|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-259 |
2.28e-131 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 371.62 E-value: 2.28e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDK 98
Cdd:COG0410 1 MPMLEVENLHAGYGG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIRFDGEDITGLPPHR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDR-EVGRDIEMVYNYFPRLKERTG-LAGYLSGGEQQMLAIGRALMAR 176
Cdd:COG0410 75 IARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRaEVRADLERVYELFPRLKERRRqRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 177 PKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKEFY 256
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAY 233
|
...
gi 501488905 257 LGG 259
Cdd:COG0410 234 LGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
22-249 |
9.43e-113 |
|
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: 324.00 E-value: 9.43e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:cd03224 1 LEVENLNAGYGK-SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGRDITGLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRLKERTG-LAGYLSGGEQQMLAIGRALMARPKMI 180
Cdd:cd03224 75 AGIGYVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKqLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 181 LMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN 249
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
20-259 |
2.79e-71 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 219.37 E-value: 2.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGllkteDGEVTRGEIVFDGERIDGTDPDKI 99
Cdd:PRK11614 4 VMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-----DPRATSGRIVFDGKDITDWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRLKER-TGLAGYLSGGEQQMLAIGRALMARPK 178
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERrIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 179 MILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKEFYLG 258
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
.
gi 501488905 259 G 259
Cdd:PRK11614 237 G 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
22-255 |
1.02e-67 |
|
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: 209.69 E-value: 1.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:TIGR03410 1 LEVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP-----VKSGSIRLDGEDITKLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREvgRDI-EMVYNYFPRLKE-RTGLAGYLSGGEQQMLAIGRALMARPKM 179
Cdd:TIGR03410 75 AGIAYVPQGREIFPRLTVEENLLTGLAALPRRS--RKIpDEIYELFPVLKEmLGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 180 ILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELrDNEDVKEF 255
Cdd:TIGR03410 153 LLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL-DEDKVRRY 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-262 |
2.33e-66 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 207.20 E-value: 2.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 18 PAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPD 97
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYR-----PTSGRILFDGRDITGLPPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRRGI---FQVMegrRIVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRLK----------ERTGLAGY------ 158
Cdd:COG0411 75 RIARLGIartFQNP---RLFPELTVLENVLVAAHARLGRGLLAALLRLPRARREEReareraeellERVGLADRadepag 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 -LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:COG0411 152 nLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
250 260
....*....|....*....|....*
gi 501488905 238 VLDGTADELRDNEDVKEFYLGGAGD 262
Cdd:COG0411 232 IAEGTPAEVRADPRVIEAYLGEEAA 256
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
22-252 |
4.43e-60 |
|
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: 190.73 E-value: 4.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:cd03219 1 LEVRGLTKRFGGL-VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLR-----PTSGSVLFDGEDITGLPPHEIAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGI---FQVMegrRIVSDMTSLENLRLGAFTRSDR-----EVGRDIEMVYNYFPRLKERTGL-------AGYLSGGEQQM 166
Cdd:cd03219 75 LGIgrtFQIP---RLFPELTVLENVMVAAQARTGSglllaRARREEREARERAEELLERVGLadladrpAGELSYGQQRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 167 LAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
....*.
gi 501488905 247 RDNEDV 252
Cdd:cd03219 231 RNNPRV 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
22-252 |
3.33e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 3.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDgTDPDKiVR 101
Cdd:COG1131 1 IEVRGLTKRYGDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR-----PTSGEVRVLGEDVA-RDPAE-VR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLRL--GAFTRSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQQMLAIGRA 172
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFfaRLYGLPRKEARERID-------ELLELFGLTDAadrkvgtLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 173 LMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN--E 250
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARllE 224
|
..
gi 501488905 251 DV 252
Cdd:COG1131 225 DV 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
22-258 |
3.92e-47 |
|
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: 157.32 E-value: 3.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:cd03218 1 LRAENLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGKILLDGQDITKLPMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLR--LGAFTRSDREVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKM 179
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILavLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 180 ILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKEFYLG 258
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
22-251 |
7.01e-45 |
|
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: 151.33 E-value: 7.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-----PTSGEVLVDGKDITKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 R-GI-FQ------VMEgrrIVSD--MTSLENLRLgaftrSDREVGRDIEMVynyfprLkERTGLAGY-------LSGGEQ 164
Cdd:COG1122 76 KvGLvFQnpddqlFAP---TVEEdvAFGPENLGL-----PREEIRERVEEA------L-ELVGLEHLadrppheLSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTAD 244
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
....*..
