|
Name |
Accession |
Description |
Interval |
E-value |
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-246 |
2.70e-96 |
|
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: 285.78 E-value: 2.70e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:COG1120 1 MLEAENLSVGYG-----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNINNLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQD 166
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 167 TPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIF 245
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVaQGPPEEVLTPELLEEVY 235
|
.
gi 1082420396 246 D 246
Cdd:COG1120 236 G 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
9-228 |
9.78e-68 |
|
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: 210.37 E-value: 9.78e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 9 EIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLV 88
Cdd:cd03214 1 EVENLSVGYG-----GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 89 SFVSTeivninnlrvfdlvalgrfphtnwfgkletkdlksvskALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTP 168
Cdd:cd03214 76 AYVPQ--------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 169 VIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII 228
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-245 |
1.09e-66 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 209.95 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 6 HILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI------IGY 79
Cdd:COG1121 5 PAIELENLTVSYG-----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPrrarrrIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 80 --SRADFARlvSFvsteivninNLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRV 157
Cdd:COG1121 80 vpQRAEVDW--DF---------PITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIwLMLNDSII-EGAPEDLI 236
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRV-LLLNRGLVaHGPPEEVL 226
|
....*....
gi 1082420396 237 LNETFNQIF 245
Cdd:COG1121 227 TPENLSRAY 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-224 |
3.58e-59 |
|
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: 189.67 E-value: 3.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 9 EIHNLEIGYHiSKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI------IGY--S 80
Cdd:cd03235 1 EVEDLTVSYG-GHPV----LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLekerkrIGYvpQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARlvSFvsteivninNLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIA 160
Cdd:cd03235 76 RRSIDR--DF---------PISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIwLMLN 224
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRV-LLLN 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-246 |
8.81e-55 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 179.82 E-value: 8.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiSKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:PRK11231 2 TLRTENLTVGYG-TKRI----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNINNLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQD 166
Cdd:PRK11231 77 RLALLPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 167 TPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIF 245
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMaQGTPEEVMTPGLLRTVF 235
|
.
gi 1082420396 246 D 246
Cdd:PRK11231 236 D 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-246 |
1.20e-49 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 166.41 E-value: 1.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIV 96
Cdd:COG4604 6 NVSKRYGGKVVlDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRVFDLVALGRFPHTNwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:COG4604 86 INSRLTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 177 AFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIFD 246
Cdd:COG4604 164 NNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVaQGTPEEIITPEVLSDIYD 234
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-239 |
1.95e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 162.50 E-value: 1.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:COG1122 1 IELENLSFSYPGGTPA----LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFV----STEIVNINnlrVFDLVAlgrfphtnwFG----KLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVM 158
Cdd:COG1122 77 VGLVfqnpDDQLFAPT---VEEDVA---------FGpenlGLPREEIRErVEEALELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLIL 237
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVaDGTPREVFS 223
|
..
gi 1082420396 238 NE 239
Cdd:COG1122 224 DY 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
26-246 |
2.48e-47 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 164.63 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 26 SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFD 105
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 LVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKY 185
Cdd:PRK09536 97 VVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 186 EIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDLILNETFNQIFD 246
Cdd:PRK09536 177 RTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAaGPPADVLTADTLRAAFD 237
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
9-222 |
1.43e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 154.55 E-value: 1.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 9 EIHNLEIGYHISKRihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLV 88
Cdd:cd03225 1 ELKNLSFSYPDGAR---PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 89 SFV----STEIVNinnLRVFDLVALGRFPhtnwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLA 164
Cdd:cd03225 78 GLVfqnpDDQFFG---PTVEEEVAFGLEN----LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 165 QDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-238 |
4.21e-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: 155.45 E-value: 4.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAD--- 83
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARLVSFV------SteivnIN-NLRVFDLVAlgrFPHTNwFGKLETKDLKS-VSKALEMVGM-KSFVNKNINEISDGER 154
Cdd:COG1123 340 LRRRVQMVfqdpysS-----LNpRMTVGDIIA---EPLRL-HGLLSRAERRErVAELLERVGLpPDLADRYPHELSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 155 QRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPE 233
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEdGPTE 490
|
....*
gi 1082420396 234 DLILN 238
Cdd:COG1123 491 EVFAN 495
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-245 |
1.49e-42 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 148.40 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 26 SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFD 105
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 LVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKY 185
Cdd:PRK10575 105 LVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 186 EIVHLLNNLSKTENKTIIFSTHDLNIAIQETDK-IWLMLNDSIIEGAPEDLILNETFNQIF 245
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYlVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-245 |
1.74e-42 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 148.21 E-value: 1.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 12 NLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFV 91
Cdd:PRK10253 12 QLTLGYG-----KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 92 STEIVNINNLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIV 171
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 172 LDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQ-ETDKIWLMLNDSIIEGAPEDLILNETFNQIF 245
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-235 |
8.52e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.58 E-value: 8.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:COG3638 2 MLELRNLSKRYPGGTPA----LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 L---VSFVSTEIVNINNLRVFDLVALGRFPHTN----WFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMI 159
Cdd:COG3638 78 LrrrIGMIFQQFNLVPRLSVLTNVLAGRLGRTStwrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 160 ARTLAQDtPVIVL-DEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIwLMLNDS--IIEGAPEDL 235
Cdd:COG3638 158 ARALVQE-PKLILaDEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRI-IGLRDGrvVFDGPPAEL 234
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-246 |
6.68e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 143.76 E-value: 6.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLeiGYHISKRihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:PRK13548 3 LEARNL--SVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 ---------VSFvsteivninNLRVFDLVALGRFPHTNwfGKLETKDLksVSKALEMVGMKSFVNKNINEISDGERQRVM 158
Cdd:PRK13548 78 ravlpqhssLSF---------PFTVEEVVAMGRAPHGL--SRAEDDAL--VAAALAQVDLAHLAGRDYPQLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 159 IARTLAQ------DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGA 231
Cdd:PRK13548 145 LARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVaDGT 224
|
250
....*....|....*
gi 1082420396 232 PEDLILNETFNQIFD 246
Cdd:PRK13548 225 PAEVLTPETLRRVYG 239
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-245 |
1.72e-40 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 142.32 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:cd03256 1 IEVENLSKTYPNGKKA----LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 ---VSFVSTEIVNINNLRVFDLVALGRFPHTNW----FGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIA 160
Cdd:cd03256 77 rrqIGMIFQQFNLIERLSVLENVLSGRLGRRSTwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLIlNE 239
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVfDGPPAELT-DE 235
|
....*.
gi 1082420396 240 TFNQIF 245
Cdd:cd03256 236 VLDEIY 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-295 |
4.04e-40 |
|
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: 147.36 E-value: 4.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL---QNSIQGDILLNKKNIIGYSRAD 83
Cdd:COG1123 4 LLEVRDLSVRYPGGDV---PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARLVSFVSTEIVN-INNLRVFDLVALGrfphtnwfgkLETKDL------KSVSKALEMVGMKSFVNKNINEISDGERQR 156
Cdd:COG1123 81 RGRRIGMVFQDPMTqLNPVTVGDQIAEA----------LENLGLsraearARVLELLEAVGLERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 157 VMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLI 236
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 237 LNetfNQIFDNSKLSFDRVKGDFRMKRKYTEKIgLFGEGIYYTW------TKKALERMNFTVEKG 295
Cdd:COG1123 231 LA---APQALAAVPRLGAARGRAAPAAAAAEPL-LEVRNLSKRYpvrgkgGVRAVDDVSLTLRRG 291
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-229 |
5.35e-40 |
|
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: 140.33 E-value: 5.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiSKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS---RAD 83
Cdd:cd03257 1 LLEVKNLSVSFP-TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARLVSFVSTEIVNINN--LRVFDLVALGRFPHtnwfGKLETKDLKSVSKALEMVGM---KSFVNKNINEISDGERQRVM 158
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNprMTIGEQIAEPLRIH----GKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-246 |
1.28e-38 |
|
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: 137.43 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQA----LKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 L---VSFVSTEIVNINNLRVFDLVALGRFPHTN----WFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMI 159
Cdd:TIGR02315 77 LrrrIGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 160 ARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIwLMLNDSII--EGAPEDLIl 237
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRI-VGLKAGEIvfDGAPSELD- 234
|
....*....
gi 1082420396 238 NETFNQIFD 246
Cdd:TIGR02315 235 DEVLRHIYG 243
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-238 |
1.34e-38 |
|
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: 137.24 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRiHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:COG1124 2 LEVRNLSVSYGQGGR-RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFV---STEIVNiNNLRVFDLVA-----LGRFPHTnwfgkletkdlKSVSKALEMVGM-KSFVNKNINEISDGERQRVM 158
Cdd:COG1124 81 VQMVfqdPYASLH-PRHTVDRILAeplriHGLPDRE-----------ERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILN 238
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-235 |
1.73e-38 |
|
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: 136.86 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiSKRIHNslvsNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:cd03261 1 IELRGLTKSFG-GRTVLK----GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 -----VSFVSTEIvnINNLRVFDLVALGRFPHTNwfgKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIART 162
Cdd:cd03261 76 rrrmgMLFQSGAL--FDSLTVFENVAFPLREHTR---LSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 163 LAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIwLMLNDS--IIEGAPEDL 235
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRI-AVLYDGkiVAEGTPEEL 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-225 |
3.25e-38 |
|
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: 135.31 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIHNSLvSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 ----VSFV--STEIvnINNLRVFDLVALGRFphtnWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIAR 161
Cdd:cd03255 80 rrrhIGFVfqSFNL--LPDLTALENVELPLL----LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 162 TLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAiQETDKIwLMLND 225
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRI-IELRD 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-222 |
1.39e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 133.80 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRL 87
Cdd:cd03259 1 LELKGLSKTYG-----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEIVNINNLRVFDLVAlgrFPHTNWFGKLETKDLKsVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIA---FGLKLRGVPKAEIRAR-VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
2.59e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.24 E-value: 2.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METrkhILEIHNLEIGYHISKRIHNSLvSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS 80
Cdd:COG1136 1 MSP---LLELRNLTKSYGTGEGEVTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARL----VSFV--STEIvnINNLRVFDLVALGRFPHtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGER 154
Cdd:COG1136 77 ERELARLrrrhIGFVfqFFNL--LPELTALENVALPLLLA----GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 155 QRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIA 212
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-236 |
5.11e-37 |
|
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: 139.51 E-value: 5.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRihnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:COG4988 337 IELEDVSFSYPGGRP----ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVS--TEIVN---INNLRvfdlvaLGRfPHTnwfgkletkDLKSVSKALEMVGMKSFVNK-------NINE----ISD 151
Cdd:COG4988 413 IAWVPqnPYLFAgtiRENLR------LGR-PDA---------SDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-G 230
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLA-LLAQADRILVLDDGRIVEqG 553
|
....*.
gi 1082420396 231 APEDLI 236
Cdd:COG4988 554 THEELL 559
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-222 |
5.24e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.86 E-value: 5.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:COG4619 1 LELEGLSFRVG-----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEivninNLRVFDLVA--LgRFPhtnWFGKLETKDLKSVSKALEMVGM-KSFVNKNINEISDGERQRVMIARTLA 164
Cdd:COG4619 76 VAYVPQE-----PALWGGTVRdnL-PFP---FQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 165 QDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-235 |
6.48e-36 |
|
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: 130.10 E-value: 6.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiSKRIHNslvsNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:COG1127 5 MIEVRNLTKSFG-DRVVLD----GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 L---VSFV--------SteivninnLRVFDLVAlgrFP---HTNwFGKLETKDLksVSKALEMVGMKSFVNKNINEISDG 152
Cdd:COG1127 80 LrrrIGMLfqggalfdS--------LTVFENVA---FPlreHTD-LSEAEIREL--VLEKLELVGLPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 153 ERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIwLMLNDS--IIEG 230
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRV-AVLADGkiIAEG 224
|
....*
gi 1082420396 231 APEDL 235
Cdd:COG1127 225 TPEEL 229
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-238 |
1.77e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.72 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSFVSTEivniNNL----RVFD 105
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQE----NNLfphlTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 LVALGRFPHtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDlPN-K 184
Cdd:COG3840 91 NIGLGLRPG----LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD-PAlR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 185 YEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILN 238
Cdd:COG3840 166 QEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-245 |
2.55e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.26 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLeigyhiSKRIHNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAdFAR 86
Cdd:COG1131 1 IEVRGL------TKRYGDKTaLDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNINNLRVFDLVAL-GRFphtnwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ 165
Cdd:COG1131 74 RIGYVPQEPALYPDLTVRENLRFfARL-----YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLiLNETFNQI 244
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVaDGTPDEL-KARLLEDV 226
|
.
gi 1082420396 245 F 245
Cdd:COG1131 227 F 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
1.31e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.13 E-value: 1.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHISKRIHNsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS 80
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTGGGGVT-ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RAdfarlVSFVsteivninnLRVFDLVALGrfPHTNWFGKLETKDLksVSKALEMVGMKSFVNKNINEISDGERQRVMIA 160
Cdd:COG1116 80 PD-----RGVVfqepallpwLTVLDNVALG--LELRGVPKAERRER--ARELLELVGLAGFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-236 |
1.41e-34 |
|
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: 133.81 E-value: 1.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:COG2274 474 IELENVSFRYPGDSPP---VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEIV----NI-NNLRVFDLVAlgrfphtnwfgkletkDLKSVSKALEMVGMKSFVNK-------NINE----ISD 151
Cdd:COG2274 551 IGVVLQDVFlfsgTIrENITLGDPDA----------------TDEEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLSG 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNIaIQETDKIWLMLNDSIIE-G 230
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLST-IRLADRIIVLDKGRIVEdG 691
|
....*.
gi 1082420396 231 APEDLI 236
Cdd:COG2274 692 THEELL 697
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-235 |
1.51e-34 |
|
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: 126.20 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIG---YSRadfarlvsfvst 93
Cdd:cd03300 5 NVSKFYGGFVaLDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKR------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 94 eivNINNlrVFDLVALgrFPHTN-----WFG----KLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVMIARTL 163
Cdd:cd03300 73 ---PVNT--VFQNYAL--FPHLTvfeniAFGlrlkKLPKAEIKErVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 164 AQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMlNDSIIE--GAPEDL 235
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVM-NKGKIQqiGTPEEI 218
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-246 |
2.12e-34 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 126.35 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL-----QNSIQgdiLLNKKnIIGYSRADFARLVSFVSTEIVN--IN 99
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptyGNDVR---LFGER-RGGEDVWELRKRIGLVSPALQLrfPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 NLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:COG1119 94 DETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 180 DLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDLILNETFNQIFD 246
Cdd:COG1119 174 DLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAaGPKEEVLTSENLSEAFG 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-222 |
5.18e-34 |
|
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: 124.51 E-value: 5.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiSKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAdfarl 87
Cdd:cd03293 1 LEVRNVSKTYG-GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEIVNINNLRVFDLVALGrfPHTNWFGKLETKDLksVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALG--LELQGVPKAEARER--AEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-251 |
5.53e-34 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 124.58 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 33 LTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI------IGY--SRADFARLVSfvsteivninnLRVF 104
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPgkgwrhIGYvpQRHEFAWDFP-----------ISVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNK 184
Cdd:TIGR03771 70 HTVMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 185 YEIVHLLNNLSKTENkTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILNETFNQIFDNSKLS 251
Cdd:TIGR03771 150 ELLTELFIELAGAGT-AILMTTHDLAQAMATCDRVVLLNGRVIADGTPQQLQDPAPWMTTFGVSDSS 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
9-222 |
9.24e-34 |
|
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: 121.97 E-value: 9.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 9 EIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLV 88
Cdd:cd00267 1 EIENLSFRYG-----GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 89 SFVSteivninnlrvfdlvalgrfphtnwfgkletkdlksvskalemvgmksfvnkninEISDGERQRVMIARTLAQDTP 168
Cdd:cd00267 76 GYVP-------------------------------------------------------QLSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 169 VIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
28-177 |
1.74e-33 |
|
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: 120.83 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFDLV 107
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 108 ALGRFPhtnwFGKLETKDLKSVSKALEMVGM----KSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTA 177
Cdd:pfam00005 81 RLGLLL----KGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-221 |
1.92e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 121.96 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLqnsiqgdillnKKNIIGYSRADFARLVSFV--STEIVNINNLRVF 104
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV-----------LRPTSGTVRRAGGARVAYVpqRSEVPDSLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNK 184
Cdd:NF040873 76 DLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1082420396 185 YEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWL 221
Cdd:NF040873 156 ERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
18-245 |
1.94e-33 |
|
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: 123.81 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAdFARLVSFVSTEIV 96
Cdd:COG4555 6 NLSKKYGKVPaLKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRVFDLVA-LGRFphtnwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEP 175
Cdd:COG4555 85 LYDRLTVRENIRyFAEL-----YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 176 TAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDL---ILNETFNQIF 245
Cdd:COG4555 160 TNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAqGSLDELreeIGEENLEDAF 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
8-222 |
6.06e-33 |
|
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: 120.37 E-value: 6.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI--IGYSRADFA 85
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RLVSFVSTEIVNINNLRVFDLVALGrfphtnwfgkletkdlksvskalemvgmksfvnknineISDGERQRVMIARTLAQ 165
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-236 |
1.62e-32 |
|
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: 127.19 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:COG4987 334 LELEDVSFRYPGAGRP---VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVS--TEIVNI---NNLRVfdlvalgrfphtnwfGKLETKDLKsVSKALEMVGMKSFVNK-------NINE----ISD 151
Cdd:COG4987 411 IAVVPqrPHLFDTtlrENLRL---------------ARPDATDEE-LWAALERVGLGDWLAAlpdgldtWLGEggrrLSG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLnIAIQETDKIWLMLNDSIIE-G 230
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRL-AGLERMDRILVLEDGRIVEqG 551
|
....*.
gi 1082420396 231 APEDLI 236
Cdd:COG4987 552 THEELL 557
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-238 |
1.63e-32 |
|
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: 121.25 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNS--LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEI 95
Cdd:cd03295 5 NVTKRYGGGkkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 96 vninnlrvfdlvalGRFPH-TNW---------FGKLETKDLKSVSKALEMVGM--KSFVNKNINEISDGERQRVMIARTL 163
Cdd:cd03295 85 --------------GLFPHmTVEenialvpklLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 164 AQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDLILN 238
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQvGTPDEILRS 226
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
19-235 |
8.22e-32 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 119.13 E-value: 8.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 19 ISKRIHN-SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSFVSTEIVN 97
Cdd:TIGR00968 6 ISKRFGSfQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARD--RKIGFVFQHYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 98 INNLRVFDLVALG----RFPhtnwfgKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLD 173
Cdd:TIGR00968 84 FKHLTVRDNIAFGleirKHP------KAKIK--ARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 174 EPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDL 235
Cdd:TIGR00968 156 EPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQiGSPDEV 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
8-235 |
1.07e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 119.84 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNkkniiGYSRADFArl 87
Cdd:TIGR04520 1 IEVENVSFSYPESEKP---ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-----GLDTLDEE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 vsfvsteivNINNLR-----VF-------------DLVAlgrfphtnwFGkLETKDLKS------VSKALEMVGMKSFVN 143
Cdd:TIGR04520 71 ---------NLWEIRkkvgmVFqnpdnqfvgatveDDVA---------FG-LENLGVPReemrkrVDEALKLVGMEDFRD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 144 KNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQeTDKIWLML 223
Cdd:TIGR04520 132 REPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMN 210
|
250
....*....|...
gi 1082420396 224 NDSII-EGAPEDL 235
Cdd:TIGR04520 211 KGKIVaEGTPREI 223
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
18-212 |
1.89e-31 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 117.33 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLN---------------KKNIIGYSR 81
Cdd:TIGR03608 3 NISKKFGDKVIlDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNgqetpplnskkaskfRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 82 ADFArlvsFVSTEIVNiNNLRVfdlvALGrfphtnwFGKLETKD-LKSVSKALEMVGMKSFVNKNINEISDGERQRVMIA 160
Cdd:TIGR03608 83 QNFA----LIENETVE-ENLDL----GLK-------YKKLSKKEkREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIA 212
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELND-EGKTIIIVTHDPEVA 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-211 |
4.25e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 116.69 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI---------- 76
Cdd:COG2884 1 MIRFENVSKRYPGGREA----LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkrreipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 ----IGYSRADFaRLvsfvsteivnINNLRVFDLVAL-----GRfphtnwfgklETKDLKS-VSKALEMVGMKSFVNKNI 146
Cdd:COG2884 77 lrrrIGVVFQDF-RL----------LPDRTVYENVALplrvtGK----------SRKEIRRrVREVLDLVGLSDKAKALP 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 147 NEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTeNKTIIFSTHDLNI 211
Cdd:COG2884 136 HELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLEL 199
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
28-238 |
5.80e-31 |
|
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: 117.74 E-value: 5.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfarlvsfvsteivnINNLR----- 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE--------------LRELRrkkis 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 103 -VFDLVALgrFPHTN-----WFGkLEtkdLKSVSK---------ALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:cd03294 106 mVFQSFAL--LPHRTvlenvAFG-LE---VQGVPRaereeraaeALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDLILN 238
Cdd:cd03294 180 DILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQvGTPEEILTN 251
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
28-255 |
6.50e-31 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 117.25 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSiQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFDLV 107
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRFPHTNwfgklETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVI-------VLDEPTAFLD 180
Cdd:COG4138 91 ALHQPAGAS-----SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVWPTInpegqllLLDEPMNSLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 181 lpnkyeIVH------LLNNLSkTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIFDnskLSFD 253
Cdd:COG4138 166 ------VAQqaaldrLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVaSGETAEVMTPENLSEVFG---VKFR 235
|
..
