVGDD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 64 ITKW---------RTDELAKEIAILKQQntyqvkmtvRELLSFGRFPYSKGRLTTED--------YEVIDKVLGYLDLES 126
Cdd:PLN03073 249 TTALqcvlntdieRTQLLEEEAQLVAQQ---------RELEFETETGKGKGANKDGVdkdavsqrLEEIYKRLELIDAYT 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 127 YGDRY-----------------LDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMkQSIVVMQTirnMADELGKTIL 189
Cdd:PLN03073 320 AEARAasilaglsftpemqvkaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAVLWLET---YLLKWPKTFI 395
|
250 260
....*....|....*....|....
gi 1821109780 190 VVLHDINFAAAYSDNIIAMKDGKI 213
Cdd:PLN03073 396 VVSHAREFLNTVVTDILHLHGQKL 419
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
119-226 |
7.37e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 119 LGYLDLesygDRYLDTLSGGQLQR--------AALAMILvqdtdYIlLDEPlnnldmkqSIVVMQ--------TIRNMAD 182
Cdd:PRK00349 478 LDYLTL----SRSAGTLSGGEAQRirlatqigSGLTGVL-----YV-LDEP--------SIGLHQrdndrlieTLKHLRD 539
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1821109780 183 eLGKTILVVLHD---InFAAaysDNIIamkD---------GKICHSGTVDEVICSE 226
Cdd:PRK00349 540 -LGNTLIVVEHDedtI-RAA---DYIV---DigpgagvhgGEVVASGTPEEIMKNP 587
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-222 |
8.60e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 20 NLELEQGTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDELAKEIA-ILKQQNTyqvkmtvrELLS-- 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdEWQRNNT--------DMLSpg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 97 ---FGRFPYSKGRLTTEDYEVIDKVLGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVV 173
Cdd:PRK10938 95 eddTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1821109780 174 MQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEV 222
Cdd:PRK10938 175 AELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-206 |
1.62e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 26 GTVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVLIKGKEITKWRTDE---------------------LAKEIAILKQQNT 84
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQEtpalpqpaleyvidgdreyrqLEAQLHDANERND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 85 YQVKMTVRellsfgrfpyskGRLTTEDYEVIDKVLGYLdLESYG------DRYLDTLSGGQLQRAALAMILVQDTDYILL 158
Cdd:PRK10636 107 GHAIATIH------------GKLDAIDAWTIRSRAASL-LHGLGfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1821109780 159 DEPLNNLDMKQSIVVMQTIRNMADelgkTILVVLHDINFAAAYSDNII 206
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKII 217
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
16-51 |
2.02e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.92 E-value: 2.02e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1821109780 16 LKDINLELEQgtVTAFIGPNGAGKSTLLSTMcRLLS 51
Cdd:COG4637 13 LRDLELPLGP--LTVLIGANGSGKSNLLDAL-RFLS 45
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-214 |
4.48e-05 |
|
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: 44.05 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 18 DINLELEQGTVTAFIGPNGAGKSTLLSTMCRLL-SKDSGHVLIKGKEI-TKWRTDELAKEIAIL----KQQNTYQV---- 87
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVdIRNPAQAIRAGIAMVpedrKRHGIVPIlgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 -KMTVRELLSFGrfpySKGRLTTE-DYEVIDKVLGYLDLESYG-DRYLDTLSGGQLQRAALAMILVQDTDYILLDEPLNN 164
Cdd:TIGR02633 358 kNITLSVLKSFC----FKMRIDAAaELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1821109780 165 LDMKQSIVVMQTIRNMADElGKTILVVLHDINFAAAYSDNIIAMKDGKIC 214
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-58 |
9.46e-05 |
|
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: 43.07 E-value: 9.46e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1821109780 16 LKDINLELEQGtVTAFIGPNGAGKSTLLSTMCRLLSKDSGHVL 58
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKF 55
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
16-105 |
5.73e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.79 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 16 LKDINLELEQGtVTAFIGPNGAGKSTLLSTMC--------RLLSKDSGHVLIKGKEITKWRTDELAKEIAILKQQNTYQV 87
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTILDAIKlalygktsRLKRKSGGGFVKGDIRIGLEGKGKAYVEITFENNDGRYTY 87
|
90
....*....|....*...
gi 1821109780 88 KMTVRELLSFGRFPYSKG 105
Cdd:pfam13476 88 AIERSRELSKKKGKTKKK 105
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-196 |
7.77e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 119 LGYLDLesygDRYLDTLSGGQLQRAALAMILV----QDTDYIlLDEPLNNL---DMKQSIVVMQTIrnmaDELGKTILVV 191
Cdd:PRK00635 798 LDYLPL----GRPLSSLSGGEIQRLKLAYELLapskKPTLYV-LDEPTTGLhthDIKALIYVLQSL----THQGHTVVII 868
|
....*
gi 1821109780 192 LHDIN 196
Cdd:PRK00635 869 EHNMH 873
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-42 |
9.65e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 9.65e-04
10 20
....*....|....*....|....*..
gi 1821109780 16 LKDINLELEQGTVTAFIGPNGAGKSTL 42
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTL 43
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-227 |
1.13e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 39.50 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 19 INLELEQGTVTAFIGPNGAGKSTLLSTMCRLLsKDSGHV-----LIKGKEITKWRTDE----LAKEIAILKQ--QNTYQV 87
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGIT-KDNWHVtadrfRWNGIDLLKLSPRErrkiIGREIAMIFQepSSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 88 KMTVRELLSF--------GRFPYSKGRLTTEDYEVIDKVlGYLDLESYGDRYLDTLSGGQLQRAALAMILVQDTDYILLD 159
Cdd:COG4170 105 SAKIGDQLIEaipswtfkGKWWQRFKWRKKRAIELLHRV-GIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIAD 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1821109780 160 EPLNNLDmkqSIVVMQTIR---NMADELGKTILVVLHDINFAAAYSDNIIAMKDGKICHSGTVDEVICSEH 227
Cdd:COG4170 184 EPTNAME---STTQAQIFRllaRLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPH 251
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
135-227 |
1.94e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.02 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1821109780 135 LSGGQLQRAALAMILVQDTDYILLDEPLNNLDMKQSIVVMQTIRNMADELGKTILVVLHDINFAAAYSDNIIAMKDGKIC 214
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90
....*....|...
gi 1821109780 215 HSGTVDEVICSEH 227
Cdd:PRK15093 239 ETAPSKELVTTPH 251
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
21-50 |
2.18e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.65 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|
gi 1821109780 21 LELEQGTVTAFIGPNGAGKSTLLSTMCRLL 50
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
16-51 |
2.44e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 2.44e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1821109780 16 LKDINLELEQG-TVTAFIGPNGAGKSTLLSTMCRLLS 51
Cdd:COG3950 14 FEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIALALS 50
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
21-43 |
7.39e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 36.67 E-value: 7.39e-03
|
| |