gi 501488905 245 ELRDNED 251
Cdd:COG1122 220 EVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
17-255 |
3.85e-44 |
|
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: 149.74 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 17 APAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDP 96
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR-----PDSGEILVDGQDITGLSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKI--VRRGI---FQvmeGRRIVSDMTSLEN--LRLGAFTR-SDREVgrdIEMVynyfpRLK-ERTGLAGY-------LS 160
Cdd:COG1127 75 KELyeLRRRIgmlFQ---GGALFDSLTVFENvaFPLREHTDlSEAEI---RELV-----LEKlELVGLPGAadkmpseLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLD 240
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*..
gi 501488905 241 GTADELR--DNEDVKEF 255
Cdd:COG1127 224 GTPEELLasDDPWVRQF 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-260 |
7.81e-44 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 149.37 E-value: 7.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDK 98
Cdd:PRK11300 3 QPLLSVSGLMMRFGG-LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKP-----TGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRRGIFQVMEGRRIVSDMTSLENL-----------------RLGAFTRSDREVgrdIEMVYNYFprlkERTGL------ 155
Cdd:PRK11300 77 IARMGVVRTFQHVRLFREMTVIENLlvaqhqqlktglfsgllKTPAFRRAESEA---LDRAATWL----ERVGLlehanr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 156 -AGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQ 234
Cdd:PRK11300 150 qAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250 260
....*....|....*....|....*.
gi 501488905 235 GKVVLDGTADELRDNEDVKEFYLGGA 260
Cdd:PRK11300 230 GTPLANGTPEEIRNNPDVIKAYLGEA 255
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
22-256 |
6.16e-41 |
|
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: 141.55 E-value: 6.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKI-- 99
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLV-----EPTSGSVLIDGTDINKLKGKALrq 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLENL---RLGA----------FTRSDREVGRdiemvynyfpRLKERTGL-------AGYL 159
Cdd:cd03256 76 LRRQIGMIFQQFNLIERLSVLENVlsgRLGRrstwrslfglFPKEEKQRAL----------AALERVGLldkayqrADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 160 SGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVL 239
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
250
....*....|....*..
gi 501488905 240 DGTADELrDNEDVKEFY 256
Cdd:cd03256 226 DGPPAEL-TDEVLDEIY 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-258 |
6.39e-41 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 141.32 E-value: 6.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKI 99
Cdd:COG1137 2 MTLEAENLVKSYGKRT-VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGRIFLDGEDITHLPMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGI---------FQvmegrrivsDMTSLENLR----LGAFTRSDREvgRDIEMVYNYFPRLKERTGLAGYLSGGEQQM 166
Cdd:COG1137 76 ARLGIgylpqeasiFR---------KLTVEDNILavleLRKLSKKERE--ERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 167 LAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
250
....*....|..
gi 501488905 247 RDNEDVKEFYLG 258
Cdd:COG1137 224 LNNPLVRKVYLG 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
21-257 |
3.10e-40 |
|
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: 139.61 E-value: 3.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGEriDGTDPDKIV 100
Cdd:COG4555 1 MIEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLK-----PDSGSILIDGE--DVRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDMTSLENLRLGA--FTRSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQQMLAIGR 171
Cdd:COG4555 73 RRQIGVLPDERGLYDRLTVRENIRYFAelYGLFDEELKKRIE-------ELIELLGLEEFldrrvgeLSTGMKKKVALAR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRD--- 248
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREeig 224
|
....*....