gi 1082420396 254 RV 255
Cdd:COG4138 236 RL 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-222 |
1.19e-30 |
|
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: 114.03 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGySRADFARLVSFVSTEIV 96
Cdd:cd03230 5 NLSKRYGKKTAlDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRVFDLVALgrfphtnwfgkletkdlksvskalemvgmksfvnknineiSDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:cd03230 84 LYENLTVRENLKL----------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1082420396 177 AFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03230 124 SGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-228 |
3.32e-30 |
|
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: 113.89 E-value: 3.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 9 EIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigySRADFARLV 88
Cdd:cd03226 1 RIENISFSYKKGTEI----LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 89 SFVSteivniNNLR-------VFDLVALGRfphtnwfgKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIAR 161
Cdd:cd03226 74 GYVM------QDVDyqlftdsVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 162 TLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSII 228
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-245 |
6.36e-30 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 115.31 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRiHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAG-LQNS-------IQGDILLNKKNIIGYSRADFARLVS 89
Cdd:PRK13547 8 HVARR-HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 90 FVSTEIVNINNLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ---- 165
Cdd:PRK13547 87 VLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 166 -----DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNE 239
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVaHGAPADVLTPA 246
|
....*.
gi 1082420396 240 TFNQIF 245
Cdd:PRK13547 247 HIARCY 252
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-235 |
6.67e-30 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 116.74 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 4 RKHILEIHNLeigyhiSKRIHNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGysra 82
Cdd:COG3842 2 AMPALELENV------SKRYGDVTaLDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 83 dfarlvsfVSTEIVNINnlrvfdLV----ALgrFPHTN-W----FGkLETKDL------KSVSKALEMVGMKSFVNKNIN 147
Cdd:COG3842 72 --------LPPEKRNVG------MVfqdyAL--FPHLTvAenvaFG-LRMRGVpkaeirARVAELLELVGLEGLADRYPH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 148 EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDlniaiQE-----TDKIWLM 222
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD-----QEealalADRIAVM 209
|
250
....*....|....*
gi 1082420396 223 lNDSIIE--GAPEDL 235
Cdd:COG3842 210 -NDGRIEqvGTPEEI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-235 |
7.04e-30 |
|
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: 113.97 E-value: 7.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHN-SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSFVSTEIV 96
Cdd:cd03296 7 NVSKRFGDfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRVFDLVALG-RF-PHTNWFGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDE 174
Cdd:cd03296 85 LFRHMTVFDNVAFGlRVkPRSERPPEAEIR--AKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 175 PTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDL 235
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQvGTPDEV 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-236 |
2.50e-29 |
|
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: 112.27 E-value: 2.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGY---HISKrihnslvsNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQ-----GDILLNKKNIIGY 79
Cdd:cd03260 1 IELRDLNVYYgdkHALK--------DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 80 SradfarlvsfvsteiVNINNLR----------------VFDLVALGRFPHtnwfGKLETKDLKS-VSKALEMVGMKSFV 142
Cdd:cd03260 73 D---------------VDVLELRrrvgmvfqkpnpfpgsIYDNVAYGLRLH----GIKLKEELDErVEEALRKAALWDEV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 143 NKNIN--EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNIAIQETDKIW 220
Cdd:cd03260 134 KDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTA 211
|
250
....*....|....*.
gi 1082420396 221 LMLNDSIIEGAPEDLI 236
Cdd:cd03260 212 FLLNGRLVEFGPTEQI 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-221 |
4.03e-29 |
|
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: 111.03 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 6 HILEIHNLEIGYHisKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNiIGYSRADFA 85
Cdd:COG4133 1 MMLEAENLSCRRG--ERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-IRDAREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RLVSFVSTEIVNINNLRVFDLVALgrfpHTNWFGKLETKDlkSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ 165
Cdd:COG4133 75 RRLAYLGHADGLKPELTVRENLRF----WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLnIAIQETDKIWL 221
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLA-RGGAVLLTTHQP-LELAAARVLDL 202
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-207 |
9.23e-29 |
|
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: 110.28 E-value: 9.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 33 LTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSFVSTEivniNN----LRVFDLVA 108
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQE----NNlfahLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 109 LGRFPHTnwfgKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIV 188
Cdd:cd03298 93 LGLSPGL----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170
....*....|....*....
gi 1082420396 189 HLLNNLSKTENKTIIFSTH 207
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTH 187
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
30-255 |
1.30e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLnKKNIIGYSRADFARLVSFVSTEIVNINNL----RVFD 105
Cdd:PRK13639 20 GINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKYDKKSLLEVRKTVGIVFQNPDDQlfapTVEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 LVALGrfPHTNWFGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKY 185
Cdd:PRK13639 99 DVAFG--PLNLGLSKEEVE--KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 186 EIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNEtfnQIFDNSKLSFDRV 255
Cdd:PRK13639 175 QIMKLLYDLNK-EGITIIISTHDVDLVPVYADKVYVMSDGKIIkEGTPKEVFSDI---ETIRKANLRLPRV 241
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-222 |
4.63e-28 |
|
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: 107.08 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVninnlrvfdl 106
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPF---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 valgRFPHTnwfgkletkdlksvskalemvgmksfVNKNIneISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:cd03228 87 ----LFSGT--------------------------IRENI--LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082420396 187 IVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLM 222
Cdd:cd03228 135 ILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVL 167
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-222 |
5.35e-28 |
|
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: 108.39 E-value: 5.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRadfarl 87
Cdd:cd03262 1 IEIKNLHKSFG-----DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKK------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 vsfvsteivNINNLR-----VFDLVALgrFPHTNWFG--KLETKDLKSVSKA---------LEMVGMKSFVNKNINEISD 151
Cdd:cd03262 70 ---------NINELRqkvgmVFQQFNL--FPHLTVLEniTLAPIKVKGMSKAeaeeralelLEKVGLADKADAYPAQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03262 139 GQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-234 |
1.03e-27 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 109.20 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 24 HNSLvSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDIllnkkNIIGYS--RADFARLVSFV--STEIVNIN 99
Cdd:PRK15056 20 HTAL-RDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPtrQALQKNLVAYVpqSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 NLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 180 DLPNKYEIVHLLNNLsKTENKTIIFSTHDLNiAIQETDKIWLMLNDSIIEGAPED 234
Cdd:PRK15056 174 DVKTEARIISLLREL-RDEGKTMLVSTHNLG-SVTEFCDYTVMVKGTVLASGPTE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-239 |
1.35e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 109.12 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 6 HILEIHNLEIGYHISKRIHNslvsNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigySRADFA 85
Cdd:PRK13652 2 HLIETRDLCYSYSGSKEALN----NINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RLVSFVSTEIVN----INNLRVFDLVALGRfphTNwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIAR 161
Cdd:PRK13652 75 EVRKFVGLVFQNpddqIFSPTVEQDIAFGP---IN-LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 162 TLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNE 239
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVaYGTVEEIFLQP 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
31-255 |
2.31e-27 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 107.71 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSiQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFDLVALG 110
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 111 RFPHTNwfgklETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVI-------VLDEPTAFLDLPN 183
Cdd:PRK03695 94 QPDKTR-----TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 184 KYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIFDnskLSFDRV 255
Cdd:PRK03695 169 QAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLaSGRRDEVLTPENLAQVFG---VNFRRL 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-235 |
1.18e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.86 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 12 NLEIGyHISKRI-HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSF 90
Cdd:PRK10851 2 SIEIA-NIKKSFgRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 91 VSTEIVNINNLRVFDLVALGR--FPHTNWFGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTP 168
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLtvLPRRERPNAAAIK--AKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 169 VIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMlNDSIIE--GAPEDL 235
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVM-SQGNIEqaGTPDQV 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
28-207 |
1.32e-26 |
|
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: 104.98 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNIN-NLRvfDL 106
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYgTLR--DN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALGRFPHTNwfgkletkdlKSVSKALEMVGMKSFVNKN-------INE----ISDGERQRVMIARTLAQDTPVIVLDEP 175
Cdd:cd03245 98 ITLGAPLADD----------ERILRAAELAGVTDFVNKHpngldlqIGErgrgLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190
....*....|....*....|....*....|..
gi 1082420396 176 TAFLDLPNKYEIVHLLNNLskTENKTIIFSTH 207
Cdd:cd03245 168 TSAMDMNSEERLKERLRQL--LGDKTLIIITH 197
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
31-212 |
1.40e-26 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 104.04 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIiGYSRADFARLVSFVSTEIVN----INNLRVFDL 106
Cdd:TIGR01166 11 LNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERRQRVGLVFQDpddqLFAADVDQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALGrfPHTnwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:TIGR01166 90 VAFG--PLN--LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|....*.
gi 1082420396 187 IVHLLNNLsKTENKTIIFSTHDLNIA 212
Cdd:TIGR01166 166 MLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
18-209 |
1.43e-26 |
|
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: 104.58 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNS-LVSNINLTASEGeLIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYsRADFARLVSFVSTEIV 96
Cdd:cd03264 5 NLTKRYGKKrALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRVFDLVAlgrfpHTNWFGKLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEP 175
Cdd:cd03264 83 VYPNFTVREFLD-----YIAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190
....*....|....*....|....*....|....
gi 1082420396 176 TAFLDLPNKYEIVHLLNNLSktENKTIIFSTHDL 209
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELG--EDRIVILSTHIV 189
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-236 |
1.46e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.25 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVninnlrVFDL- 106
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTF------LFSGt 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 ----VALGRfphtnwfgklETKDLKSVSKALEMVGMKSFVNK-------NINE----ISDGERQRVMIARTLAQDTPVIV 171
Cdd:COG1132 430 irenIRYGR----------PDATDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 172 LDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIwLMLND-SIIE-GAPEDLI 236
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLS-TIRNADRI-LVLDDgRIVEqGTHEELL 562
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-239 |
3.32e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 6 HILEIHNLEIGYhiskRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDI-----LLNKKNI---- 76
Cdd:PRK13647 3 NIIEVEDLHFRY----KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrEVNAENEkwvr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 --IGYSRADFARLVsFVSTeivninnlrVFDLVALGrfPHTNWFGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGER 154
Cdd:PRK13647 79 skVGLVFQDPDDQV-FSST---------VWDDVAFG--PVNMGLDKDEVE--RRVEEALKAVRMWDFRDKPPYHLSYGQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 155 QRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIwLMLND--SIIEGAP 232
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQV-IVLKEgrVLAEGDK 222
|
....*..
gi 1082420396 233 EdLILNE 239
Cdd:PRK13647 223 S-LLTDE 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-229 |
3.33e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 102.39 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGY-HISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAdFAR 86
Cdd:cd03247 1 LSINNVSFSYpEQEQQV----LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIvninnlRVFDlvalgrfphtnwfgkletkdlksvSKALEMVGMKsfvnknineISDGERQRVMIARTLAQD 166
Cdd:cd03247 76 LISVLNQRP------YLFD------------------------TTLRNNLGRR---------FSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 167 TPVIVLDEPTAFLDLPNKYEIVHLLnnLSKTENKTIIFSTHDLnIAIQETDKIWLMLNDSIIE 229
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLI--FEVLKDKTLIWITHHL-TGIEHMDKILFLENGKIIM 176
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
32-227 |
4.92e-26 |
|
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: 103.02 E-value: 4.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 32 NLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGysRADFARLVSFVSTEIVNINNLRVFDLVALGR 111
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG--LAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 112 FPHTnwfgKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLL 191
Cdd:TIGR01277 96 HPGL----KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082420396 192 NNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSI 227
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-234 |
8.24e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.18 E-value: 8.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNleigyhISKRI-HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGy 79
Cdd:PRK09452 8 PSSLSPLVELRG------ISKSFdGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 80 sradfarlvsfVSTEIVNINNlrVFDLVALgrFPHTNWF------------GKLETKdlKSVSKALEMVGMKSFVNKNIN 147
Cdd:PRK09452 81 -----------VPAENRHVNT--VFQSYAL--FPHMTVFenvafglrmqktPAAEIT--PRVMEALRMVQLEEFAQRKPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 148 EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMlNDSI 227
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM-RDGR 222
|
....*....
gi 1082420396 228 IE--GAPED 234
Cdd:PRK09452 223 IEqdGTPRE 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-244 |
8.59e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.92 E-value: 8.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHISkriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigyS 80
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNS---ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARLVSFVSTEIVNINN----LRVFDLVALGrfphtnwfgkLETKDLKS------VSKALEMVGMKSFVNKNINEIS 150
Cdd:PRK13632 75 KENLKEIRKKIGIIFQNPDNqfigATVEDDIAFG----------LENKKVPPkkmkdiIDDLAKKVGMEDYLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 151 DGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQeTDKIWLMLNDSII-E 229
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIaQ 223
|
250
....*....|....*
gi 1082420396 230 GAPEDLILNETFNQI 244
Cdd:PRK13632 224 GKPKEILNNKEILEK 238
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
28-239 |
1.03e-25 |
|
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: 102.90 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL---VSFvstEIVNI-NNLRV 103
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigRTF---QIPRLfPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDLVALGRFPHTN---WFGKLETKDLKSVSKA---LEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTA 177
Cdd:cd03219 93 LENVMVAAQARTGsglLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 178 FLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNE 239
Cdd:cd03219 173 GLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIaEGTPDEVRNNP 234
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
28-209 |
1.09e-25 |
|
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: 107.45 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFV-------STEIvnINN 100
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCaqdahlfDTTV--REN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 101 LRVfdlvalgrfphtnwfGKLETKDlKSVSKALEMVGMKSFV-------NKNINE----ISDGERQRVMIARTLAQDTPV 169
Cdd:TIGR02868 429 LRL---------------ARPDATD-EELWAALERVGLADWLralpdglDTVLGEggarLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1082420396 170 IVLDEPTAFLDLPNKYEIVHLLnnLSKTENKTIIFSTHDL 209
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-236 |
1.20e-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: 104.75 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSlVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL---QNSIQGDILLNKKNIIGYSRAD 83
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKA-VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARL----VSFV------SteivnIN-NLRVFDLVALGRFPHtnwfGKLETKDLKS-VSKALEMVGM---KSFVNKNINE 148
Cdd:COG0444 80 LRKIrgreIQMIfqdpmtS-----LNpVMTVGDQIAEPLRIH----GGLSKAEARErAIELLERVGLpdpERRLDRYPHE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 149 ISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII 228
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
....*....
gi 1082420396 229 EGAP-EDLI 236
Cdd:COG0444 231 EEGPvEELF 239
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-238 |
1.24e-25 |
|
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: 102.66 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSLvSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAD--- 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTAL-KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARLVSFVSTEIVNINNLRVFDLVALgrfPhtnwfgkLEtkdLKSVSKA---------LEMVGMKSFVNKNINEISDGER 154
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVAL---P-------LE---IAGVPKAeieervlelLELVGLEDKADAYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 155 QRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPE 233
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEeGTVE 226
|
....*
gi 1082420396 234 DLILN 238
Cdd:cd03258 227 EVFAN 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-211 |
1.30e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 102.10 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL---VSFVSTEIVNINNLRVFD 105
Cdd:cd03292 18 DGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 LVALG----RFPHTNWfgkletkdLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDL 181
Cdd:cd03292 98 NVAFAlevtGVPPREI--------RKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190
....*....|....*....|....*....|
gi 1082420396 182 PNKYEIVHLLNNLSKTeNKTIIFSTHDLNI 211
Cdd:cd03292 170 DTTWEIMNLLKKINKA-GTTVVVATHAKEL 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-222 |
4.78e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.86 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIHNSLvSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSrADfaRL 87
Cdd:COG4525 4 LTVRHVSVRYPGGGQPQPAL-QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-AD--RG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFvsteivniNN------LRVFDLVALGrfphtnwfgkLEtkdLKSVSKA---------LEMVGMKSFVNKNINEISDG 152
Cdd:COG4525 80 VVF--------QKdallpwLNVLDNVAFG----------LR---LRGVPKAerraraeelLALVGLADFARRRIWQLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 153 ERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-236 |
5.12e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 105.68 E-value: 5.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISkriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:PRK11160 339 LTLNNVSFTYPDQ---PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEiVNINN--LRvfDLVALGrfphtnwfgkLETKDLKSVSKALEMVGMKSFVNKN------INE----ISDGERQ 155
Cdd:PRK11160 416 ISVVSQR-VHLFSatLR--DNLLLA----------APNASDEALIEVLQQVGLEKLLEDDkglnawLGEggrqLSGGEQR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 156 RVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-GAPED 234
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQIIEqGTHQE 559
|
..
gi 1082420396 235 LI 236
Cdd:PRK11160 560 LL 561
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-229 |
7.56e-25 |
|
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: 100.02 E-value: 7.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSFVSTEIV 96
Cdd:cd03301 5 NVTKRFGNVTaLDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRVFDLVALG----RFPhtnwfgKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:cd03301 83 LYPHMTVYDNIAFGlklrKVP------KDEID--ERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIwLMLNDSIIE 229
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRI-AVMNDGQIQ 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-235 |
1.17e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 102.53 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHN-SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI----------IGYSRADFA- 85
Cdd:COG1118 7 NISKRFGSfTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlpprerrVGFVFQHYAl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 -RlvsfvsteivninNLRVFDLVALG---RFPhtnwfGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIAR 161
Cdd:COG1118 87 fP-------------HMTVAENIAFGlrvRPP-----SKAEIR--ARVEELLELVQLEGLADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 162 TLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIwLMLNDSIIE--GAPEDL 235
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRV-VVMNQGRIEqvGTPDEV 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-228 |
1.77e-24 |
|
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: 99.27 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 16 GYHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS---IQGDILLNKKNIigySRADFARLVSFVS 92
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPR---KPDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 93 TEIVNINNLRV-----FDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGmksfvNKNINEISDGERQRVMIARTLAQDT 167
Cdd:cd03234 88 QDDILLPGLTVretltYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIG-----GNLVKGISGGERRRVSIAVQLLWDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTH----DLniaIQETDKIWLMLNDSII 228
Cdd:cd03234 163 KVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILTIHqprsDL---FRLFDRILLLSSGEIV 223
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
29-212 |
2.03e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 98.96 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLrVFDLVA 108
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHHL-LPDFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 109 LGRFPHTNWFGKLETKDLKSVSKA-LEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEI 187
Cdd:TIGR02211 101 LENVAMPLLIGKKSVKEAKERAYEmLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180
|
170 180
....*....|....*....|....*
gi 1082420396 188 VHLLNNLSKTENKTIIFSTHDLNIA 212
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHDLELA 205
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
28-236 |
2.41e-24 |
|
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: 103.64 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNlRVFDLV 107
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND-TIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRfphtnwfgkLETKDLKSVSKALEMVGMKSFVNK-----------NINEISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:TIGR02203 427 AYGR---------TEQADRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 177 AFLDLPNKYEIVHLLNNLskTENKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-GAPEDLI 236
Cdd:TIGR02203 498 SALDNESERLVQAALERL--MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVErGTHNELL 555
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-249 |
4.47e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.53 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLeigyhiSKRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRadfa 85
Cdd:COG1126 1 MIEIENL------HKSFGDLEVlKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKK---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 rlvsfvsteivNINNLR-----VFDLVALgrFPHtnwfgK--LE------TKDLKsVSKA---------LEMVGMKSFVN 143
Cdd:COG1126 71 -----------DINKLRrkvgmVFQQFNL--FPH-----LtvLEnvtlapIKVKK-MSKAeaeeramelLERVGLADKAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 144 KNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLML 223
Cdd:COG1126 132 AYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAK-EGMTMVVVTHEMGFAREVADRVVFMD 210
|
250 260
....*....|....*....|....*..
gi 1082420396 224 NDSIIE-GAPEdlilnetfnQIFDNSK 249
Cdd:COG1126 211 GGRIVEeGPPE---------EFFENPQ 228
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-209 |
5.09e-24 |
|
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: 97.70 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAA----LHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 L---VSFVSTEIVNINNLRVFDLVALG---RfphtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIA 160
Cdd:TIGR02673 77 LrrrIGVVFQDFRLLPDRTVYENVALPlevR-------GKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDL 209
Cdd:TIGR02673 150 RAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDL 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-222 |
6.11e-24 |
|
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: 97.37 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 19 ISKRiHNSLVSNINLTASEgELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLN-------KKNIIGYSRAdfaRLVSFV 91
Cdd:cd03297 6 IEKR-LPDFTLKIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsRKKINLPPQQ---RKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 92 steivninnlrvFDLVALgrFPHTN-----WFG---KLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTL 163
Cdd:cd03297 81 ------------FQQYAL--FPHLNvrenlAFGlkrKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 164 AQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM 205
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-222 |
1.02e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 101.59 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYhiskRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:TIGR02857 322 LEFSGVSVAY----PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTE--IVN---INNLRvfdlvalgrfphtnwFGKLETKDLkSVSKALEMVGMKSFVN-----------KNINEISD 151
Cdd:TIGR02857 398 IAWVPQHpfLFAgtiAENIR---------------LARPDASDA-EIREALERAGLDEFVAalpqgldtpigEGGAGLSG 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSktENKTIIFSTHDLNIAIqETDKIWLM 222
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-224 |
1.55e-23 |
|
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: 96.77 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigySRADFARLVSFVSTEIVNInnLRVFDLVAL 109
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRMVVFQNYSLLPW--LTVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 110 G---RFPHTNwfgklETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:TIGR01184 78 AvdrVLPDLS-----KSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1082420396 187 IVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLN 224
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTN 190
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
7-229 |
1.62e-23 |
|
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: 97.57 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHIS----KRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNII---GY 79
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 80 SRADFARLVSFVSTEIVNINNLRVFDLVALGRfPHTNWFGKLETKDLKSVSKALEMVGMKSFV-NKNINEISDGERQRVM 158
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGE-PLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
24-256 |
1.73e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 97.39 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 24 HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLqnsIQGD-ILLNKKNIIGYSRADFARL----------VSFVS 92
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDkSAGSHIELLGRTVQREGRLardirksranTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 93 TEIVNINNLRVFDLVALGRFPHT-------NWFGKLETKDlksVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ 165
Cdd:PRK09984 93 QQFNLVNRLSVLENVLIGALGSTpfwrtcfSWFTREQKQR---ALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILNETFNQIF 245
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLY 249
|
250
....*....|.
gi 1082420396 246 DnsklSFDRVK 256
Cdd:PRK09984 250 R----SINRVE 256
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-212 |
2.78e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKrIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:PRK11629 5 LLQCDNLCKRYQEGS-VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNINNLrVFDLVALGRFPHTNWFGKLETKDLKSvsKALEM---VGMKSFVNKNINEISDGERQRVMIARTL 163
Cdd:PRK11629 84 LRNQKLGFIYQFHHL-LPDFTALENVAMPLLIGKKKPAEINS--RALEMlaaVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082420396 164 AQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIA 212
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-236 |
2.81e-23 |
|
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: 96.25 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLeigyhiSKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRL 87
Cdd:cd03299 1 LKVENL------SKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEIVNINNLRVFDLVALGRFPHTNwfGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:cd03299 73 ISYVPQNYALFPHMTVYKNIAYGLKKRKV--DKKEIE--RKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDLI 236
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQvGKPEEVF 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
28-234 |
3.71e-23 |
|
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: 96.26 E-value: 3.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL---VSFvstEIVNI-NNLRV 103
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiaRTF---QNPRLfPELTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDLVALGRFPHT--NWFGKL---------ETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:COG0411 97 LENVLVAAHARLgrGLLAALlrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPED 234
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIaEGTPAE 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
28-233 |
3.92e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.01 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL----QNSIQ-GDILLNKKNIigysrADFARLVSFVsteIVNINN-- 100
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLllpeAGTITvGGMVLSEETV-----WDVRRQVGMV---FQNPDNqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 101 --LRVFDLVALGrfphtnwfgkLETKD------LKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK13635 95 vgATVQDDVAFG----------LENIGvpreemVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQeTDKIwLMLNDSII--EGAPE 233
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRV-IVMNKGEIleEGTPE 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
30-235 |
4.60e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.01 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfarlvsfvsteivNINNLR-----VF 104
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNK-------------KLKPLRkkvgiVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 dlvalgRFPH----------------TNwFGKLETKDLKSVSKALEMVGM-KSFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:PRK13634 92 ------QFPEhqlfeetvekdicfgpMN-FGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDL 235
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFlQGTPREI 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
6-235 |
1.44e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 6 HILEIHnlEIGYHISKRIHnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIiGYSRADFA 85
Cdd:PRK13636 4 YILKVE--ELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RLVSFVSTEIVNINN----LRVFDLVALGRFPhtnwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIAR 161
Cdd:PRK13636 79 KLRESVGMVFQDPDNqlfsASVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 162 TLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDL 235
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVIlQGNPKEV 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-222 |
5.18e-22 |
|
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: 91.84 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS--IQGDILLNKKNIigySRADFARLVSFVSTEIVNINNLRVF 104
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DlvalgrfphTNWFgkletkdlksvskALEMVGmksfvnknineISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNK 184
Cdd:cd03213 101 E---------TLMF-------------AAKLRG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 1082420396 185 YEIVHLLNNLSKTeNKTIIFSTHDLNIAIQET-DKIWLM 222
Cdd:cd03213 148 LQVMSLLRRLADT-GRTIICSIHQPSSEIFELfDKLLLL 185
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
27-238 |
6.94e-22 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 92.43 E-value: 6.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS----IQGDILLNKKNIIGYS-RAdfaRLVSFVS-------TE 94
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPLSiRG---RHIATIMqnprtafNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 IVNINNLRVFDLVALGrfphtnwfgKLETKDLKSVSKALEMVGM---KSFVNKNINEISDGERQRVMIARTLAQDTPVIV 171
Cdd:TIGR02770 78 LFTMGNHAIETLRSLG---------KLSKQARALILEALEAVGLpdpEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 172 LDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDLILN 238
Cdd:TIGR02770 149 ADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVErGTVKEIFYN 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-235 |
1.07e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigysradfar 86
Cdd:PRK11607 19 LLEIRNLTKSFD-----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 lvSFVSTEIVNINNLrvFDLVALgrFPHTN-----WFG----KLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQR 156
Cdd:PRK11607 84 --SHVPPYQRPINMM--FQSYAL--FPHMTveqniAFGlkqdKLPKAEIASrVNEMLGLVHMQEFAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 157 VMIARTLAQDTPVIVLDEPTAFLD--LPNK--YEIVHLLNNLSktenKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GA 231
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDkkLRDRmqLEVVDILERVG----VTCVMVTHDQEEAMTMAGRIAIMNRGKFVQiGE 233
|
....
gi 1082420396 232 PEDL 235
Cdd:PRK11607 234 PEEI 237
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
28-237 |
2.53e-21 |
|
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: 90.75 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVnINNLRVFDLV 107
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTF-LFSGTIMENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRfphtnwfgklETKDLKSVSKALEMVGMKSFVNK-------NINE----ISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:cd03254 98 RLGR----------PNATDEEVIEAAKEAGAHDFIMKlpngydtVLGEnggnLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 177 AFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNIaIQETDKIWLMLNDSIIE-GAPEDLIL 237
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMK--GRTSIIIAHRLST-IKNADKILVLDDGKIIEeGTHDELLA 226
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-238 |
3.10e-21 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 92.08 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSL--VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI-----------IGYsradf 84
Cdd:COG1125 6 NVTKRYPDGTvaVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIrdldpvelrrrIGY----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 85 arlvsfVsteIVNInnlrvfdlvalGRFPHtnwfgkLETKD-------LKSVSKA---------LEMVGM--KSFVNKNI 146
Cdd:COG1125 81 ------V---IQQI-----------GLFPH------MTVAEniatvprLLGWDKErirarvdelLELVGLdpEEYRDRYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 147 NEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDlPnkyeIV-----HLLNNLSKTENKTIIFSTHDLNIAIQETDKIWL 221
Cdd:COG1125 135 HELSGGQQQRVGVARALAADPPILLMDEPFGALD-P----ITreqlqDELLRLQRELGKTIVFVTHDIDEALKLGDRIAV 209
|
250
....*....|....*....
gi 1082420396 222 MlNDSIIE--GAPEDLILN 238
Cdd:COG1125 210 M-REGRIVqyDTPEEILAN 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-235 |
7.30e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 91.70 E-value: 7.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 2 ETRKHILEIHNleigyhISKRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS 80
Cdd:PRK11432 1 MTQKNFVVLKN------ITKRFGSNTViDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 radfarlvsfvsteIVNINNLRVFDLVALgrFPHTNW------------FGKLETKdlKSVSKALEMVGMKSFVNKNINE 148
Cdd:PRK11432 75 --------------IQQRDICMVFQSYAL--FPHMSLgenvgyglkmlgVPKEERK--QRVKEALELVDLAGFEDRYVDQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 149 ISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII 228
Cdd:PRK11432 137 ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
....*...
gi 1082420396 229 E-GAPEDL 235
Cdd:PRK11432 217 QiGSPQEL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-210 |
8.55e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNleigyhISKRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFA 85
Cdd:COG1129 4 LLEMRG------ISKSFGGVKAlDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RL-VSFVSTEIVNINNLRVFDLVALGRFPHTnwFGKLETKDLKSVSKA-LEMVGMKSFVNKNINEISDGERQRVMIARTL 163
Cdd:COG1129 78 AAgIAIIHQELNLVPNLSVAENIFLGREPRR--GGLIDWRAMRRRARElLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082420396 164 AQDTPVIVLDEPTAFLDlpnKYEIVHLLNNLS--KTENKTIIFSTHDLN 210
Cdd:COG1129 156 SRDARVLILDEPTASLT---EREVERLFRIIRrlKAQGVAIIYISHRLD 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-238 |
8.63e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.77 E-value: 8.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNleigyhISKRI-HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNkkniiGYSradfa 85
Cdd:PRK09493 1 MIEFKN------VSKHFgPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-----GLK----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 rlvsfVSTEIVNINNLR-----VFDLVALgrFPHTN-----WFGKLETK-----DLKSVSKAL-EMVGMKSFVNKNINEI 149
Cdd:PRK09493 65 -----VNDPKVDERLIRqeagmVFQQFYL--FPHLTalenvMFGPLRVRgaskeEAEKQARELlAKVGLAERAHHYPSEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 150 SDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSkTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:PRK09493 138 SGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
250
....*....|
gi 1082420396 230 -GAPEDLILN 238
Cdd:PRK09493 217 dGDPQVLIKN 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-222 |
9.90e-21 |
|
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: 88.96 E-value: 9.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRI-----HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLvSFVS 92
Cdd:cd03266 6 ALTKRFrdvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL-GFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 93 teivniNNLRVFD-------LVALGRFphtnwFGkLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVMIARTLA 164
Cdd:cd03266 85 ------DSTGLYDrltarenLEYFAGL-----YG-LKGDELTArLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 165 QDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVL 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
28-236 |
1.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.05 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNkkniiGYSRADFARLVSFvsTEIVNInnlrVFdlv 107
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS-----GIDTGDFSKLQGI--RKLVGI----VF--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 algRFPHTNWFGKLETKDL---------------KSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK13644 84 ---QNPETQFVGRTVEEDLafgpenlclppieirKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 173 DEPTAFLDlPNKYEIVhlLNNLSK--TENKTIIFSTHDLNiAIQETDKIWLMLNDSII-EGAPEDLI 236
Cdd:PRK13644 161 DEVTSMLD-PDSGIAV--LERIKKlhEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVlEGEPENVL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-238 |
1.26e-20 |
|
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: 92.44 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRI------HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSiQGDILLNKKNIIGYS 80
Cdd:COG4172 275 LLEARDLKVWFPIKRGLfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARLVSFVstEIV------NIN-NLRVFDLVALGRFPHTNWFGKLETKDLksVSKALEMVGMK-SFVNKNINEISDG 152
Cdd:COG4172 354 RRALRPLRRRM--QVVfqdpfgSLSpRMTVGQIIAEGLRVHGPGLSAAERRAR--VAEALEEVGLDpAARHRYPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 153 ERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNI--AIqeTDKIWLMLNDSIIEG 230
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVvrAL--AHRVMVMKDGKVVEQ 507
|
....*...
gi 1082420396 231 APEDLILN 238
Cdd:COG4172 508 GPTEQVFD 515
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-235 |
1.26e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.18 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQG-----DILL---NKKNIIGYSRADFARLVSFVSTEIVNINNL 101
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVsstSKQKEIKPVRKKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 102 RVfdlVALGrfPHTnwFGKLETKDLKSVSKALEMVGM-KSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLD 180
Cdd:PRK13643 104 KD---VAFG--PQN--FGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 181 LPNKYEIVHLLNNLSKTeNKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDL 235
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIIScGTPSDV 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-244 |
1.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 89.72 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSradfarlvsfvsteiVNINNLR-----VF 104
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK---------------VKLSDIRkkvglVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 dlvalgRFPHTNWFGKLETKDL---------------KSVSKALEMVGMK--SFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:PRK13637 90 ------QYPEYQLFEETIEKDIafgpinlglseeeieNRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEdlilnETFNQI 244
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCElQGTPR-----EVFKEV 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-241 |
1.59e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 5 KHILEIHNLEIGYHIsKRIHNslvsnINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADf 84
Cdd:PRK13651 6 KNIVKIFNKKLPTEL-KALDN-----VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 85 arLVSFVSTEIV----------NINNLR-----VFDLVALGRFPHTN----WFG-------KLETKdlKSVSKALEMVGM 138
Cdd:PRK13651 79 --EKEKVLEKLViqktrfkkikKIKEIRrrvgvVFQFAEYQLFEQTIekdiIFGpvsmgvsKEEAK--KRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 139 -KSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETD 217
Cdd:PRK13651 155 dESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTK 233
|
250 260
....*....|....*....|....*
gi 1082420396 218 KIWLMLNDSII-EGAPEDLILNETF 241
Cdd:PRK13651 234 RTIFFKDGKIIkDGDTYDILSDNKF 258
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
17-225 |
2.15e-20 |
|
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: 87.66 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 17 YHISKRI-HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNiIGYSRADFARLVSFVSTEI 95
Cdd:cd03268 4 NDLTKTYgKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 96 VNIN-----NLRVFDLVALGRFphtnwfgkletkdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVI 170
Cdd:cd03268 83 FYPNltareNLRLLARLLGIRK--------------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 171 VLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNiAIQETDKIWLMLND 225
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLS-EIQKVADRIGIINK 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-219 |
2.44e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.85 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNleIGYHISKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS 80
Cdd:PRK10247 1 MQENSPLLQLQN--VGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARLVSFvSTEIVNINNLRVFDLVAlgrFPhtnWFGKLETKDLKSVSKALEMVGM-KSFVNKNINEISDGERQRVMI 159
Cdd:PRK10247 76 PEIYRQQVSY-CAQTPTLFGDTVYDNLI---FP---WQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 160 ARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNiAIQETDKI 219
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD-EINHADKV 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
31-212 |
2.53e-20 |
|
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: 88.26 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS---RADF-ARLVSFVSTEIVNINNLRVFDL 106
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLrARHVGFVFQSFQLLPTLTALEN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALgrfPhtnwfgkLE---TKDLKSVSKA-LEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLP 182
Cdd:COG4181 111 VML---P-------LElagRRDARARARAlLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAA 180
|
170 180 190
....*....|....*....|....*....|
gi 1082420396 183 NKYEIVHLLNNLSKTENKTIIFSTHDLNIA 212
Cdd:COG4181 181 TGEQIIDLLFELNRERGTTLVLVTHDPALA 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-214 |
3.37e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.72 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 32 NLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNiigYSRADFA-RLVSFVSTEivniNNL----RVFDL 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD---HTTTPPSrRPVSMLFQE----NNLfshlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALGRFPHTnwfgKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:PRK10771 92 IGLGLNPGL----KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180
....*....|....*....|....*...
gi 1082420396 187 IVHLLNNLSKTENKTIIFSTHDLNIAIQ 214
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAAR 195
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
28-235 |
3.40e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 89.75 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSFVSTEIVNINNLRVFDLV 107
Cdd:COG3839 19 LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMVFQSYALYPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALG----RFPhtnwfgKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDlpn 183
Cdd:COG3839 97 AFPlklrKVP------KAEID--RRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD--- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 184 kY--------EIVHLLNNLskteNKTIIFSTHD----LNIAiqetDKIwLMLNDSIIE--GAPEDL 235
Cdd:COG3839 166 -AklrvemraEIKRLHRRL----GTTTIYVTHDqveaMTLA----DRI-AVMNDGRIQqvGTPEEL 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-247 |
4.93e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 89.40 E-value: 4.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNkkniiGYSRADFARLVsFVSTEIVNINnlRVFDLVALg 110
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-----GRTLFDSRKGI-FLPPEKRRIG--YVFQEARL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 111 rFPHTNWFGKLE------TKDLKSVS--KALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLP 182
Cdd:TIGR02142 87 -FPHLSVRGNLRygmkraRPSERRISfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 183 NKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIFDN 247
Cdd:TIGR02142 166 RKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAaAGPIAEVWASPDLPWLARE 231
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
30-222 |
5.23e-20 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 87.00 E-value: 5.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR-------------LVSFVSTEiv 96
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQlrrrigyifqahnLLGFLTAR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 niNNLRVfdlvALGRFPHTNWfgkletKDLKSVSKA-LEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEP 175
Cdd:TIGR02982 101 --QNVQM----ALELQPNLSY------QEARERARAmLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082420396 176 TAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHD---LNIAiqetDKIWLM 222
Cdd:TIGR02982 169 TAALDSKSGRDVVELMQKLAKEQGCTILMVTHDnriLDVA----DRILQM 214
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
28-236 |
6.46e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 86.90 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVnINNLRVFDLV 107
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVF-LFNDTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRFPHTnwfgkletkdLKSVSKALEMVGMKSFVNK-------NINE----ISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:cd03251 97 AYGRPGAT----------REEVEEAARAANAHEFIMElpegydtVIGErgvkLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 177 AFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-GAPEDLI 236
Cdd:cd03251 167 SALDTESERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKIVErGTHEELL 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-219 |
8.01e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 8.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKrihnslvsNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVSFvsteivn 97
Cdd:PRK11000 17 VISK--------DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGM------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 98 innlrVFDLVALgrFPHTNW-----FG-KLETKDL----KSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:PRK11000 80 -----VFQSYAL--YPHLSVaenmsFGlKLAGAKKeeinQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKI 219
Cdd:PRK11000 153 SVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKI 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-224 |
8.45e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 87.48 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 5 KHILEIHNLEIGYHISKriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADF 84
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQ--EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 85 ARLVSFVsteIVNINN----LRVFDLVALGrfphtnwfgkLETKDL------KSVSKALEMVGMKSFVNKNINEISDGER 154
Cdd:PRK13650 80 RHKIGMV---FQNPDNqfvgATVEDDVAFG----------LENKGIpheemkERVNEALELVGMQDFKEREPARLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 155 QRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNiAIQETDKIWLMLN 224
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKN 215
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
8-235 |
1.49e-19 |
|
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: 85.56 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGY---HIskrihnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADF 84
Cdd:cd03224 1 LEVENLNAGYgksQI--------LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 85 ARL-VSFVsTEIVNI-NNLRVFDLVALGRFPHTNwfgkletkdlKSVSKALEMV-GM----KSFVNKNINEISDGERQRV 157
Cdd:cd03224 73 ARAgIGYV-PEGRRIfPELTVEENLLLGAYARRR----------AKRKARLERVyELfprlKERRKQLAGTLSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 158 MIARTLAQDTPVIVLDEPTA-----FLDlpnkyEIVHLLNNLSKTEnKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGA 231
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEglapkIVE-----EIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVlEGT 215
|
....
gi 1082420396 232 PEDL 235
Cdd:cd03224 216 AAEL 219
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
1.77e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.73 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHISKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS 80
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQSDASF---TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARLVSFVSTEIVN--INNLRVFDlVALGRFPHTnwfgkLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRV 157
Cdd:PRK13648 78 FEKLRKHIGIVFQNPDNqfVGSIVKYD-VAFGLENHA-----VPYDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIqETDKIwLMLNDSII--EGAPEDL 235
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM-EADHV-IVMNKGTVykEGTPTEI 229
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-239 |
2.34e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGysRADFAR 86
Cdd:PRK13537 7 PIDFRNVEKRYG-----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNIN-------NLRVFdlvalGRFphtnwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMI 159
Cdd:PRK13537 80 QRVGVVPQFDNLDpdftvreNLLVF-----GRY-----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 160 ARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLND-SIIEGAPEDLILN 238
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGrKIAEGAPHALIES 228
|
.