gi 501488905 249 NEDVKEFYL 257
Cdd:COG4555 225 EENLEDAFV 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-256 |
5.88e-40 |
|
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: 139.41 E-value: 5.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIV 100
Cdd:COG1120 1 MLEAENLSVGYGGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-----PSSGEVLLDGRDLASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RR-GIfqVMEGRRIVSDMTSLENLRLG------AFTRSDREvgrDIEMVYNYFprlkERTGLAGY-------LSGGEQQM 166
Cdd:COG1120 75 RRiAY--VPQEPPAPFGLTVRELVALGryphlgLFGRPSAE---DREAVEEAL----ERTGLEHLadrpvdeLSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 167 LAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
250
....*....|
gi 501488905 247 RDNEDVKEFY 256
Cdd:COG1120 226 LTPELLEEVY 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
22-258 |
1.01e-39 |
|
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: 138.18 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDKIVR 101
Cdd:TIGR04406 2 LVAENLIKSYKKR-KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIL-----IDGQDITHLPMHERAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLRLGAFTRSD---REVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPK 178
Cdd:TIGR04406 76 LGIGYLPQEASIFRKLTVEENIMAVLEIRKDldrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 179 MILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKEFYLG 258
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
22-237 |
8.25e-39 |
|
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: 133.68 E-value: 8.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIdGTDPDKIVR 101
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-----PDSGEIKVLGKDI-KKEPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RgIFQVMEGRRIVSDMTSLENLRlgaftrsdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMARPKMIL 181
Cdd:cd03230 74 R-IGYLPEEPSLYENLTVRENLK----------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 182 MDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-246 |
1.14e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 138.69 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 18 PAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPD 97
Cdd:COG3842 2 AMPALELENVSKRYGDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFE-----TPDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KivrRGI---FQvmegrrivSD-----MTSLEN----LRLGAFTRSDRE--VGRDIEMVynyfprlkertGLAGY----- 158
Cdd:COG3842 76 K---RNVgmvFQ--------DYalfphLTVAENvafgLRMRGVPKAEIRarVAELLELV-----------GLEGLadryp 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 --LSGGEQQMLAIGRALMARPKMILMDEPsmgLSPL---LVKEVFAIIQQINRDLGVTILLV-----EqnaraALSVASH 228
Cdd:COG3842 134 hqLSGGQQQRVALARALAPEPRVLLLDEP---LSALdakLREEMREELRRLQRELGITFIYVthdqeE-----ALALADR 205
|
250
....*....|....*...
gi 501488905 229 GYIMEQGKVVLDGTADEL 246
Cdd:COG3842 206 IAVMNDGRIEQVGTPEEI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-238 |
5.69e-38 |
|
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: 5.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDD---VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTD 95
Cdd:COG1136 2 SPLLELRNLTKSYGTgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDR-----PTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 96 PDKIVR-RG-----IFQvmeGRRIVSDMTSLEN----LRLGAFTRSDREvGRDIEMVynyfprlkERTGLAGY------- 158
Cdd:COG1136 77 ERELARlRRrhigfVFQ---FFNLLPELTALENvalpLLLAGVSRKERR-ERARELL--------ERVGLGDRldhrpsq 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAAlSVASHGYIMEQGKVV 238
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
22-241 |
1.22e-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: 132.26 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDkivR 101
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLE-----RPDSGEILIDGRDVTGVPPE---R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLEN----LRLGAFTRSDRE--VGRDIEMVynyfprlkertGLAGY-------LSGGEQQMLA 168
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENiafgLKLRGVPKAEIRarVRELLELV-----------GLEGLlnrypheLSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 169 IGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
22-255 |
1.76e-37 |
|
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: 132.24 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDP--DKI 99
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP-----DSGEVLIDGEDISGLSEaeLYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLEN--LRLGAFTRSDREVGRDI-----EMVynyfprlkertGLAGY-------LSGGEQQ 165
Cdd:cd03261 75 LRRRMGMLFQSGALFDSLTVFENvaFPLREHTRLSEEEIREIvleklEAV-----------GLRGAedlypaeLSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 166 MLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADE 245
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
250
....*....|..