gi 1082420396 239 E 239
Cdd:PRK13537 229 E 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
19-222 |
2.56e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.88 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 19 ISKRIHNSLVSN-INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNK---KNIIGYSRADF--ARLVSFVs 92
Cdd:PRK11247 18 VSKRYGERTVLNqLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplAEAREDTRLMFqdARLLPWK- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 93 teivninnlRVFDLVALGrfphtnWFGKLETKDLKsvskALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK11247 97 ---------KVIDNVGLG------LKGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLI 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-232 |
2.60e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.89 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYH----ISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRA 82
Cdd:PRK10419 3 LLNVSGLSHHYAhgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 83 D---FARLVSFVSTEIVNINNLRvFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMK-SFVNKNINEISDGERQRVM 158
Cdd:PRK10419 83 QrkaFRRDIQMVFQDSISAVNPR-KTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAP 232
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-235 |
2.75e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.37 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSfvstEIVNInnlrVFdlv 107
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVR----KRIGM----VF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 algRFPHTNWFGKLETKDL----KSVSKALEMVGMKSF-------VNKNINE-----ISDGERQRVMIARTLAQDTPVIV 171
Cdd:PRK13646 92 ---QFPESQLFEDTVEREIifgpKNFKMNLDEVKNYAHrllmdlgFSRDVMSqspfqMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 172 LDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDL 235
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSqTSPKEL 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-225 |
3.25e-19 |
|
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: 82.50 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYsradFARL 87
Cdd:cd03221 1 IELENLSKTYG-----GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGY----FEQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 vsfvsteivninnlrvfdlvalgrfphtnwfgkletkdlksvskalemvgmksfvnknineiSDGERQRVMIARTLAQDT 167
Cdd:cd03221 72 --------------------------------------------------------------SGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 168 PVIVLDEPTAFLDLPNkyeiVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLND 225
Cdd:cd03221 90 NLLLLDEPTNHLDLES----IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-212 |
3.41e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.83 E-value: 3.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHnleigyHISKRIHN-----SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY-- 79
Cdd:PRK10584 6 IVEVH------HLKKSVGQgehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMde 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 80 -SRADF-ARLVSFVSTE---IVNINNLRVFDLVALGRfphtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGER 154
Cdd:PRK10584 80 eARAKLrAKHVGFVFQSfmlIPTLNALENVELPALLR-------GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 155 QRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIA 212
Cdd:PRK10584 153 QRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
28-235 |
3.58e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLvSFVSTeivnINNLRVFD-- 105
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRT----FQHVRLFRem 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 ------LVALGRFPHTNWFGKL---------ETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVI 170
Cdd:PRK11300 96 tvienlLVAQHQQLKTGLFSGLlktpafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 171 VLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM-LNDSIIEGAPEDL 235
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVnQGTPLANGTPEEI 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-242 |
3.69e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 3 TRKHILEIHNLEIGyhiskrihnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRA 82
Cdd:PRK10070 30 SKEQILEKTGLSLG-----------VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 83 DFARL----VSFVSTEIVNINNLRVFDLVALGrfphTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVM 158
Cdd:PRK10070 99 ELREVrrkkIAMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILN 238
Cdd:PRK10070 175 LARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
....
gi 1082420396 239 ETFN 242
Cdd:PRK10070 255 NPAN 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-229 |
3.87e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.20 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 5 KHILEIHNLEIGYHiSKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY---SR 81
Cdd:COG0488 313 KKVLELEGLSKSYG-DKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYfdqHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 82 ADFArlvsfvsteivniNNLRVFDLVALGRfphtnwfgklETKDLKSVSKALEmvgmkSF------VNKNINEISDGERQ 155
Cdd:COG0488 388 EELD-------------PDKTVLDELRDGA----------PGGTEQEVRGYLG-----RFlfsgddAFKPVGVLSGGEKA 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 156 RVMIARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHD---LN-IAiqetDKIWLMLNDSIIE 229
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDryfLDrVA----TRILEFEDGGVRE 509
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-222 |
4.02e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.68 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHI--------SKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLN 72
Cdd:PRK15079 2 TEGKKVLLEVADLKVHFDIkdgkqwfwQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 73 KKNIIGYSRADFARlvsfVSTEIVNIN-------NLR--VFDLVALgrfPHTNWFGKLETKDLKSVSKALEM-VGM-KSF 141
Cdd:PRK15079 82 GKDLLGMKDDEWRA----VRSDIQMIFqdplaslNPRmtIGEIIAE---PLRTYHPKLSRQEVKDRVKAMMLkVGLlPNL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 142 VNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWL 221
Cdd:PRK15079 155 INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 234
|
.
gi 1082420396 222 M 222
Cdd:PRK15079 235 M 235
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
43-235 |
5.40e-19 |
|
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: 86.01 E-value: 5.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 43 VIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIgysradfarlvsFVSTEIVNINNlrVFDLVALgrFPHTNWFG--- 119
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------------NVPPHLRHINM--VFQSYAL--FPHMTVEEnva 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 120 ------KLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLN 192
Cdd:TIGR01187 65 fglkmrKVPRAEIKPrVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1082420396 193 NLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDL 235
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQiGTPEEI 188
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-213 |
6.03e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 84.75 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSrADfaRLVSFVSTEIVNINNlrVFDLVA 108
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-AE--RGVVFQNEGLLPWRN--VQDNVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 109 LGrfphtnwfgkLEtkdLKSVSK------ALEM---VGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:PRK11248 93 FG----------LQ---LAGVEKmqrleiAHQMlkkVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190
....*....|....*....|....*....|....
gi 1082420396 180 DLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAI 213
Cdd:PRK11248 160 DAFTREQMQTLLLKLWQETGKQVLLITHDIEEAV 193
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-207 |
6.08e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 84.69 E-value: 6.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAG--LQNSIQGDILLNKKNIIG 78
Cdd:CHL00131 1 MNKNKPILEIKNLHASVN-----ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 79 YSRADFARLVSFVS----TEIVNINNLRVFDLVALGRFPHTNwfgkLETKD----LKSVSKALEMVGMK-SFVNKNINE- 148
Cdd:CHL00131 76 LEPEERAHLGIFLAfqypIEIPGVSNADFLRLAYNSKRKFQG----LPELDplefLEIINEKLKLVGMDpSFLSRNVNEg 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 149 ISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTH 207
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITH 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
22-239 |
6.18e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.20 E-value: 6.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 22 RIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRA---DFARLVSFVSTEIVNI 98
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 99 NNLRVFDLVALGRFPHTNwfgkLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTA 177
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTQ----LPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 178 FLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNE 239
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVaHGSAQALQANP 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
7-241 |
6.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.06 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLnKKNIIGYSRADFAR 86
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNINNLR-----VFdlvalgRFPHTNWFGKLETKDL---------------KSVSKALEMVGMK-SFVNKN 145
Cdd:PRK13631 100 ITNPYSKKIKNFKELRrrvsmVF------QFPEYQLFKDTIEKDImfgpvalgvkkseakKLAKFYLNKMGLDdSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 146 INEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNlSKTENKTIIFSTHDLNIAIQETDKIWLMLND 225
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*..
gi 1082420396 226 SIIE-GAPEDLILNETF 241
Cdd:PRK13631 253 KILKtGTPYEIFTDQHI 269
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-210 |
6.33e-19 |
|
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: 84.09 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSL---VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIiGYSRADFARLVSFVSTE 94
Cdd:cd03263 5 NLTKTYKKGTkpaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 IVNINNLRVFDLVAL-GRFPhtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLD 173
Cdd:cd03263 84 DALFDELTVREHLRFyARLK-----GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1082420396 174 EPTAFLDLPNKYEIVHLLnnLSKTENKTIIFSTHDLN 210
Cdd:cd03263 159 EPTSGLDPASRRAIWDLI--LEVRKGRSIILTTHSMD 193
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-232 |
6.56e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.58 E-value: 6.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKrihnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL-----QNSIQGDILLNKKNIIGYSRA 82
Cdd:PRK14247 4 IEIRDLKVSFGQVE-----VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 83 DFARLVSFVsTEIVN-INNLRVFDLVALGrfPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNIN----EISDGERQRV 157
Cdd:PRK14247 79 ELRRRVQMV-FQIPNpIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAP 232
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-235 |
8.51e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 8.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ--LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVN-INNLRVFDLVALGRFPHtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ 165
Cdd:PRK13642 82 KIGMVFQNPDNqFVGATVEDDVAFGMENQ----GIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAiQETDKIWLMLNDSII-EGAPEDL 235
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIkEAAPSEL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-210 |
8.99e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 8.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRiHNSLVSN--INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL-VSFVSTE 94
Cdd:COG3845 10 GITKR-FGGVVANddVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 IVNINNLRVFDLVALGRFPHTNWFGKLET--KDLKSVSKALemvGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:COG3845 89 FMLVPNLTVAENIVLGLEPTKGGRLDRKAarARIRELSERY---GLDVDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1082420396 173 DEPTAFLDLPnkyEIVHLLNNLS--KTENKTIIFSTHDLN 210
Cdd:COG3845 166 DEPTAVLTPQ---EADELFEILRrlAAEGKSIIFITHKLR 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
27-222 |
9.23e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 82.26 E-value: 9.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIvninNLrvfdl 106
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD----EL----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 valgrFPHTnwfgkletkdlksvskalemvgmksfVNKNIneISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:cd03246 88 -----FSGS--------------------------IAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082420396 187 IVHLLNNLSKtENKTIIFSTHDLNiAIQETDKIWLM 222
Cdd:cd03246 135 LNQAIAALKA-AGATRIVIAHRPE-TLASADRILVL 168
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
28-235 |
1.20e-18 |
|
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: 83.19 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRaDFARLVSFVSTEIVNINNLRVFDlv 107
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDELTGWE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 algrfpHTNWFGKLE----TKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPN 183
Cdd:cd03265 93 ------NLYIHARLYgvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 184 KYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDL 235
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIaEGTPEEL 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-236 |
1.42e-18 |
|
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: 83.43 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:cd03253 1 IEFENVTFAYDPGRPV----LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEIVNINNlRVFDLVALGRFPHTNwfgkletKDLKSVSKAL----EMVGMKSFVNKNINE----ISDGERQRVMI 159
Cdd:cd03253 77 IGVVPQDTVLFND-TIGYNIRYGRPDATD-------EEVIEAAKAAqihdKIMRFPDGYDTIVGErglkLSGGEKQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 160 ARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-GAPEDLI 236
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLS-TIVNADKIIVLKDGRIVErGTHEELL 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-219 |
2.45e-18 |
|
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: 80.94 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNkkniigysradfarlvsfvsTEIV 96
Cdd:cd03216 5 GITKRFGGVKAlDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--------------------GKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRvfDLVALGrfphtnwfgkletkdlksvskalemVGMksfvnknINEISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:cd03216 65 SFASPR--DARRAG-------------------------IAM-------VYQLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1082420396 177 AFLDLPnkyEIVHLLNNLS--KTENKTIIFSTHDLNIAIQETDKI 219
Cdd:cd03216 111 AALTPA---EVERLFKVIRrlRAQGVAVIFISHRLDEVFEIADRV 152
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-212 |
2.65e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLV---SFVSTEIVNINNLRv 103
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLghrNAMKPALTVAENLE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FdlvalgrfphtnWFGKLETKDLkSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLpn 183
Cdd:PRK13539 96 F------------WAAFLGGEEL-DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA-- 160
|
170 180 190
....*....|....*....|....*....|...
gi 1082420396 184 kyEIVHLLNNLSKT---ENKTIIFSTH-DLNIA 212
Cdd:PRK13539 161 --AAVALFAELIRAhlaQGGIVIAATHiPLGLP 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-225 |
3.38e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 85.18 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIV--------NI 98
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVElfdgtiaeNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 99 nnlrvfdlvalGRFPhtnwfgklETKDLKsVSKALEMVGMKSFVNK-------NINE----ISDGERQRVMIARTLAQDT 167
Cdd:COG4618 427 -----------ARFG--------DADPEK-VVAAAKLAGVHEMILRlpdgydtRIGEggarLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 168 PVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIaIQETDKIwLMLND 225
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSL-LAAVDKL-LVLRD 541
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-236 |
3.44e-18 |
|
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: 85.24 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGD---------ILL 71
Cdd:TIGR03269 273 VEVGEPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnvrvgdewVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 72 NKKNIIGYSRAdfARLVSFVSTEivninnlrvFDLvalgrFPHTNWFGKL------ETKDLKSVSKA---LEMVGM---- 138
Cdd:TIGR03269 353 TKPGPDGRGRA--KRYIGILHQE---------YDL-----YPHRTVLDNLteaiglELPDELARMKAvitLKMVGFdeek 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 139 -KSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETD 217
Cdd:TIGR03269 417 aEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCD 496
|
250 260
....*....|....*....|
gi 1082420396 218 KIWLMLNDSIIE-GAPEDLI 236
Cdd:TIGR03269 497 RAALMRDGKIVKiGDPEEIV 516
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-211 |
8.82e-18 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.86 E-value: 8.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHISKRI------HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKK 74
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 75 NIIGYSRADFARL------V---SFVSteivnIN-NLRVFDLVAlgrFPHTNwFGKLETKDLKS-VSKALEMVGMK-SFV 142
Cdd:COG4608 81 DITGLSGRELRPLrrrmqmVfqdPYAS-----LNpRMTVGDIIA---EPLRI-HGLASKAERRErVAELLELVGLRpEHA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 143 NKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNI 211
Cdd:COG4608 152 DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSV 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-240 |
1.06e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL-------QNSIQGD-ILLNKKNIig 78
Cdd:PRK13640 5 IVEFKHVSFTYPDSKK---PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpNSKITVDgITLTAKTV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 79 ysrADFARLVSFVsteIVNINN----LRVFDLVALGrfphtnwfgkLETKD------LKSVSKALEMVGMKSFVNKNINE 148
Cdd:PRK13640 80 ---WDIREKVGIV---FQNPDNqfvgATVGDDVAFG----------LENRAvprpemIKIVRDVLADVGMLDYIDSEPAN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 149 ISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII 228
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
250
....*....|..
gi 1082420396 229 EGAPEDLILNET 240
Cdd:PRK13640 224 QGSPVEIFSKVE 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-238 |
1.22e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 82.43 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSLvSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFaR 86
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSEREL-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LV---------SFvsteivninNL---R-VFDLVAlgrFPhtnwfgkLEtkdLKSVSKA---------LEMVGMKSFVNK 144
Cdd:COG1135 79 AArrkigmifqHF---------NLlssRtVAENVA---LP-------LE---IAGVPKAeirkrvaelLELVGLSDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 145 NINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIaIQET-DKIWLML 223
Cdd:COG1135 137 YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDV-VRRIcDRVAVLE 215
|
250
....*....|....*.
gi 1082420396 224 NDSIIE-GAPEDLILN 238
Cdd:COG1135 216 NGRIVEqGPVLDVFAN 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-229 |
1.30e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiSKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS-----IQGDILLNKKNIIgysR 81
Cdd:PRK15134 5 LLAIENLSVAFR-QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLL---H 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 82 ADFARL-------VSFVSTE-IVNINNL-----RVFDLVALGRfphtnwfGKLETKDLKSVSKALEMVGM---KSFVNKN 145
Cdd:PRK15134 81 ASEQTLrgvrgnkIAMIFQEpMVSLNPLhtlekQLYEVLSLHR-------GMRREAARGEILNCLDRVGIrqaAKRLTDY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 146 INEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLND 225
Cdd:PRK15134 154 PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
....
gi 1082420396 226 SIIE 229
Cdd:PRK15134 234 RCVE 237
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-236 |
1.56e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 83.53 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTllrnIAGLQNSI----QGDILLNKKNIIGYSRADFARLVSFVSTEiVNINNLRVF 104
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKST----IANLLTRFydidEGEILLDGHDLRDYTLASLRNQVALVSQN-VHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DLVALGRfphTNWFGKLETKDLKSVSKALEMV-----GMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:PRK11176 435 NNIAYAR---TEQYSREQIEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 180 DLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-GAPEDLI 236
Cdd:PRK11176 512 DTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEILVVEDGEIVErGTHAELL 566
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
30-235 |
1.74e-17 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 82.07 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLN-------KKNI--------IGYSRADfARLvsfvste 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdsARGIflpphrrrIGYVFQE-ARL------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 ivninnlrvfdlvalgrFPH----TN-----WFGKlETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ 165
Cdd:COG4148 89 -----------------FPHlsvrGNllygrKRAP-RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDL 235
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVaSGPLAEV 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
28-222 |
1.84e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL-VSFVSTEIVNINNLRVFDL 106
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALGRFPHTNWFGK--LETKDLKSV-SKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAflDLPN 183
Cdd:PRK09700 101 LYIGRHLTKKVCGVniIDWREMRVRaAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS--SLTN 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1082420396 184 K-YEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK09700 179 KeVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVM 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
30-239 |
2.64e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 79.84 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNlRVFDLVAL 109
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SIRDNIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 110 GRfphtnwfgklETKDLKSVSKALEMVGMKSF-----------VNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAF 178
Cdd:cd03252 99 AD----------PGMSMERVIEAAKLAGAHDFiselpegydtiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 179 LDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIEGAPEDLILNE 239
Cdd:cd03252 169 LDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-232 |
2.92e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.44 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIiGYSRADFARLVSFVSTeIVNINNLRVF-- 104
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVAT-VFQDPEQQIFyt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DLVALGRFPHTNwFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNK 184
Cdd:PRK13638 94 DIDSDIAFSLRN-LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082420396 185 YEIVHLLNNLSKTENKTIIfSTHDLNIAIQETDKIWLMLNDSII-EGAP 232
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILtHGAP 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-236 |
2.95e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.42 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDIllnkkNIIGY---SRADFARLVSFVSTEIVNIN---- 99
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-----TVLGVpvpARARLARARIGVVPQFDNLDleft 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 ---NLRVFdlvalGRFphtnwFGkLETKDLKSV-SKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEP 175
Cdd:PRK13536 131 vreNLLVF-----GRY-----FG-MSTREIEAViPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 176 TAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLND-SIIEGAPEDLI 236
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGrKIAEGRPHALI 260
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-229 |
4.86e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.94 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIvninnlRVFDLV 107
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDF------HLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 aLGrfphtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISD-----GERQRVMIARTLAQDTPVIVLDEPTAFLDLP 182
Cdd:PRK10522 413 -LG--------PEGKPANPALVEKWLERLKMAHKLELEDGRISNlklskGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1082420396 183 NKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQeTDKIWLMLNDSIIE 229
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
8-180 |
5.23e-17 |
|
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: 78.17 E-value: 5.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLeigyhISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNiIGYSRADFARL 87
Cdd:TIGR01189 1 LAARNL-----ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-LAEQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSF------VSTEIVNINNLRvfdlvalgrfphtnWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIAR 161
Cdd:TIGR01189 75 ILYlghlpgLKPELSALENLH--------------FWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALAR 140
|
170
....*....|....*....
gi 1082420396 162 TLAQDTPVIVLDEPTAFLD 180
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALD 159
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
9-207 |
5.98e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 80.62 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 9 EIHNLEIGYHISKRIHNSLvSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADF--AR 86
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHAL-NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LvsfvsteivNIN------NL----RVFDLVAlgrFPHT--NWfGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGER 154
Cdd:PRK11153 82 R---------QIGmifqhfNLlssrTVFDNVA---LPLElaGT-PKAEIK--ARVTELLELVGLSDKADRYPAQLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 155 QRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTH 207
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
19-232 |
8.02e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.64 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 19 ISKRIHNSLVSN-INLTASEGELIAVIGKNGVGKSTLLRNIAGLQN----SIQ-GDILLNKKNIIGYSRADFARL---VS 89
Cdd:PRK11264 9 LVKKFHGQTVLHgIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagTIRvGDITIDTARSLSQQKGLIRQLrqhVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 90 FVsteivninnLRVFDLvalgrFPHTNWFG---------KLETKDlKSVSKALEM---VGMKSFVNKNINEISDGERQRV 157
Cdd:PRK11264 89 FV---------FQNFNL-----FPHRTVLEniiegpvivKGEPKE-EATARARELlakVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAP 232
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQ-EKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGP 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
5-253 |
8.41e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 5 KHILEIHNLEIGYHISKRIHNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILL------NKKNII 77
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESTEKLaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVdgldtsDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 78 GYSRAdfARLV------SFVSTeIVNINnlrvfdlVALGrfPHTNWFGKLETKdlKSVSKALEMVGMKSFVNKNINEISD 151
Cdd:PRK13633 82 DIRNK--AGMVfqnpdnQIVAT-IVEED-------VAFG--PENLGIPPEEIR--ERVDESLKKVGMYEYRRHAPHLLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIqETDKIWLMLNDSII-EG 230
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVMDSGKVVmEG 226
|
250 260
....*....|....*....|...
gi 1082420396 231 APEdlilnETFNQIFDNSKLSFD 253
Cdd:PRK13633 227 TPK-----EIFKEVEMMKKIGLD 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
31-238 |
9.62e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 9.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigysradfaRLV--SFVSTEIVNINNLRVFDLVA 108
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI---------NLVrdKDGQLKVADKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 109 LGRFPHTNWFGKLETkdLKSVSKA-LEMVGMKS---------FVNK-NINE---------ISDGERQRVMIARTLAQDTP 168
Cdd:PRK10619 95 TMVFQHFNLWSHMTV--LENVMEApIQVLGLSKqeareravkYLAKvGIDEraqgkypvhLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 169 VIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIwLMLNDSIIE--GAPEDLILN 238
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHV-IFLHQGKIEeeGAPEQLFGN 242
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-235 |
9.77e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 9.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLeigyhiSKRIHNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLN-------KKNIIG 78
Cdd:COG4152 1 MLELKGL------TKRFGDKTaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgepldpeDRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 79 Y---SRADFARLvsfvsteivninnlRVFD-LVALGRfphtnwfgkletkdLKSVSKA---------LEMVGMKSFVNKN 145
Cdd:COG4152 75 YlpeERGLYPKM--------------KVGEqLVYLAR--------------LKGLSKAeakrradewLERLGLGDRANKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 146 INEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIwLMLND 225
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRI-VIINK 204
|
250
....*....|..
gi 1082420396 226 S--IIEGAPEDL 235
Cdd:COG4152 205 GrkVLSGSVDEI 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
27-245 |
1.39e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.23 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYsradfarlvsfVSTEIvninNLRVFDL 106
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGY-----------VPQKL----YLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALGRFPHTnwfgKLETKDlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:PRK09544 84 LTVNRFLRL----RPGTKK-EDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 187 IVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIwLMLNDSI-IEGAPEDLILNETFNQIF 245
Cdd:PRK09544 159 LYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV-LCLNHHIcCSGTPEVVSLHPEFISMF 217
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-232 |
1.77e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.24 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 34 TASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKniigysradfarlVSFVSTEIVNINNLRVFDLV--ALGR 111
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQYIKPDYDGTVEDLLrsITDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 112 FpHTNWFgKLEtkdlksVSKALemvGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLL 191
Cdd:PRK13409 428 L-GSSYY-KSE------IIKPL---QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1082420396 192 NNLSKTENKTIIFSTHDlnIAIQEtdkiwlMLNDSII--EGAP 232
Cdd:PRK13409 497 RRIAEEREATALVVDHD--IYMID------YISDRLMvfEGEP 531
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
27-180 |
1.93e-16 |
|
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: 76.76 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNiIGYSRADFARLVSF------VSTEIVNINN 100
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-LDFQRDSIARGLLYlghapgIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 101 LRvfdlvalgrfphtnWFGKLETKDlkSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLD 180
Cdd:cd03231 94 LR--------------FWHADHSDE--QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-247 |
2.40e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 77.38 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METRKHILEIHNLEIGYHiSKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL-----QNSIQGDILLNKKN 75
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYG-DKQA----LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 76 IigYSRAdfarlvsfvsteiVNINNLR----------------VFDLVALGrfPHTNwfGKLETKDLKS-VSKALEMVGM 138
Cdd:COG1117 80 I--YDPD-------------VDVVELRrrvgmvfqkpnpfpksIYDNVAYG--LRLH--GIKSKSELDEiVEESLRKAAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 139 ----KSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDlP---NKYEivHLLNNLSKteNKTIIFSTHDLNI 211
Cdd:COG1117 141 wdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD-PistAKIE--ELILELKK--DYTIVIVTHNMQQ 215
|
250 260 270
....*....|....*....|....*....|....*.
gi 1082420396 212 AIQETDKIWLMLNDSIIEgapedliLNETfNQIFDN 247
Cdd:COG1117 216 AARVSDYTAFFYLGELVE-------FGPT-EQIFTN 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-208 |
2.83e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRI-HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYsradfarlvsfVSTEIV 96
Cdd:COG0488 3 NLSKSFgGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGY-----------LPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINNLRVFDLVALG----------------RFPHTNW----FGKLETK-------DLKS-VSKALEMVGMK-SFVNKNIN 147
Cdd:COG0488 72 LDDDLTVLDTVLDGdaelraleaeleeleaKLAEPDEdlerLAELQEEfealggwEAEArAEEILSGLGFPeEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 148 EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHD 208
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHD 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-219 |
3.08e-16 |
|
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: 76.74 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 5 KHILEIHNLEIGYhiSKRIHNSLVSNINLTASEGELIAVIGKNGVGKST---LLRNIAGLQnsiQGDILLNKKNIIGYSR 81
Cdd:cd03248 9 KGIVKFQNVTFAY--PTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTvvaLLENFYQPQ---GGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 82 ADFARLVSFVSTEIVnINNLRVFDLVALGrfphtnwfgkLETKDLKSVSKALEMVGMKSF-----------VNKNINEIS 150
Cdd:cd03248 84 KYLHSKVSLVGQEPV-LFARSLQDNIAYG----------LQSCSFECVKEAAQKAHAHSFiselasgydteVGEKGSQLS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 151 DGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNlsKTENKTIIFSTHDLNIaIQETDKI 219
Cdd:cd03248 153 GGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD--WPERRTVLVIAHRLST-VERADQI 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-211 |
3.61e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRI------HNSLVSNINLTASEGELIAVIGKNGVGKST----LLRNIAGlqnsiQGDILLNKKNI 76
Cdd:PRK15134 275 LLDVEQLQVAFPIRKGIlkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 IGYSRAD---FARLVSFVSTEIVNINN--LRVFDLVALGRFPHTNWFGKLETKDlkSVSKALEMVGMKSFV-NKNINEIS 150
Cdd:PRK15134 350 HNLNRRQllpVRHRIQVVFQDPNSSLNprLNVLQIIEEGLRVHQPTLSAAQREQ--QVIAVMEEVGLDPETrHRYPAEFS 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 151 DGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNI 211
Cdd:PRK15134 428 GGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHV 488
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-226 |
3.69e-16 |
|
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: 76.17 E-value: 3.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNleigyhISKRI-HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:cd03269 1 LEVEN------VTKRFgRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LvsfvSTEIVNINNLRVFD-LVALGRFPhtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ 165
Cdd:cd03269 75 L----PEERGLYPKMKVIDqLVYLAQLK-----GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIwLMLNDS 226
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRV-LLLNKG 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-232 |
3.72e-16 |
|
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: 79.44 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 34 TASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKniigysradfarlVSFVSTEIVNINNLRVFDL---VALG 110
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYKPQYISPDYDGTVEEFlrsANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 111 RFPhTNWFgKLEtkdlksVSKALemvGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHL 190
Cdd:COG1245 429 DFG-SSYY-KTE------IIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1082420396 191 LNNLSKTENKTIIFSTHDlnIAIQEtdkiwlMLNDSII--EGAP 232
Cdd:COG1245 498 IRRFAENRGKTAMVVDHD--IYLID------YISDRLMvfEGEP 533
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-247 |
4.09e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 4.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKrihnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLqNSIQGDILLNKK-----NIIGYSRA 82
Cdd:PRK14258 8 IKVNNLSFYYDTQK-----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRveffnQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 83 DFARL---VSFVSTEiVNINNLRVFDLVALGrFPHTNWFGKLETKDL-KSVSKALEMVG-MKSFVNKNINEISDGERQRV 157
Cdd:PRK14258 82 NLNRLrrqVSMVHPK-PNLFPMSVYDNVAYG-VKIVGWRPKLEIDDIvESALKDADLWDeIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETD-KIWLMLNDSIIEGAPEDLI 236
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDfTAFFKGNENRIGQLVEFGL 239
|
250
....*....|.
gi 1082420396 237 LNETFNQIFDN 247
Cdd:PRK14258 240 TKKIFNSPHDS 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-209 |
4.14e-16 |
|
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: 76.32 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METrkhILEIHNLeigyhiSKR--IHN------SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLN 72
Cdd:COG4778 1 MTT---LLEVENL------SKTftLHLqggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 73 -------------------KKNIIGY-SRadFARLVSFVSTEivninnlrvfDLVA-----LGRFPHT------NWFGKL 121
Cdd:COG4778 72 hdggwvdlaqaspreilalRRRTIGYvSQ--FLRVIPRVSAL----------DVVAeplleRGVDREEarararELLARL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 122 ETKD-LKSVSKAlemvgmkSFvnknineiSDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENK 200
Cdd:COG4778 140 NLPErLWDLPPA-------TF--------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGT 203
|
....*....
gi 1082420396 201 TIIFSTHDL 209
Cdd:COG4778 204 AIIGIFHDE 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
8-237 |
6.27e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 75.26 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNL--EIGyhiSKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS--IQGDILLNKKNIIGYSRAD 83
Cdd:cd03217 1 LEIKDLhvSVG---GKEI----LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARLVSFVSTEIvninnlrvfdlvalgrfphtnwfgkletkdlksvSKALEMVGMKSFVnKNINE-ISDGERQRVMIART 162
Cdd:cd03217 74 RARLGIFLAFQY----------------------------------PPEIPGVKNADFL-RYVNEgFSGGEKKRNEILQL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 163 LAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQ-ETDKIWLMLNDSIIEGAPEDLIL 237
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYiKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-222 |
7.00e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 21 KRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLL-----RNIAGLQnsIQGDILLNKKNIigysRADFARLVS-FVSTE 94
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVK--GSGSVLLNGMPI----DAKEMRAISaYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 IVNINNLRVFD-LVALGRFPhtnwFGKLETKDLK--SVSKALEMVGMKSFVNKNINE------ISDGERQRVMIARTLAQ 165
Cdd:TIGR00955 108 DLFIPTLTVREhLMFQAHLR----MPRRVTKKEKreRVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKYEIVHLLNNLSkTENKTIIFSTHDLNIAIQET-DKIWLM 222
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIHQPSSELFELfDKIILM 240
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-208 |
7.28e-16 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 75.91 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 36 SEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLnkkniigysradFARLVSFVSTEIVNINNLRVFDLVA--LGRFP 113
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------------ELDTVSYKPQYIKADYEGTVRDLLSsiTKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 114 HTNWFgKLEtkdlksVSKALemvGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNN 193
Cdd:cd03237 91 THPYF-KTE------IAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170
....*....|....*
gi 1082420396 194 LSKTENKTIIFSTHD 208
Cdd:cd03237 161 FAENNEKTAFVVEHD 175
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-241 |
1.01e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.87 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISK-RIHnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS---IQGDIL-LNKKNIIGYSR 81
Cdd:COG4170 3 LLDIRNLTIEIDTPQgRVK--AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhVTADRFrWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 82 ADFARLVSfvsTEIVNI---------NNLRVFDLV--ALGRFPHTNWFGKLETKDLKSVSKALEMVG-------MKSFVN 143
Cdd:COG4170 81 RERRKIIG---REIAMIfqepsscldPSAKIGDQLieAIPSWTFKGKWWQRFKWRKKRAIELLHRVGikdhkdiMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 144 kninEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLML 223
Cdd:COG4170 158 ----ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLY 233
|
250
....*....|....*...
gi 1082420396 224 NDSIIEGAPEDLILNETF 241
Cdd:COG4170 234 CGQTVESGPTEQILKSPH 251
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-208 |
1.04e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.62 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY----SRAD 83
Cdd:PRK15064 320 LEVENLTKGFD-----NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYyaqdHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FArlvsfvsteivniNNLRVFDlvalgrfphtnWFG--KLETKDLKSVSKAL-EMVGMKSFVNKNINEISDGERQRVMIA 160
Cdd:PRK15064 395 FE-------------NDLTLFD-----------WMSqwRQEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFG 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHD 208
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDM----ESIESLNMALEKYEGTLIFVSHD 494
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-209 |
1.09e-15 |
|
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: 75.45 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSL--VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNkkNIIGYSRAD-FARLVSFV--- 91
Cdd:cd03267 25 SLFKRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA--GLVPWKRRKkFLRRIGVVfgq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 92 STEIvnINNLRVFDLVALGRfpHTNWFGKLETKdlKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIV 171
Cdd:cd03267 103 KTQL--WWDLPVIDSFYLLA--AIYDLPPARFK--KRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1082420396 172 LDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDL 209
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYM 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-207 |
1.13e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.64 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI-IGYSRADFARLVSFVSTEIVNINNLRVFDLV 107
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrFASTTAALAAGVAIIYQELHLVPEMTVAENL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRFPHTnwFGKLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:PRK11288 101 YLGQLPHK--GGIVNRRLLNYeAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQ 178
|
170 180
....*....|....*....|.
gi 1082420396 187 IVHLLNNLsKTENKTIIFSTH 207
Cdd:PRK11288 179 LFRVIREL-RAEGRVILYVSH 198
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-239 |
1.21e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.20 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGdillnkKNIIGysraDFARLVSFvsTEIVNINNLRVfDLV 107
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG------QTIVG----DYAIPANL--KKIKEVKRLRK-EIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRFPHTNWFGKLETKDL---------------KSVSKALEMVGM-KSFVNKNINEISDGERQRVMIARTLAQDTPVIV 171
Cdd:PRK13645 94 LVFQFPEYQLFQETIEKDIafgpvnlgenkqeayKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 172 LDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDLILNE 239
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISiGSPFEIFSNQ 242
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-235 |
1.37e-15 |
|
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: 74.87 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIHNslvsnINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI----------- 76
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRG-----VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklppherara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 -IGY---SRADFARLvsfvSTEivniNNLRVfDLVALGRFPHtnwfgkletkdlKSVSKALEM--VgMKSFVNKNINEIS 150
Cdd:TIGR03410 76 gIAYvpqGREIFPRL----TVE----ENLLT-GLAALPRRSR------------KIPDEIYELfpV-LKEMLGRRGGDLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 151 DGERQRVMIARTLAQDTPVIVLDEPTAFLDlPN-KYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII- 228
Cdd:TIGR03410 134 GGQQQQLAIARALVTRPKLLLLDEPTEGIQ-PSiIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVa 212
|
....*..
gi 1082420396 229 EGAPEDL 235
Cdd:TIGR03410 213 SGAGDEL 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
26-228 |
1.39e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.61 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 26 SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAG-LQ-NSIQGDILLNKKNIIgysrADFARLVSFVSTEIVNINNLRV 103
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQgNNFTGTILANNRKPT----KQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FD---LVALGRFPHTnwfgklETKDLK-----SVSKALEMVGMKSFV--NKNINEISDGERQRVMIARTLAQDTPVIVLD 173
Cdd:PLN03211 158 REtlvFCSLLRLPKS------LTKQEKilvaeSVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 174 EPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHdlniaiQETDKIWLMLnDSII 228
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMH------QPSSRVYQMF-DSVL 278
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-229 |
1.83e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRihnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQnSIQGDILLNKKNIIGYSRADFARL 87
Cdd:PRK11174 350 IEAEDLEILSPDGKT----LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSteivniNNLRVF-----DLVALGRFPHTNwfgkletkdlKSVSKALEMVGMKSFVNKNIN----EISD------- 151
Cdd:PRK11174 425 LSWVG------QNPQLPhgtlrDNVLLGNPDASD----------EQLQQALENAWVSEFLPLLPQgldtPIGDqaaglsv 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE 229
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLE-DLAQWDQIWVMQDGQIVQ 563
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
17-239 |
2.60e-15 |
|
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: 74.12 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 17 YHISKRIHN-SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL-VSFVSTE 94
Cdd:cd03218 4 ENLSKRYGKrKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 IVNINNLRVFD--LVALGRFPHTNWFGKLETKDLksvskaLEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:cd03218 84 ASIFRKLTVEEniLAVLEIRGLSKKEREEKLEEL------LEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNE 239
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLaEGTPEEIAANE 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-238 |
2.93e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.43 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNslvsnINLTASEGELIAVIGKNGVGKSTLLRNIAGLQN-----SIQGDILLNKKNIigYS- 80
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNS-----VSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNI--YSp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARLVSFVSTEIVNINN--LRVFDLVALGRfphtnwfgKLE-TKDLKSVSKALEmvgmKSFVNKNI-NEISD----- 151
Cdd:PRK14239 78 RTDTVDLRKEIGMVFQQPNPfpMSIYENVVYGL--------RLKgIKDKQVLDEAVE----KSLKGASIwDEVKDrlhds 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 152 ------GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNIAIQETDKIWLMLND 225
Cdd:PRK14239 146 alglsgGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDG 223
|
250
....*....|....
gi 1082420396 226 SIIE-GAPEDLILN 238
Cdd:PRK14239 224 DLIEyNDTKQMFMN 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-232 |
4.86e-15 |
|
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: 72.91 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYhiskRIHNSLV-SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:cd03244 3 IEFKNVSLRY----RPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNI-----NNLrvfDlvalgrfPhtnwFGKLETKDLKSvskALEMVGMKSFVNKN-------INE----IS 150
Cdd:cd03244 79 RISIIPQDPVLFsgtirSNL---D-------P----FGEYSDEELWQ---ALERVGLKEFVESLpggldtvVEEggenLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 151 DGERQRVMIARTLAQDTPVIVLDEPTAFLDlpnkYEIVHLLNNLSKTE--NKTIIFSTHDLNiAIQETDKIWLMLNDSII 228
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVD----PETDALIQKTIREAfkDCTVLTIAHRLD-TIIDSDRILVLDKGRVV 216
|
....*
gi 1082420396 229 E-GAP 232
Cdd:cd03244 217 EfDSP 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
28-222 |
5.07e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 74.76 E-value: 5.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLqnsiqgdilLNKKNIIGYSradfarlVSFVSTEIVNI-----NNLR 102
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGL---------LAANGRIGGS-------ATFNGREILNLpekelNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 103 VFDLVALGRFPHT--NWFGK-----LETKDL-KSVSKA---LEMVGMKSFVN-----KNIN----EISDGERQRVMIART 162
Cdd:PRK09473 96 AEQISMIFQDPMTslNPYMRvgeqlMEVLMLhKGMSKAeafEESVRMLDAVKmpearKRMKmyphEFSGGMRQRVMIAMA 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 163 LAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-236 |
7.82e-15 |
|
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: 72.96 E-value: 7.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVnINNLRVFDLVAL 109
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPV-LFDGTIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 110 GRFPHTnwfgkletkdLKSVSKALEMVGMKSFVNKNIN-----------EISDGERQRVMIARTLAQDTPVIVLDEPTAF 178
Cdd:cd03249 100 GKPDAT----------DEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 179 LDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-GAPEDLI 236
Cdd:cd03249 170 LDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEqGTHDELM 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-229 |
8.73e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.74 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIHNslvsnINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDIllnkkNIIGYsRADFARl 87
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD-----ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTL-----NIAGN-HFDFSK- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 vsfvSTEIVNINNLR-----VFDLVALgrFPH-----------TNWFGKLETKDLKSVSKALEMVGMKSFVNKNINEISD 151
Cdd:PRK11124 71 ----TPSDKAIRELRrnvgmVFQQYNL--WPHltvqqnlieapCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTeNKTIIFSTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
30-235 |
1.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS--------RADFARLVSFVSTEIVNINnl 101
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqiRKKVGLVFQFPESQLFEET-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 102 rVFDLVALGrfPHTnwFGKLETKDLKSVSKALEMVGM-KSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLD 180
Cdd:PRK13649 103 -VLKDVAFG--PQN--FGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 181 LPNKYEIVHLLNNLSKTeNKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDL 235
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVlSGKPKDI 232
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
28-229 |
2.39e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLlrnIAGLQNSI---QGDILLNKKNIIGYSRADFARLVSFVSTEIVNIN----- 99
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRVFdpqSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNrsied 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 NLRVfdlvalGRFPHTNwfgkLETKDLKSVSKALEMV-----GMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDE 174
Cdd:PRK13657 428 NIRV------GRPDATD----EEMRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 175 PTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLMLNDSIIE 229
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMK--GRTTFIIAHRLS-TVRNADRILVFDNGRVVE 549
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-222 |
2.55e-14 |
|
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: 70.15 E-value: 2.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskrihnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:cd03215 4 VLEVRGLSVKGA---------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 L-VSFVsteivninnlrvfdlvalgrfphtnwfgkleTKDLKSVSKALEMVgmksfVNKNI---NEISDGERQRVMIART 162
Cdd:cd03215 75 AgIAYV-------------------------------PEDRKREGLVLDLS-----VAENIalsSLLSGGNQQKVVLARW 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 163 LAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:cd03215 119 LARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVM 177
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-229 |
2.96e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.74 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 1 METrkhILEIHNLEIGYH----ISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI 76
Cdd:PRK15112 1 VET---LLEVRNLSKTFRyrtgWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 I--GYS-RADFARLVSFVSTEIVNINNlRVFDLVALGRFPHTnwfgKLETKDL-KSVSKALEMVGMK-SFVNKNINEISD 151
Cdd:PRK15112 78 HfgDYSyRSQRIRMIFQDPSTSLNPRQ-RISQILDFPLRLNT----DLEPEQReKQIIETLRQVGLLpDHASYYPHMLAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
8-207 |
3.20e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.30 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIgYHISKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDIllnkkniigySRADFARL 87
Cdd:COG4178 363 LALEDLTL-RTPDGRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----------ARPAGARV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VsFVSTEI-VNINNLRvfDLVAlgrFPHTNwfgklETKDLKSVSKALEMVGMKSFVNKnINEI-------SDGERQRVMI 159
Cdd:COG4178 429 L-FLPQRPyLPLGTLR--EALL---YPATA-----EAFSDAELREALEAVGLGHLAER-LDEEadwdqvlSLGEQQRLAF 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082420396 160 ARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNN-LSKTenkTIIFSTH 207
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGT---TVISVGH 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-229 |
4.18e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 4.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 4 RKHILEIHNLeIGYHISKrihnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAD 83
Cdd:PRK09700 262 HETVFEVRNV-TSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARLVSFVSTEIVNIN----NLRVFDLVALGRFPHTNWFGKL-----ETKDLKSVSKALEMVGMK-SFVNKNINEISDGE 153
Cdd:PRK09700 335 AVKKGMAYITESRRDNgffpNFSIAQNMAISRSLKDGGYKGAmglfhEVDEQRTAENQRELLALKcHSVNQNITELSGGN 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 154 RQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:PRK09700 415 QQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-224 |
4.22e-14 |
|
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: 70.19 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAG----LQNSIQ--GDI--------LLN- 72
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGelekLSGSVSvpGSIayvsqepwIQNg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 73 --KKNIIGYSRADFARLvsfvsteivninnLRVFDLVALgrfphtnwfgkleTKDLKSVSKALE-MVGMKSfvnknINeI 149
Cdd:cd03250 81 tiRENILFGKPFDEERY-------------EKVIKACAL-------------EPDLEILPDGDLtEIGEKG-----IN-L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 150 SDGERQRVMIARTLAQDTPVIVLDEPTAFLDlpnkyeiVH---------LLNNLSKteNKTIIFSTHDLNIaIQETDKIW 220
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVD-------AHvgrhifencILGLLLN--NKTRILVTHQLQL-LPHADQIV 198
|
....