gi 501488905 246 LR--DNEDVKEF 255
Cdd:cd03261 224 LRasDDPLVRQF 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
22-237 |
3.42e-37 |
|
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: 131.11 E-value: 3.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktedGEVTRGEIVFDGERIDGTDPD-KIV 100
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTIIIDGLKLTDDKKNiNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDMTSLENLRLG---AFTRSDREVgRDIEMvynyfpRLKERTGLA-------GYLSGGEQQMLAIG 170
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLApikVKGMSKAEA-EERAL------ELLEKVGLAdkadaypAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-238 |
9.86e-37 |
|
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: 128.32 E-value: 9.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:cd03216 1 LELRGITKRFGGVK-ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-----PDSGEILVDGKEVSFASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGifqvmegrrivsdmtslenlrlgaftrsdrevgrdIEMVYNyfprlkertglagyLSGGEQQMLAIGRALMARPKMIL 181
Cdd:cd03216 75 AG-----------------------------------IAMVYQ--------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 182 MDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVV 238
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
22-237 |
2.08e-36 |
|
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: 129.15 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDP-- 96
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR-----PTSGEVRVDGTDISKLSEke 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 -DKIVRR--G-IFQvmeGRRIVSDMTSLENLRLGAFTRSDRevGRDIEMVYNYfprLKERTGLAGY-------LSGGEQQ 165
Cdd:cd03255 76 lAAFRRRhiGfVFQ---SFNLLPDLTALENVELPLLLAGVP--KKERRERAEE---LLERVGLGDRlnhypseLSGGQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 166 MLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAAlSVASHGYIMEQGKV 237
Cdd:cd03255 148 RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
22-236 |
2.15e-36 |
|
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: 127.69 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERI-DGTDPDKIV 100
Cdd:cd03229 1 LELKNVSKRYGQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDSGSILIDGEDLtDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDMTSLENLRLGaftrsdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMARPKMI 180
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 181 LMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGK 236
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-255 |
2.24e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.34 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktEdgEVTRGEIVFDGERID--GTDPDK 98
Cdd:COG1126 1 MIEIENLHKSFGDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL---E--EPDSGTITVDGEDLTdsKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IvRRGI---FQvmegrrivS-----DMTSLENLRLGAFT--RSDREVGRDIEMvynyfpRLKERTGLAGY-------LSG 161
Cdd:COG1126 75 L-RRKVgmvFQ--------QfnlfpHLTVLENVTLAPIKvkKMSKAEAEERAM------ELLERVGLADKadaypaqLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 162 GEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEG 218
|
250
....*....|....*..
gi 501488905 242 TADELRDN---EDVKEF 255
Cdd:COG1126 219 PPEEFFENpqhERTRAF 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
19-249 |
7.40e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.88 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtEDGEVTrGEIVFDGERIDGTDPD 97
Cdd:COG1123 2 TPLLEVRDLSVRYpGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP-HGGRIS-GEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRR--GIFQvmegrrivSDMTSL----------ENLRLGAFTRSDREvGRDIEMVynyfprlkERTGLAGY------- 158
Cdd:COG1123 80 LRGRRigMVFQ--------DPMTQLnpvtvgdqiaEALENLGLSRAEAR-ARVLELL--------EAVGLERRldryphq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVV 238
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIV 222
|
250
....*....|.
gi 501488905 239 LDGTADELRDN 249
Cdd:COG1123 223 EDGPPEEILAA 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
22-246 |
1.06e-35 |
|
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: 127.30 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKI-V 100
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLeL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGI---FQvmegRRIVSDMTSLENLRLG--AFTRSDREVGRDI-----EMVYnYFPRLKERTGlAGYLSGGEQQMLAIG 170
Cdd:cd03260 80 RRRVgmvFQ----KPNPFPGSIYDNVAYGlrLHGIKLKEELDERveealRKAA-LWDEVKDRLH-ALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlgVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-236 |
1.40e-35 |
|
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: 126.81 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDD-VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDKIVR 101
Cdd:cd03225 1 ELKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVL-----VDGKDLTKLSLKELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 R-G-IFQ------VMEgrrIVSD--MTSLENLRLgaftrSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQ 164
Cdd:cd03225 76 KvGlVFQnpddqfFGP---TVEEevAFGLENLGL-----PEEEIEERVE-------EALELVGLEGLrdrspftLSGGQK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGK 236
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-249 |
4.17e-35 |
|
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: 131.95 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 8 HPPQPGASTAPAPLLSVRNIEVVYD----DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGE 83
Cdd:COG1123 247 RGRAAPAAAAAEPLLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 84 IVFDGERIDGTDPDKIVRRG-----IFQ--------VMEGRRIVSDmtSLENLRLGAFTRSDREVGRDIEMV------YN 144
Cdd:COG1123 322 ILFDGKDLTKLSRRSLRELRrrvqmVFQdpysslnpRMTVGDIIAE--PLRLHGLLSRAERRERVAELLERVglppdlAD 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 145 YFPRLkertglagyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALS 224
Cdd:COG1123 400 RYPHE---------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRY 470
|
250 260
....*....|....*....|....*
gi 501488905 225 VASHGYIMEQGKVVLDGTADELRDN 249
Cdd:COG1123 471 IADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-248 |
5.89e-35 |
|
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: 126.07 E-value: 5.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYD---DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIdGTDPD 97
Cdd:COG1124 1 MLEVRNLSVSYGqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER-----PWSGEVTFDGRPV-TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRRGI---FQ----VMEGRRIVsDMTSLENLRLGAFTRSDREVGRDIEMV---YNYFPRLKERtglagyLSGGEQQML 167
Cdd:COG1124 75 KAFRRRVqmvFQdpyaSLHPRHTV-DRILAEPLRIHGLPDREERIAELLEQVglpPSFLDRYPHQ------LSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 168 AIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELR 247
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
.