gi 1082420396 221 LMLN 224
Cdd:cd03250 199 VLDN 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-229 |
4.76e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiSKRIHNSLVSNINLTASEGELIAVIGKNGVGKS----TLLRNIAGLQNSIQGD-ILLNKKN--IIGY 79
Cdd:PRK10261 12 VLAVENLNIAFM-QEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDkMLLRRRSrqVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 80 SRADFARLVSFVSTEIVNINN---------LRVFDLVALGRFPHTNwFGKLETkdLKSVSKALEMVGM---KSFVNKNIN 147
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQepmtslnpvFTVGEQIAESIRLHQG-ASREEA--MVEAKRMLDQVRIpeaQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 148 EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSI 227
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
..
gi 1082420396 228 IE 229
Cdd:PRK10261 248 VE 249
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-229 |
5.66e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIHNslvsnINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDIllnkknIIGYSRADFARL 87
Cdd:COG4161 3 IQLKNINCFYGSHQALFD-----INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQL------NIAGHQFDFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSfvsteIVNINNLR-----VFDLVALgrFPHTN----------WFGKLETKD-LKSVSKALEMVGMKSFVNKNINEISD 151
Cdd:COG4161 72 PS-----EKAIRLLRqkvgmVFQQYNL--WPHLTvmenlieapcKVLGLSKEQaREKAMKLLARLRLTDKADRFPLHLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFsTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIV-THEVEFARKVASQVVYMEKGRIIE 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-238 |
6.76e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.41 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNsLVSNINLTASEGELIAVIGKNGVGKS----TLLRNIAGLQNSIQGDILLNKKNIIGYSRA 82
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVE-AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 83 DFARL----VSFVSTE-IVNINNL-RVFDLVALGRFPHTnwfgKLETKDLKS-VSKALEMVG-------MKSFVNkninE 148
Cdd:COG4172 85 ELRRIrgnrIAMIFQEpMTSLNPLhTIGKQIAEVLRLHR----GLSGAAARArALELLERVGipdperrLDAYPH----Q 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 149 ISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII 228
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250
....*....|.
gi 1082420396 229 E-GAPEDLILN 238
Cdd:COG4172 237 EqGPTAELFAA 247
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-236 |
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: 71.37 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQN--SIQGDILLN------------------------------KKNII 77
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvgepcpvcggtlepeEVDFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 78 GYSRADFARLVSFVSTEIVNINNL----RVFDLVaLGRFPHTNWFGKletKDLKSVSKALEMVGMKSFVNKNINEISDGE 153
Cdd:TIGR03269 98 NLSDKLRRRIRKRIAIMLQRTFALygddTVLDNV-LEALEEIGYEGK---EAVGRAVDLIEMVQLSHRITHIARDLSGGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 154 RQRVMIARTLAQDTPVIVLDEPTAFLDlPNKYEIVH-LLNNLSKTENKTIIFSTHDLNIAIQETDK-IWLMLNDSIIEGA 231
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVHnALEEAVKASGISMVLTSHWPEVIEDLSDKaIWLENGEIKEEGT 252
|
....*
gi 1082420396 232 PEDLI 236
Cdd:TIGR03269 253 PDEVV 257
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
30-230 |
1.77e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.29 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLlrnIAGLQNSIQ---GDILLNKKNIIGYSRADFARLVSFVSTEIVNINNlRVFDL 106
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTV---AALLQNLYQptgGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALGrfphtnwfgkLETKDLKSVSKALEMVGMKSFV-------NKNINE----ISDGERQRVMIARTLAQDTPVIVLDEP 175
Cdd:TIGR00958 575 IAYG----------LTDTPDEEIMAAAKAANAHDFImefpngyDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 176 TAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHDLNIaIQETDKIWLMLNDSIIEG 230
Cdd:TIGR00958 645 TSALDA----ECEQLLQESRSRASRTVLLIAHRLST-VERADQILVLKKGSVVEM 694
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-221 |
1.99e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNiIGYSRADFARLVSF------VSTEIVNINN 100
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP-IRRQRDEYHQDLLYlghqpgIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 101 LRvfdlvalgrfphtnWFGKL-ETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEP-TAf 178
Cdd:PRK13538 95 LR--------------FYQRLhGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPfTA- 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1082420396 179 LDLPNKYEIVHLLnnLSKTENK-TIIFSTH-DLNIAIQETDKIWL 221
Cdd:PRK13538 160 IDKQGVARLEALL--AQHAEQGgMVILTTHqDLPVASDKVRKLRL 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
38-194 |
2.25e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 38 GELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigySRADFARLVSFVSteivNINNLRVfDLVALGRFPHTNW 117
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA---TRGDRSRFMAYLG----HLPGLKA-DLSTLENLHFLCG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 118 FGKLETKDLKsvSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNL 194
Cdd:PRK13543 109 LHGRRAKQMP--GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLVNRM 179
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
7-236 |
2.29e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.83 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSlVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLqnsiqgdillNKKNI------IGYS 80
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKA-VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV----------TKDNWrvtadrMRFD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARLVSFVSTEIVNINNLRVFD--------LVALGR-----FPHTNWFGKLETKDLKSVSKALEM---VGMKSfvNK 144
Cdd:PRK15093 72 DIDLLRLSPRERRKLVGHNVSMIFQepqscldpSERVGRqlmqnIPGWTYKGRWWQRFGWRKRRAIELlhrVGIKD--HK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 145 NI-----NEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKI 219
Cdd:PRK15093 150 DAmrsfpYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
250
....*....|....*...
gi 1082420396 220 WLMLNDSIIEGA-PEDLI 236
Cdd:PRK15093 230 NVLYCGQTVETApSKELV 247
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
30-238 |
2.90e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.09 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDIllnkkNIIGYSradfarlvsfVSTEIVNINNLRVFDLVAL 109
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI-----TIAGYH----------ITPETGNKNLKKLRKKVSL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 110 G-RFPHTNWFGKLETKDL------------KSVSKALE---MVGMK-SFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK13641 90 VfQFPEAQLFENTVLKDVefgpknfgfsedEAKEKALKwlkKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGA-PEDLILN 238
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHAsPKEIFSD 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
13-228 |
2.90e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 13 LEIgyHISKRIHNsLVSNINLT-ASEGeLIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNK-------KNI-------- 76
Cdd:PRK11144 2 LEL--NFKQQLGD-LCLTVNLTlPAQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGIclppekrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 IGYSRADfARLvsfvsteivninnlrvfdlvalgrFPHTNWFGKLE----TKDLKSVSKALEMVGMKSFVNKNINEISDG 152
Cdd:PRK11144 78 IGYVFQD-ARL------------------------FPHYKVRGNLRygmaKSMVAQFDKIVALLGIEPLLDRYPGSLSGG 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 153 ERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII 228
Cdd:PRK11144 133 EKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-211 |
3.15e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 37 EGELIAVIGKNGVGKSTLLRNIAGLQ--NSIQGDILLNKKNIIGYSRAD-----FARLVS---FVSTEIVNINNL-RVFD 105
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpNLGDYDEEPSWDEVLKRFRGTelqdyFKKLANgeiKVAHKPQYVDLIpKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 lvalgrfphtnwfGK----LETKDLKSVSKAL-EMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLD 180
Cdd:COG1245 178 -------------GTvrelLEKVDERGKLDELaEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|.
gi 1082420396 181 LPNKYEIVHLLNNLSKtENKTIIFSTHDLNI 211
Cdd:COG1245 245 IYQRLNVARLIRELAE-EGKYVLVVEHDLAI 274
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-211 |
5.05e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.29 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 22 RIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGdillnkkniigysrADFARLVSFVSTEIVNInnl 101
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV--------------AGCVDVPDNQFGREASL--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 102 rvfdLVALGRfphtnwfgkleTKDLKSVSKALEMVGMKSFVN--KNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:COG2401 103 ----IDAIGR-----------KGDFKDAVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|..
gi 1082420396 180 DLPNKYEIVHLLNNLSKTENKTIIFSTHDLNI 211
Cdd:COG2401 168 DRQTAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-238 |
5.55e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.20 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 40 LIAVIGKNGVGKSTLLRNIAGLQNSIQG-----DILLNKKNIIGYSRA-DFARLVSFVSTEiVNINNLRVFDLVALGRFP 113
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQR-PNPFPMSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 114 HTnwfgKLETKDLKSVSKA-LEMVGMKSFVNKNINE----ISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIV 188
Cdd:PRK14271 128 HK----LVPRKEFRGVAQArLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082420396 189 HLLNNLSktENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILN 238
Cdd:PRK14271 204 EFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
27-222 |
5.82e-13 |
|
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: 66.50 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS--IQGDILLNKKNIigysRADFARLVSFVSTEIVNINNLrvf 104
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL----DKNFQRSTGYVEQQDVHSPNL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 dlvalgrfphtnwfgkletkdlkSVSKALEMvgmksfvNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNK 184
Cdd:cd03232 95 -----------------------TVREALRF-------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1082420396 185 YEIVHLLNNLSKTeNKTIIFSTHDLNIAIQET-DKIWLM 222
Cdd:cd03232 145 YNIVRFLKKLADS-GQAILCTIHQPSASIFEKfDRLLLL 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-244 |
1.22e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 26 SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL------QNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNIN 99
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 NLRVFDLVALGRFPHtnwfGKLETKDLKS-VSKALEMVGMKSFVNKNIN----EISDGERQRVMIARTLAQDTPVIVLDE 174
Cdd:PRK14246 104 HLSIYDNIAYPLKSH----GIKEKREIKKiVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 175 PTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILNETFNQI 244
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-218 |
1.48e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskrihNSL-VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSI-----QGDILLNKKNIIGyS 80
Cdd:PRK14243 10 VLRTENLNVYYG------SFLaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLYA-P 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARLVSFVSTEIVNINNL--RVFDLVALGrfPHTNWF-GKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRV 157
Cdd:PRK14243 83 DVDPVEVRRRIGMVFQKPNPFpkSIYDNIAYG--ARINGYkGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSktENKTIIFSTHDLNIAIQETDK 218
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAARVSDM 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-224 |
2.23e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.13 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 2 ETRKHILEIHNLEIGYHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNK----KNI- 76
Cdd:PTZ00265 375 KKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIn 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 -------IGYSRADFARLVSFVSTEI-VNINNLRvfDLVALGRFPHTNWFGKLETKDLKSVSKAL--------------- 133
Cdd:PTZ00265 455 lkwwrskIGVVSQDPLLFSNSIKNNIkYSLYSLK--DLEALSNYYNEDGNDSQENKNKRNSCRAKcagdlndmsnttdsn 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 134 EMVGMK--------------------------------SFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDL 181
Cdd:PTZ00265 533 ELIEMRknyqtikdsevvdvskkvlihdfvsalpdkyeTLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1082420396 182 PNKYEIVHLLNNLSKTENKTIIFSTHDLNiAIQETDKIWLMLN 224
Cdd:PTZ00265 613 KSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
30-214 |
2.37e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.83 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLrNIAG-LQNSIQGDILLNKKNIIGYSRADFARL--------------VSFVSTE 94
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLM-NILGcLDKPTSGTYRVAGQDVATLDADALAQLrrehfgfifqryhlLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 ivniNNLRVFDLVAlgrfphtnwfGKLETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDE 174
Cdd:PRK10535 105 ----QNVEVPAVYA----------GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1082420396 175 PTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQ 214
Cdd:PRK10535 171 PTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-229 |
2.67e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:PRK10790 341 IDIDNVSFAYRDDNLV----LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEIVNINNlRVFDLVALGR-FPHTNWFGKLETKDLKSVSKALEMvGMKSFVNKNINEISDGERQRVMIARTLAQD 166
Cdd:PRK10790 417 VAMVQQDPVVLAD-TFLANVTLGRdISEEQVWQALETVQLAELARSLPD-GLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 167 TPVIVLDEPTAFLDLPNKYEIVHLLNNLSktENKTIIFSTHDLNiAIQETDKIWLMLNDSIIE 229
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVR--EHTTLVVIAHRLS-TIVEADTILVLHRGQAVE 554
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-232 |
2.99e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSL------VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS 80
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGLLNRVtrevhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 -------RAD--------FARLVSFVSTEIVNINNLRVFDLVAlgrfphtnwfGKLETKdlkSVSKALEMVGMK-SFVNK 144
Cdd:PRK10261 393 pgklqalRRDiqfifqdpYASLDPRQTVGDSIMEPLRVHGLLP----------GKAAAA---RVAWLLERVGLLpEHAWR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 145 NINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLN 224
Cdd:PRK10261 460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL 539
|
....*...
gi 1082420396 225 DSIIEGAP 232
Cdd:PRK10261 540 GQIVEIGP 547
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-232 |
3.81e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 5 KHILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL-----QNSIQGDILLNKKNIigY 79
Cdd:PRK14267 2 KFAIETVNLRVYYG-----SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 80 SR----ADFARLVSFVSTEIVNINNLRVFDLVALGRfpHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINE----ISD 151
Cdd:PRK14267 75 SPdvdpIEVRREVGMVFQYPNPFPHLTIYDNVAIGV--KLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDypsnLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGA 231
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
.
gi 1082420396 232 P 232
Cdd:PRK14267 231 P 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
27-245 |
4.56e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNII---GYSRAdfARLVSFVSTEIVNINNLRV 103
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLHARA--RRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDlvalgrfphtNWFGKLET-KDLKSVSKA------LEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:PRK10895 96 YD----------NLMAVLQIrDDLSAEQREdranelMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 177 AFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIF 245
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIaHGTPTEILQDEHVKRVY 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
27-220 |
4.93e-12 |
|
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: 64.21 E-value: 4.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL---QNSIQGDILLNkkniiGYSRADFA----RLVSFVSTEIVNIN 99
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYN-----GIPYKEFAekypGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 NLRVFDLValgRFphtnwfgkletkdlksvskALEMVGmksfvNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:cd03233 97 TLTVRETL---DF-------------------ALRCKG-----NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1082420396 180 DLPNKYEIVHLLNNLSKTENKTIIFSTHdlniaiQETDKIW 220
Cdd:cd03233 150 DSSTALEILKCIRTMADVLKTTTFVSLY------QASDEIY 184
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-210 |
5.15e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNkkniiGYS----RADFARLVSFVsteivninnlrv 103
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----GYVpfkrRKEFARRIGVV------------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 F--------DLVALGRFphtNWFG---KLETKDLKSVSKAL-EMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIV 171
Cdd:COG4586 101 FgqrsqlwwDLPAIDSF---RLLKaiyRIPDAEYKKRLDELvELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1082420396 172 LDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLN 210
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-232 |
7.10e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIgyhiskRIHNSLVSNINLTASEGELIAVIGKNGVGKStlLRNIAGLQ------NSIQGDILLNKKNIIGYS- 80
Cdd:PRK10418 5 IELRNIAL------QAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAPCAl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RAdfaRLVSfvsTEIVN----INNLRVF------DLVALGRfphtnwfgkleTKDLKSVSKALEMVGM---KSFVNKNIN 147
Cdd:PRK10418 77 RG---RKIA---TIMQNprsaFNPLHTMhthareTCLALGK-----------PADDATLTAALEAVGLenaARVLKLYPF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 148 EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSI 227
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
....*
gi 1082420396 228 IEGAP 232
Cdd:PRK10418 220 VEQGD 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
38-231 |
7.86e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.13 E-value: 7.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 38 GELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigySRADfARLVSFVSTEIVNI-------NNLRVFDLVALG 110
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI---TRLK-NREVPFLRRQIGMIfqdhhllMDRTVYDNVAIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 111 RFphtnwFGKLETKDLKS-VSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVH 189
Cdd:PRK10908 104 LI-----IAGASGDDIRRrVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1082420396 190 LLNNLSKTeNKTIIFSTHDLNIAIQETDKIwLMLNDSIIEGA 231
Cdd:PRK10908 179 LFEEFNRV-GVTVLMATHDIGLISRRSYRM-LTLSDGHLHGG 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-211 |
1.21e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 37 EGELIAVIGKNGVGKSTLLRNIAG--LQNSIQGDILLNKKNIIGYSRAD-----FARLVSfvsteivniNNLRV------ 103
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGelIPNLGDYEEEPSWDEVLKRFRGTelqnyFKKLYN---------GEIKVvhkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDLVAlgrfphtNWF-GK----LETKDLKSVSKAL-EMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTA 177
Cdd:PRK13409 169 VDLIP-------KVFkGKvrelLKKVDERGKLDEVvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190
....*....|....*....|....*....|....
gi 1082420396 178 FLDLPNKYEIVHLLNNLskTENKTIIFSTHDLNI 211
Cdd:PRK13409 242 YLDIRQRLNVARLIREL--AEGKYVLVVEHDLAV 273
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
27-236 |
1.40e-11 |
|
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: 65.74 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFDL 106
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 107 VALGRFPHTNWFGKLETKDLKSVSKALEmVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLpnkyE 186
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALP-DKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL----E 1455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 187 IVHLLNNLSKT--ENKTIIFSTHDLNIAIQETDKIwlMLNDSIIE--GAPEDLI 236
Cdd:TIGR00957 1456 TDNLIQSTIRTqfEDCTVLTIAHRLNTIMDYTRVI--VLDKGEVAefGAPSNLL 1507
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-240 |
1.89e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 64.73 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 24 HNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI----IGYSRADFArLVS---FVSTEIV 96
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtklqLDSWRSRLA-VVSqtpFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 97 NINnlrvfdlVALGRfPHTNWFGKLETKDLKSVSKALEMV--GMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDE 174
Cdd:PRK10789 406 ANN-------IALGR-PDATQQEIEHVARLASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 175 PTAFLDLPNKYEIVHllnNLSK-TENKTIIFSTHDLNiAIQETDKIWLMLNDSIIEGAPEDLILNET 240
Cdd:PRK10789 478 ALSAVDGRTEHQILH---NLRQwGEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-225 |
2.18e-11 |
|
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: 64.68 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 2 ETRKHiLEIHNLEIGYHISKRihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSR 81
Cdd:TIGR01842 312 EPEGH-LSVENVTIVPPGGKK---PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 82 ADFARLVSFVSTEIvninnlRVFD-LVA--LGRFPhtnwfgklETKDLKSVSKAL------EMV-----GMKSFVNKNIN 147
Cdd:TIGR01842 388 ETFGKHIGYLPQDV------ELFPgTVAenIARFG--------ENADPEKIIEAAklagvhELIlrlpdGYDTVIGPGGA 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1082420396 148 EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNiAIQETDKIwLMLND 225
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKI-LVLQD 528
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-209 |
2.55e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskrihnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:COG1129 256 VLEVEGLSVGGV---------VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 L-VSFVSTE-----IV-------NINnlrvfdLVALGRFphtNWFGKLETKDLKSVSKALemvgMKSF------VNKNIN 147
Cdd:COG1129 327 AgIAYVPEDrkgegLVldlsireNIT------LASLDRL---SRGGLLDRRRERALAEEY----IKRLriktpsPEQPVG 393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 148 EISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDL 209
Cdd:COG1129 394 NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSEL 454
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-176 |
3.47e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.87 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS-RADFARLVSFVSTEIVNINNLRVFDLV 107
Cdd:PRK10762 21 SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpKSSQEAGIGIIHQELNLIPQLTIAENI 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRFPhTNWFGKLETKDL-KSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:PRK10762 101 FLGREF-VNRFGRIDWKKMyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-222 |
3.97e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI-IGYSRADFARLVSFVSTEIVNINNLRVFDLVA 108
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQELNLVLQRSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 109 LGRFPHTNWFGKlETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLdlpNKYEIV 188
Cdd:PRK10982 96 LGRYPTKGMFVD-QDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVN 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082420396 189 HLLNNLSKTENK--TIIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK10982 172 HLFTIIRKLKERgcGIVYISHKMEEIFQLCDEITIL 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
28-245 |
4.56e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 61.91 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIG---YSRAdfaRL-VSFVSTEIVNINNLRV 103
Cdd:TIGR04406 17 VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlpmHERA---RLgIGYLPQEASIFRKLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDlvalgrfphtNWFGKLET-KDL------KSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:TIGR04406 94 EE----------NIMAVLEIrKDLdraereERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 177 AFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNETFNQIF 245
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLaEGTPAEIVANEKVRRVY 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
38-238 |
5.10e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 62.67 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 38 GELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL--------------------VSFVSTEIVN 97
Cdd:PRK11308 41 GKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkiqivfqnpygslnprkkVGQILEEPLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 98 INNlrvfDLVALGRfphtnwfgkletkdlksVSKALEM---VGMKS-FVNKNINEISDGERQRVMIARTLAQDTPVIVLD 173
Cdd:PRK11308 121 INT----SLSAAER-----------------REKALAMmakVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 174 EPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILN 238
Cdd:PRK11308 180 EPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
28-219 |
5.50e-11 |
|
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: 63.88 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIigYSRADFARLvsfvSTEIVNINNLRVFDLV 107
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQ----SLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALgrfPHTNWFGKLETKDLKS----VSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPN 183
Cdd:TIGR01257 1020 VA---EHILFYAQLKGRSWEEaqleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082420396 184 KYEIVHLLnnLSKTENKTIIFSTHDLNIAIQETDKI 219
Cdd:TIGR01257 1097 RRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRI 1130
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
37-211 |
6.53e-11 |
|
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: 61.61 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 37 EGELIAVIGKNGVGKSTLLRNIAGLQ--NSIQGDILLNKKNIIGYSRAD-----FARLVSFVSTEIVNINNL----RVFD 105
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLkpNLGKFDDPPDWDEILDEFRGSelqnyFTKLLEGDVKVIVKPQYVdlipKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 LVALGRFPHTNWFGKLETkdlksVSKALEMVGMksfVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKY 185
Cdd:cd03236 105 GKVGELLKKKDERGKLDE-----LVDQLELRHV---LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|....*.
gi 1082420396 186 EIVHLLNNLSKtENKTIIFSTHDLNI 211
Cdd:cd03236 177 NAARLIRELAE-DDNYVLVVEHDLAV 201
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-209 |
6.83e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.19 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 26 SLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL----VSFVSTEIVNINNL 101
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 102 RVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMVGMKSFVNKNINeISDGERQRVMIARTLAQDTPVIVLDEPTAFLDl 181
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALD- 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082420396 182 pnkyeiVHLLNNLSKT--------ENKTIIFSTHDL 209
Cdd:cd03290 173 ------IHLSDHLMQEgilkflqdDKRTLVLVTHKL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-180 |
1.15e-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: 62.65 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY---SRAD 83
Cdd:TIGR03719 322 VIEAENLTKAFG-----DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYvdqSRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 FARLVSF---VS--TEIVNINNLRVFDLVALGRFphtNWFGkletkdlksvskalemvgmkSFVNKNINEISDGERQRVM 158
Cdd:TIGR03719 397 LDPNKTVweeISggLDIIKLGKREIPSRAYVGRF---NFKG--------------------SDQQKKVGQLSGGERNRVH 453
|
170 180
....*....|....*....|..
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLD 180
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
36-240 |
1.17e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 36 SEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFDLVALGRFPHT 115
Cdd:PLN03232 1260 SPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 116 NWFGKLETKDLKSVSKAlEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLS 195
Cdd:PLN03232 1340 DLWEALERAHIKDVIDR-NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV----RTDSLIQRTI 1414
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1082420396 196 KTENK--TIIFSTHDLNIAIqETDKIWLMLNDSIIE-GAPEDLILNET 240
Cdd:PLN03232 1415 REEFKscTMLVIAHRLNTII-DCDKILVLSSGQVLEyDSPQELLSRDT 1461
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-222 |
1.17e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFarlvsfVSTEIVNINNLRVFD-- 105
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDG------LANGIVYISEDRKRDgl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 -----------LVALGRFPHTNwfGKLETKDLK-SVSKALEMVGMKS-FVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK10762 342 vlgmsvkenmsLTALRYFSRAG--GSLKHADEQqAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-213 |
1.47e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 60.87 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSfvsteivninnlRVF-D---------------LVALGRfphtnwfGK-------LETKDLKSVSKALEMVGM--KSF 141
Cdd:COG1101 81 YIG------------RVFqDpmmgtapsmtieenlALAYRR-------GKrrglrrgLTKKRRELFRELLATLGLglENR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 142 VNKNINEISDGERQRV-MIARTLAQdtP-VIVLDEPTAFLDlPNKYEIV-HLLNNLSKTENKTIIFSTHDLNIAI 213
Cdd:COG1101 142 LDTKVGLLSGGQRQALsLLMATLTK--PkLLLLDEHTAALD-PKTAALVlELTEKIVEENNLTTLMVTHNMEQAL 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-235 |
1.99e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.91 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNsIQGDILLNKkniIGYSRADFARLVSFVSTEIVNINNLRVFDLV 107
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAEK---LEFNGQDLQRISEKERRNLVGAEVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 ALGRFP-HTNWFGKLET-KDLKSVSKA---------LEMVGM---KSFVNKNINEISDGERQRVMIARTLAQDTPVIVLD 173
Cdd:PRK11022 99 MTSLNPcYTVGFQIMEAiKVHQGGNKKtrrqraidlLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 174 EPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE-GAPEDL 235
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVEtGKAHDI 241
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-239 |
2.33e-10 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 60.23 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKN-----IIGYSRADFARLV----SFVSTEIVNIN 99
Cdd:TIGR02323 20 RDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRLMrtewGFVHQNPRDGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 NLRVF-------DLVALG-------RFPHTNWFGKLE-----TKDLKSvskalemvgmksfvnkninEISDGERQRVMIA 160
Cdd:TIGR02323 100 RMRVSaganigeRLMAIGarhygniRATAQDWLEEVEidptrIDDLPR-------------------AFSGGMQQRLQIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLILNE 239
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
28-210 |
2.87e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL--QNSIQGDILLNKKNIIGYSRADFARL-VSFVSTEIVNINNLRVF 104
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DLVALGRFPHTNWFGKLETKDLKSvSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLdlpNK 184
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRA-QKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL---TE 176
|
170 180
....*....|....*....|....*...
gi 1082420396 185 YEIVHLLNNLS--KTENKTIIFSTHDLN 210
Cdd:PRK13549 177 SETAVLLDIIRdlKAHGIACIYISHKLN 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
31-208 |
3.05e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.97 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEivninnlrvFDLvalg 110
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSD---------FHL---- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 111 rFPHTnwFGKLETKDLKSVSKALEMVGMK---SFVNKNI--NEISDGERQRV-MIArTLAQDTPVIVLDEPTA------- 177
Cdd:COG4615 418 -FDRL--LGLDGEADPARARELLERLELDhkvSVEDGRFstTDLSQGQRKRLaLLV-ALLEDRPILVFDEWAAdqdpefr 493
|
170 180 190
....*....|....*....|....*....|...
gi 1082420396 178 --FldlpnkYEivHLLNNLsKTENKTIIFSTHD 208
Cdd:COG4615 494 rvF------YT--ELLPEL-KARGKTVIAISHD 517
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-239 |
3.47e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 59.27 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 6 HILEIHNLEIGYhiSKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIG---YSRA 82
Cdd:COG1137 2 MTLEAENLVKSY--GKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 83 dfaRL-VSFVSTE--IvninnlrvfdlvalgrfphtnwFGKLETKD-LKSVskaLEMVG-------------MKSFvnkN 145
Cdd:COG1137 77 ---RLgIGYLPQEasI----------------------FRKLTVEDnILAV---LELRKlskkereerleelLEEF---G 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 146 INEI--------SDGERQRVMIARTLAQDTPVIVLDEPTAFLDlPnkyeivhllnnLSKTENKTIIFSTHDLNIAI---- 213
Cdd:COG1137 126 ITHLrkskayslSGGERRRVEIARALATNPKFILLDEPFAGVD-P-----------IAVADIQKIIRHLKERGIGVlitd 193
|
250 260 270
....*....|....*....|....*....|....
gi 1082420396 214 ---QET----DKIWLMLNDSII-EGAPEDLILNE 239
Cdd:COG1137 194 hnvRETlgicDRAYIISEGKVLaEGTPEEILNNP 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
30-208 |
1.12e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY--------SRADFARLVSFVSTEIVNInnL 101
Cdd:TIGR03719 23 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYlpqepqldPTKTVRENVEEGVAEIKDA--L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 102 RVFDLVALGRFPHTNWFGKL-----------ETKDLKSVSKALEMVgMKSFV----NKNINEISDGERQRVMIARTLAQD 166
Cdd:TIGR03719 101 DRFNEISAKYAEPDADFDKLaaeqaelqeiiDAADAWDLDSQLEIA-MDALRcppwDADVTKLSGGERRRVALCRLLLSK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1082420396 167 TPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHD 208
Cdd:TIGR03719 180 PDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-222 |
2.32e-09 |
|
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: 58.30 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 2 ETRKHILEIHNLEiGYHISKRiHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL-QNSIQGDILLNKKNIIGYS 80
Cdd:TIGR02633 252 EIGDVILEARNLT-CWDVINP-HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 81 RADFARL-VSFVSTE-----IVNINNL-RVFDLVALGRFphtNWFGKL-ETKDLKSVSKALEMVGMKSFV-NKNINEISD 151
Cdd:TIGR02633 330 PAQAIRAgIAMVPEDrkrhgIVPILGVgKNITLSVLKSF---CFKMRIdAAAELQIIGSAIQRLKVKTASpFLPIGRLSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
31-208 |
2.35e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKniigysradfarlvsfvsteivNINNLR-------- 102
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR----------------------VVNELEpadrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 103 VFDLVALgrFPHTNWFGKLE--------TKDL--KSVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK11650 81 VFQNYAL--YPHMSVRENMAyglkirgmPKAEieERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1082420396 173 DEPTAFLD--------LpnkyEIVHLLNNLskteNKTIIFSTHD 208
Cdd:PRK11650 159 DEPLSNLDaklrvqmrL----EIQRLHRRL----KTTSLYVTHD 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
31-222 |
3.31e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL-VSFVSTEIVNINNLRVFDLVAL 109
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNLSVKENILF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 110 GRFPHTNWFGKLETKdLKSVSKALEMVgmksfVNKNINEISDgeRQRVMIARTLAQDTPVIVLDEPTAFLdlpNKYEIVH 189
Cdd:PRK15439 110 GLPKRQASMQKMKQL-LAALGCQLDLD-----SSAGSLEVAD--RQIVEILRGLMRDSRILILDEPTASL---TPAETER 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1082420396 190 LLNNLSKTENKT--IIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK15439 179 LFSRIRELLAQGvgIVFISHKLPEIRQLADRISVM 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-229 |
3.45e-09 |
|
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: 55.88 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGY--HISKRIHNslvsnINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFA 85
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKN-----VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RLVSFVSTEIVNI-----NNLRVFDlvalgrfphtnwfgklETKDlKSVSKALEmvgmksfVNKNINEISDGERQRVMIA 160
Cdd:cd03369 82 SSLTIIPQDPTLFsgtirSNLDPFD----------------EYSD-EEIYGALR-------VSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 161 RTLAQDTPVIVLDEPTAFLDlpnkYEIVHLLNNLSKTE--NKTIIFSTHDLNiAIQETDKIWLMLNDSIIE 229
Cdd:cd03369 138 RALLKRPRVLVLDEATASID----YATDALIQKTIREEftNSTILTIAHRLR-TIIDYDKILVMDAGEVKE 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
8-207 |
6.58e-09 |
|
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: 54.47 E-value: 6.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIgyhiSKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGdillnkkNIIGYSRADFArl 87
Cdd:cd03223 1 IELENLSL----ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-------RIGMPEGEDLL-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 vsFVSTE-IVNINNLRvfDLVAlgrFPhtnWFGKLetkdlksvskalemvgmksfvnknineiSDGERQRVMIARTLAQD 166
Cdd:cd03223 68 --FLPQRpYLPLGTLR--EQLI---YP---WDDVL----------------------------SGGEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1082420396 167 TPVIVLDEPTAFLDLPNKYEIVHLLNNLSktenKTIIFSTH 207
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
7-239 |
7.47e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHISKRIHNslvsnINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHE-----VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 -LVSFVSTEIVNINNLRVFDLVALGRFphtnwFGKlETKDLKSVSKALEMVG-MKSFVNKNINEISDGERQRVMIARTLA 164
Cdd:PRK11614 80 eAVAIVPEGRRVFSRMTVEENLAMGGF-----FAE-RDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 165 QDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKIWLMLNDSII-EGAPEDLILNE 239
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVlEDTGDALLANE 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
67-219 |
8.98e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 67 GDILLNKKNIIGYSRADFARLVSFVSTEIVnINNLRVFDLVALGRfphtnwfgklETKDLKSVSKALEMVGMKSFVNKNI 146
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPM-LFNMSIYENIKFGK----------EDATREDVKRACKFAAIDEFIESLP 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 147 NE-----------ISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLnIAIQE 215
Cdd:PTZ00265 1346 NKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKR 1424
|
....
gi 1082420396 216 TDKI 219
Cdd:PTZ00265 1425 SDKI 1428
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-208 |
9.71e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 9.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHN--LEIGYHiskrihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADF 84
Cdd:PRK11147 3 LISIHGawLSFSDA-------PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 85 ARLV-----SFVSTEIVNINNL-----RVFDLVA----------LGR----FPHTN-WfgKLETKdLKSVSKALEMVGmk 139
Cdd:PRK11147 76 PRNVegtvyDFVAEGIEEQAEYlkryhDISHLVEtdpseknlneLAKlqeqLDHHNlW--QLENR-INEVLAQLGLDP-- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1082420396 140 sfvNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHD 208
Cdd:PRK11147 151 ---DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-180 |
1.05e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNiIGYSRADFAR 86
Cdd:PRK13540 1 MLDVIELDFDYH-----DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-IKKDLCTYQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEI-VNIN-NLR---VFDLvalgrfpHTNwFGKLETKDLKSVSKalemvgMKSFVNKNINEISDGERQRVMIAR 161
Cdd:PRK13540 75 QLCFVGHRSgINPYlTLRencLYDI-------HFS-PGAVGITELCRLFS------LEHLIDYPCGLLSSGQKRQVALLR 140
|
170
....*....|....*....
gi 1082420396 162 TLAQDTPVIVLDEPTAFLD 180
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALD 159
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-222 |
1.22e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTE------IVNINNLRvf 104
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEdrkaegIIPVHSVA-- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DLVALGRFPHTNWFGKL-----ETKDLKSVSKALEmVGMKSfVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:PRK11288 350 DNINISARRHHLRAGCLinnrwEAENADRFIRSLN-IKTPS-REQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1082420396 180 DLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK11288 428 DVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVM 469
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-256 |
1.38e-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: 56.46 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 25 NSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSiQGDILLNKkniigysradfarlvsfVSTEIVNINNLR-V 103
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDG-----------------VSWNSVTLQTWRkA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDLVALGRFPHTNWFGK----LETKDLKSVSKALEMVGMKSFVNKNINEI-----------SDGERQRVMIARTLAQDTP 168
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKnldpYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAK 1373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 169 VIVLDEPTAFLDlPNKYEIVHllNNLSKT-ENKTIIFSTHDLNiAIQETDKIWLMLNDSIIEGAPEDLILNET--FNQIF 245
Cdd:TIGR01271 1374 ILLLDEPSAHLD-PVTLQIIR--KTLKQSfSNCTVILSEHRVE-ALLECQQFLVIEGSSVKQYDSIQKLLNETslFKQAM 1449
|
250
....*....|.
gi 1082420396 246 DNSklsfDRVK 256
Cdd:TIGR01271 1450 SAA----DRLK 1456
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-229 |
1.45e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 55.98 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 16 GYHISKRIhnslVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNI------------------- 76
Cdd:COG5265 366 GYDPERPI----LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdvtqaslraaigivpqdt 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 ----------IGYSRADFARlvsfvsTEIVninnlRVFDLVALGRFphtnwfgkletkdLKSVSKALE-MVG---MKsfv 142
Cdd:COG5265 442 vlfndtiaynIAYGRPDASE------EEVE-----AAARAAQIHDF-------------IESLPDGYDtRVGergLK--- 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 143 nknineISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKteNKTIIFSTHDLNiAIQETDKIWLM 222
Cdd:COG5265 495 ------LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLS-TIVDADEILVL 565
|
....*..
gi 1082420396 223 LNDSIIE 229
Cdd:COG5265 566 EAGRIVE 572
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
7-61 |
1.85e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 54.32 E-value: 1.85e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 7 ILEIHNLEIGYHISKRIHNSL-----------------VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL 61
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSLkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI 75
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-224 |
3.86e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLeigyhisKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAD--- 83
Cdd:PRK10982 250 ILEVRNL-------TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEain 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 84 --FArLVS--FVSTEIVNINNLRVFDLVALGRfPHTNWFGKLETKDLKSVSK-ALEMVGMKSFVNK-NINEISDGERQRV 157
Cdd:PRK10982 323 hgFA-LVTeeRRSTGIYAYLDIGFNSLISNIR-NYKNKVGLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKV 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLMLN 224
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSN 466
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
38-238 |
5.36e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 38 GELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVninnlrVFD-LVALGRFPHtn 116
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPV------LFDgTVRQNVDPF-- 1407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 117 wfgkLETKDlKSVSKALEMVGMKSFVNKNINEI-----------SDGERQRVMIART-LAQDTPVIVLDEPTAFLDLPNK 184
Cdd:PTZ00243 1408 ----LEASS-AEVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQLMCMARAlLKKGSGFILMDEATANIDPALD 1482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 185 YEIVHLLnnLSKTENKTIIFSTHDLNIAIQeTDKIWLMLNDSIIE-GAPEDLILN 238
Cdd:PTZ00243 1483 RQIQATV--MSAFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEmGSPRELVMN 1534
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-61 |
6.86e-08 |
|
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: 52.53 E-value: 6.86e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1082420396 8 LEIHNLEIGYHISKRIHNSL-----------------VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL 61
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLkklgilgrkgevgefwaLKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI 71
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-232 |
6.95e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKniigysradfarlVSFVSTEiVNINNLRVFDLVALG 110
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQ-AWIQNDSLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 111 RfphtnwfgKLETKDLKSVSKA------LEMV--GMKSFV-NKNINeISDGERQRVMIARTLAQDTPVIVLDEPTAFLDL 181
Cdd:TIGR00957 723 K--------ALNEKYYQQVLEAcallpdLEILpsGDRTEIgEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 182 P-NKYEIVHLLNNLSKTENKTIIFSTHDLNIaIQETDKIWLMLNDSIIEGAP 232
Cdd:TIGR00957 794 HvGKHIFEHVIGPEGVLKNKTRILVTHGISY-LPQVDVIIVMSGGKISEMGS 844
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
28-219 |
7.06e-08 |
|
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: 53.68 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL--QNSIQGDILLNKKNIIGYSRADFARL-VSFVSTEIVNINNLRVF 104
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 105 DLVALGR---FPHTNWFGKLETKDLKSVSKALEMVGMKsfVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDL 181
Cdd:TIGR02633 97 ENIFLGNeitLPGGRMAYNAMYLRAKNLLRELQLDADN--VTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1082420396 182 PNKYEIVHLLNNLsKTENKTIIFSTHDLNIAIQETDKI 219
Cdd:TIGR02633 175 KETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTI 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
29-210 |
1.45e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGL--QNSIQGDILLNK-----KNIigysRADFARLVSFVSTEIVNINNL 101
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGevcrfKDI----RDSEALGIVIIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 102 RVFDLVALG----RFPHTNWFG-KLETKDLksvskaLEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:NF040905 94 SIAENIFLGneraKRGVIDWNEtNRRAREL------LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1082420396 177 AFLdlpNKYEIVHLLNNLS--KTENKTIIFSTHDLN 210
Cdd:NF040905 168 AAL---NEEDSAALLDLLLelKAQGITSIIISHKLN 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-180 |
2.53e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY---SRADFArlvsfvsteivniNNLRV 103
Cdd:PRK11819 339 LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYvdqSRDALD-------------PNKTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDLVALGRfpHTNWFGKLETKdlksvSKAleMVGMKSFV----NKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFL 179
Cdd:PRK11819 406 WEEISGGL--DIIKVGNREIP-----SRA--YVGRFNFKggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDL 476
|
.
gi 1082420396 180 D 180
Cdd:PRK11819 477 D 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-232 |
2.58e-07 |
|
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: 49.88 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 36 SEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDillnkkniigysradfarlvsfvsteivninnlrvfdlvalgrfphT 115
Cdd:cd03222 23 KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN----------------------------------------------D 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 116 NWfgkletkDLKSVSKALEMVgmksfvnkninEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLS 195
Cdd:cd03222 57 EW-------DGITPVYKPQYI-----------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180 190
....*....|....*....|....*....|....*..
gi 1082420396 196 KTENKTIIFSTHDLNIAIQETDKIwlmlndSIIEGAP 232
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRI------HVFEGEP 149
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-222 |
3.11e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADfaRLVS--------------FVSTE 94
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ--RLARglvylpedrqssglYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 95 IV-NINNLRVFDLvalGRFPHTnwfgKLETKDLKSVSKALemvGMK-SFVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK15439 358 LAwNVCALTHNRR---GFWIKP----ARENAVLERYRRAL---NIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIAIQETDKIWLM 222
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-196 |
3.34e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.85 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIgYHISKRiHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGL-QNSIQGDILLNKKNIIGYSRADFA 85
Cdd:PRK13549 259 ILEVRNLTA-WDPVNP-HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RL-VSFVSTE-----IV-------NINnlrvfdLVALGRFPHtnwFGKL-ETKDLKSVSKALEMVGMK-SFVNKNINEIS 150
Cdd:PRK13549 337 AQgIAMVPEDrkrdgIVpvmgvgkNIT------LAALDRFTG---GSRIdDAAELKTILESIQRLKVKtASPELAIARLS 407
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1082420396 151 DGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSK 196
Cdd:PRK13549 408 GGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ 453
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-222 |
7.08e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 2 ETRKHILEIHNL--EIGYHISKRIhnsLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS---IQGDILLNkkni 76
Cdd:TIGR00956 754 ESGEDIFHWRNLtyEVKIKKEKRV---ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVN---- 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 77 iGYSR-ADFARLVSFVSTEIVNINNLRV---FDLVALGRFPhtNWFGKLETKDLksVSKALEMVGMKSFVNKNINEISDG 152
Cdd:TIGR00956 827 -GRPLdSSFQRSIGYVQQQDLHLPTSTVresLRFSAYLRQP--KSVSKSEKMEY--VEEVIKLLEMESYADAVVGVPGEG 901
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 153 ----ERQRVMIARTLAQDTPVIV-LDEPTAFLDLPNKYEIVHLLNNLSKTeNKTIIFSTHDLNIAI-QETDKIWLM 222
Cdd:TIGR00956 902 lnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHQPSAILfEEFDRLLLL 976
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
38-213 |
9.34e-07 |
|
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: 47.75 E-value: 9.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 38 GELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILlnkkniigysradfarlvsFVSTEIVNINNLRVFDLVALGRFPHtnw 117
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------YIDGEDILEEVLDQLLLIIVGGKKA--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 118 fgkletkdlksvskalemvgmksfvnkninEISDGERQRVMIARTLAQDTPVIVLDEPTAFLD-----LPNKYEIVHLLN 192
Cdd:smart00382 60 ------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDaeqeaLLLLLEELRLLL 109
|
170 180
....*....|....*....|.
gi 1082420396 193 NLSKTENKTIIFSTHDLNIAI 213
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG 130
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-180 |
1.03e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLeigyHISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFAR 86
Cdd:COG3845 257 VLEVENL----SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRR 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 L-VSFVSTE-----IVniNNLRVFDLVALGRFpHTNWFGK---LETKDLKSVSKALemvgMKSF------VNKNINEISD 151
Cdd:COG3845 333 LgVAYIPEDrlgrgLV--PDMSVAENLILGRY-RRPPFSRggfLDRKAIRAFAEEL----IEEFdvrtpgPDTPARSLSG 405
|
170 180
....*....|....*....|....*....
gi 1082420396 152 GERQRVMIARTLAQDTPVIVLDEPTAFLD 180
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
29-237 |
2.26e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.38 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKK-----NIIGYSRADFARLVSfvsTE--IVNIN-- 99
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLR---TEwgFVHQHpr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 100 -NLRVF---------DLVALG-------RFPHTNWFGKLE-----TKDLKSvskalemvgmkSFvnknineiSDGERQRV 157
Cdd:PRK11701 100 dGLRMQvsaggnigeRLMAVGarhygdiRATAGDWLERVEidaarIDDLPT-----------TF--------SGGMQQRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 158 MIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIEGAPEDLIL 237
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-235 |
4.42e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYS--------RAD------FARLVSFVS 92
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFaqhqleflRADesplqhLARLAPQEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 93 TEivninNLRVFdlvaLGRFPHTnwfgkletkdlksvskalemvGMKsfVNKNINEISDGERQRVMIARTLAQDTPVIVL 172
Cdd:PRK10636 407 EQ-----KLRDY----LGGFGFQ---------------------GDK--VTEETRRFSGGEKARLVLALIVWQRPNLLLL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1082420396 173 DEPTAFLDLPNKYEIVHLLNNLsktENKTIIFStHDLNIAIQETDKIWLmLNDSIIEGAPEDL 235
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDF---EGALVVVS-HDRHLLRSTTDDLYL-VHDGKVEPFDGDL 512
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-239 |
4.93e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.58 E-value: 4.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 31 INLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARLVSFVSTEIVNINNLRVFDLVALG 110
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 111 RFPHTNWFGKLETKDLKSVSKAlEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHL 190
Cdd:PLN03130 1338 EHNDADLWESLERAHLKDVIRR-NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKT 1416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1082420396 191 LNNLSKTENKTIIfsTHDLNIAIqETDKIWLMLNDSIIE-GAPEDLILNE 239
Cdd:PLN03130 1417 IREEFKSCTMLII--AHRLNTII-DCDRILVLDAGRVVEfDTPENLLSNE 1463
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
38-222 |
6.15e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.30 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 38 GELIAVIGKNGVGKSTLLRNIAGLQNS--IQGDIllnkkNIIGYSRAD--FARLVSFV-STEI----VNINNLRVFDlvA 108
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDI-----RISGFPKKQetFARISGYCeQNDIhspqVTVRESLIYS--A 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 109 LGRFPhtnwfgKLETKDLKS--VSKALEMVGMKSFVNK-----NINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDL 181
Cdd:PLN03140 979 FLRLP------KEVSKEEKMmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1082420396 182 PNKYEIVHLLNNLSKTeNKTIIFSTHDLNIAIQET-DKIWLM 222
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDT-GRTVVCTIHQPSIDIFEAfDELLLM 1093
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-210 |
7.59e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 28 VSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDIllnkkNIIGysRADFARLVSFVSTEIVNINNLRVFDLV 107
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG--SAALIAISSGLNGQLTGIENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 108 AlgrfphtnwfgKLETKDLKSVS-KALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYE 186
Cdd:PRK13545 113 M-----------GLTKEKIKEIIpEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|....
gi 1082420396 187 IVHLLNNLsKTENKTIIFSTHDLN 210
Cdd:PRK13545 182 CLDKMNEF-KEQGKTIFFISHSLS 204
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-211 |
8.01e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLRNIAG----------LQNSI----QGDILLN---KKNIIGYSRADFARLvs 89
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqfeisegrvwAERSIayvpQQAWIMNatvRGNILFFDEEDAARL-- 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 90 fvsTEIVNINNLRVfDLVALGrfphtnwfGKLETKdlksvskalemVGMKSfVNknineISDGERQRVMIARTLAQDTPV 169
Cdd:PTZ00243 753 ---ADAVRVSQLEA-DLAQLG--------GGLETE-----------IGEKG-VN-----LSGGQKARVSLARAVYANRDV 803
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1082420396 170 IVLDEPTAFLDLPNKYEIVH--LLNNLSkteNKTIIFSTHDLNI 211
Cdd:PTZ00243 804 YLLDDPLSALDAHVGERVVEecFLGALA---GKTRVLATHQVHV 844
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-239 |
1.14e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 46.06 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 8 LEIHNLEIGYHISKRihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRADFARL 87
Cdd:cd03288 20 IKIHDLCVRYENNLK---PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 88 VSFVSTEIVNINNLRVFDLVALGRFPHTNWFGKLETKDLKSVSKALEMvGMKSFVNKNINEISDGERQRVMIARTLAQDT 167
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPG-GLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 168 PVIVLDEPTAFLDLPNKyeivHLLNNLSKT--ENKTIIFSTHDLNiAIQETDKIWLMLNDSIIE-GAPEDLILNE 239
Cdd:cd03288 176 SILIMDEATASIDMATE----NILQKVVMTafADRTVVTIAHRVS-TILDADLVLVLSRGILVEcDTPENLLAQE 245
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
25-256 |
1.19e-05 |
|
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: 46.39 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 25 NSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNsIQGDILLNKkniigysradfarlvsfVSTEIVNINNLR-V 103
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDG-----------------VSWNSVPLQKWRkA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 104 FDLVALGRFPHTNWF-------GKLETKDLKSVSkalEMVGMKSFVNKNINE-----------ISDGERQRVMIARTLAQ 165
Cdd:cd03289 79 FGVIPQKVFIFSGTFrknldpyGKWSDEEIWKVA---EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 166 DTPVIVLDEPTAFLDlPNKYEIvhllnnLSKTENK-----TIIFSTHDLNiAIQETDKIWLMLNDSIIEGAPEDLILNET 240
Cdd:cd03289 156 KAKILLLDEPSAHLD-PITYQV------IRKTLKQafadcTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
250
....*....|....*.
gi 1082420396 241 fnQIFDNSKLSFDRVK 256
Cdd:cd03289 228 --SHFKQAISPSDRLK 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-248 |
2.35e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 29 SNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGdillnkKNIIGYSRADFARLVSFVSTEIVNINNL------- 101
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD------ASVVIRGTVAYVPQVSWIFNATVRDNILfgspfdp 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 102 ----RVFDLVALGRfphtnwfgkletkDLKSVSKA-LEMVGMKSfVNknineISDGERQRVMIARTLAQDTPVIVLDEPT 176
Cdd:PLN03130 708 eryeRAIDVTALQH-------------DLDLLPGGdLTEIGERG-VN-----ISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1082420396 177 AFLDLPNKYEIvhlLNNLSKTE--NKTIIFSTHDLNIaIQETDKIWLMLNDSIIE-GAPEDLILN-ETFNQIFDNS 248
Cdd:PLN03130 769 SALDAHVGRQV---FDKCIKDElrGKTRVLVTNQLHF-LSQVDRIILVHEGMIKEeGTYEELSNNgPLFQKLMENA 840
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-196 |
2.35e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISK---RIHNSLVSNI-NLTASEGELIAVIGKNGVGKSTLLRNIAG--------LQNSIQGDILLNkkniigysradFA 85
Cdd:PRK10938 5 QISQgtfRLSDTKTLQLpSLTLNAGDSWAFVGANGSGKSALARALAGelpllsgeRQSQFSHITRLS-----------FE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 86 RLVSFVSTEIVNINNlrvfDLVAlgrfPHTNWFGK-------LETKDLKSVSKALEMVGMKSFVNKNINEISDGERQRVM 158
Cdd:PRK10938 74 QLQKLVSDEWQRNNT----DMLS----PGEDDTGRttaeiiqDEVKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTL 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 1082420396 159 IARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSK 196
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-208 |
2.59e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY----SRADFARLVsfvsTEIVNINNLRVFD 105
Cdd:PRK11819 25 DISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYlpqePQLDPEKTV----RENVEEGVAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 106 LVAlgRFPHTN--------WF-------GKLETK-------DLKSvskALEMVgMKSF----VNKNINEISDGERQRVMI 159
Cdd:PRK11819 101 ALD--RFNEIYaayaepdaDFdalaaeqGELQEIidaadawDLDS---QLEIA-MDALrcppWDAKVTKLSGGERRRVAL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082420396 160 ARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHD 208
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
30-209 |
4.41e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 30 NINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKK-NIIGYSRADFARLvsfvsTEIVNINnlrvFDLVA 108
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQL-----TGIENIE----FKMLC 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 109 LGrfphtnwFGKLETKDLksVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLD-------L 181
Cdd:PRK13546 113 MG-------FKRKEIKAM--TPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqtfaqkcL 183
|
170 180
....*....|....*....|....*...
gi 1082420396 182 PNKYEIvhllnnlsKTENKTIIFSTHDL 209
Cdd:PRK13546 184 DKIYEF--------KEQNKTIFFVSHNL 203
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
7-207 |
5.93e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGYHiskriHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNS--IQGDILLNKKNIIGYSRADF 84
Cdd:PRK09580 1 MLSIKDLHVSVE-----DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYevTGGTVEFKGKDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 85 ARLVSFVS----TEIVNINNlRVF---DLVALGRFPHTNWFGKLETKDLksVSKALEMVGM-KSFVNKNINE-ISDGERQ 155
Cdd:PRK09580 76 AGEGIFMAfqypVEIPGVSN-QFFlqtALNAVRSYRGQEPLDRFDFQDL--MEEKIALLKMpEDLLTRSVNVgFSGGEKK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 156 RVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTH 207
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
18-212 |
9.21e-05 |
|
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: 42.35 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 18 HISKRIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAglqnsiqgdillnkkniigysradfarlvsfvsteivn 97
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 98 innlrvfdLVALGRFPHTNWfGKLETKDLKSVSKALEMVGMksfvnknINEISDGERQRVMIARTLA----QDTPVIVLD 173
Cdd:cd03227 43 --------LALGGAQSATRR-RSGVKAGCIVAAVSAELIFT-------RLQLSGGEKELSALALILAlaslKPRPLYILD 106
|
170 180 190
....*....|....*....|....*....|....*....
gi 1082420396 174 EPTAFLDLPNKYEIVHLLNNLSKtENKTIIFSTHDLNIA 212
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPELA 144
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
156-208 |
2.13e-04 |
|
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: 41.82 E-value: 2.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1082420396 156 RVMIARTLAQDTPVIVLDEPTAFLDLPNKYE-IVHLLNNLSKTENKTIIFSTHD 208
Cdd:cd03240 129 RLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-219 |
2.41e-04 |
|
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: 41.15 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 17 YHISKRIHNSLvSNINLTASEGELIAVIGKNGVGKSTLLrniaglqnsiqgdillnkkNIIGYSRADfARLVSFVST--- 93
Cdd:cd03238 1 LTVSGANVHNL-QNLDVSIPLNVLVVVTGVSGSGKSTLV-------------------NEGLYASGK-ARLISFLPKfsr 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 94 -EIVNINNLRVFDLVALGRFPhtnwfgkletkdlksvskalemvgmksfVNKNINEISDGERQRVMIARTLAQDTP--VI 170
Cdd:cd03238 60 nKLIFIDQLQFLIDVGLGYLT----------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLF 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1082420396 171 VLDEPTAFLDLPNKYEIVHLLNNLsKTENKTIIFSTHDLNIaIQETDKI 219
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDV-LSSADWI 158
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-208 |
2.47e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 5 KHILEIHNLEigYHISKRihnSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGY---SR 81
Cdd:PRK11147 317 KIVFEMENVN--YQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYfdqHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 82 A--DFARLVsfvsteivnINNLR--VFDLVALGRFPHTnwFGKLEtkD-LKSVSKAleMVGMKSfvnknineISDGERQR 156
Cdd:PRK11147 392 AelDPEKTV---------MDNLAegKQEVMVNGRPRHV--LGYLQ--DfLFHPKRA--MTPVKA--------LSGGERNR 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1082420396 157 VMIARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHD 208
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-209 |
4.69e-04 |
|
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: 42.31 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 38 GELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYsradfarlVSFVSTEIVNINNLRVFDLVALGRfPHTNW 117
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN--------ISDVHQNMGYCPQFDAIDDLLTGR-EHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 118 FGKLETKDLKSVSK----ALEMVGMKSFVNKNINEISDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNN 193
Cdd:TIGR01257 2036 YARLRGVPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170
....*....|....*.
gi 1082420396 194 LSKtENKTIIFSTHDL 209
Cdd:TIGR01257 2116 IIR-EGRAVVLTSHSM 2130
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-229 |
1.15e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 27 LVSNINLTASEGELIAVIGKNGVGKSTLLrniAGLQNSIQGD------------ILLNKKN----------IIGYSRaDF 84
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLL---ALLKNEISADggsytfpgnwqlAWVNQETpalpqpaleyVIDGDR-EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 85 ARLVSfvSTEIVNINNlrvfDLVALGRFpHtnwfGKLETKDLKSV-SKALEMVGMKSFVNKN----INEISDGERQRVMI 159
Cdd:PRK10636 92 RQLEA--QLHDANERN----DGHAIATI-H----GKLDAIDAWTIrSRAASLLHGLGFSNEQlerpVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 160 ARTLAQDTPVIVLDEPTAFLDLpnkyEIVHLLNNLSKTENKTIIFSTHDLNIAIQETDKIWLMLNDSIIE 229
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDL----DAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
145-211 |
1.17e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 145 NINEISDGERQ---RVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKTENKtIIFSTHDLNI 211
Cdd:pfam13304 233 PAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQ-LILTTHSPLL 301
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
142-219 |
3.24e-03 |
|
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: 38.39 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 142 VNKNINEISDGERQRVMIARTLAQD-TPVI-VLDEPTAFLDLPNKYEIVHLLNNLSKTENkTIIFSTHDLNIaIQETDKI 219
Cdd:cd03270 131 LSRSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDT-IRAADHV 208
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
7-194 |
3.44e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 37.93 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 7 ILEIHNLEIGyhiskrIHNSLVSNINLTASEGELIAVIGKNGVGKSTLLRNIAGLQNSIQGDILLNKKNIIGYSRAdfar 86
Cdd:PRK13541 1 MLSLHQLQFN------IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1082420396 87 LVSFVSTEIVNINNLRVFD-LVALGRFphtnwFGKLETkdlksVSKALEMVGMKSFVNKNINEISDGERQRVMIARTLAQ 165
Cdd:PRK13541 71 YCTYIGHNLGLKLEMTVFEnLKFWSEI-----YNSAET-----LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIAC 140
|
170 180
....*....|....*....|....*....
gi 1082420396 166 DTPVIVLDEPTAFLDLPNKyeivHLLNNL 194
Cdd:PRK13541 141 QSDLWLLDEVETNLSKENR----DLLNNL 165
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
150-204 |
9.24e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.85 E-value: 9.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1082420396 150 SDGERQRVMIARTLAQDTPVIVLDEPTAFLDLPNKYEIVHLLNNLSKtENKTIIF 204
Cdd:NF040905 406 SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAA-EGKGVIV 459
|
|
| |