gi 501488905 248 D 248
Cdd:COG1124 228 A 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
24-247 |
2.72e-34 |
|
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: 123.63 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDVILVlRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDgTDPDKiVRRG 103
Cdd:cd03265 3 VENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK-----PTSGRATVAGHDVV-REPRE-VRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 104 IFQVMEGRRIVSDMTSLENL----RLGAFTRSDREvgRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKM 179
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLyihaRLYGVPGAERR--ERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 180 ILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELR 247
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-247 |
4.27e-34 |
|
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: 123.00 E-value: 4.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDgTDPDKIv 100
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR-----PTSGTAYINGYSIR-TDRKAA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDMTSLENLRLgaFTR----SDREVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMAR 176
Cdd:cd03263 74 RQSLGYCPQFDALFDELTVREHLRF--YARlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 177 PKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELR 247
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-241 |
4.42e-34 |
|
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: 121.77 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDPDKIVRR 102
Cdd:cd03214 1 EVENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL----------LDGKDLASLSPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 gifqvmEGRRIVSDM-TSLENLRLGAFtrSDREVGRdiemvynyfprlkertglagyLSGGEQQMLAIGRALMARPKMIL 181
Cdd:cd03214 70 ------ELARKIAYVpQALELLGLAHL--ADRPFNE---------------------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 182 MDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
16-215 |
5.45e-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: 124.05 E-value: 5.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 16 TAPAPLLSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERID 92
Cdd:COG1116 2 SAAAPALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK-----PTSGEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 93 GTDPDKIVrrgIFQvmegrrivSD-----MTSLENLRLGA-FTRSDREVGRDIEMvynyfpRLKERTGLAGY-------L 159
Cdd:COG1116 77 GPGPDRGV---VFQ--------EPallpwLTVLDNVALGLeLRGVPKAERRERAR------ELLELVGLAGFedayphqL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 160 SGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLV 215
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFV 195
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
23-236 |
1.42e-33 |
|
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: 119.66 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIdGTDPDKIVRR 102
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDI-AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 GIFQVMEgrrivsdmtslenlrlgaftrsdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMARPKMILM 182
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501488905 183 DEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGK 236
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
22-249 |
1.84e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.80 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKivr 101
Cdd:COG3839 4 LELENVSKSYGGVE-ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLE-----DPTSGEILIGGRDVTDLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGI---FQvmegrrivS-----DMTSLEN----LRLGAFTRSDRE--VGRDIEMVynyfprlkertGLAGY-------LS 160
Cdd:COG3839 75 RNIamvFQ--------SyalypHMTVYENiafpLKLRKVPKAEIDrrVREAAELL-----------GLEDLldrkpkqLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPsmgLS---PLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEP---LSnldAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
250
....*....|..
gi 501488905 238 VLDGTADELRDN 249
Cdd:COG3839 213 QQVGTPEELYDR 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
17-256 |
4.02e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 17 APAPLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIvfdgeRIDGTDP 96
Cdd:COG1121 2 MMMPAIELENLTVSYGGR-PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP-----PTSGTV-----RLFGKPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKiVRRGI------------FQ------VMEGRRivsdmtslenLRLGAFTRSDREvgrDIEMVYnyfpRLKERTGLAGY 158
Cdd:COG1121 71 RR-ARRRIgyvpqraevdwdFPitvrdvVLMGRY----------GRRGLFRRPSRA---DREAVD----EALERVGLEDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 -------LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYI 231
Cdd:COG1121 133 adrpigeLSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLL 211
|
250 260
....*....|....*....|....*
gi 501488905 232 MEQGkVVLDGTADELRDNEDVKEFY 256
Cdd:COG1121 212 LNRG-LVAHGPPEEVLTPENLSRAY 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
25-241 |
8.87e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.77 E-value: 8.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKI--VRR 102
Cdd:COG2884 5 ENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEER-----PTSGQVLVNGQDLSRLKRREIpyLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 GI---FQvmeGRRIVSDMTSLENLRLG--AFTRSDREVGRDIEMVynyfprLkERTGLAGY-------LSGGEQQMLAIG 170
Cdd:COG2884 80 RIgvvFQ---DFRLLPDRTVYENVALPlrVTGKSRKEIRRRVREV------L-DLVGLSDKakalpheLSGGEQQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdLGVTILlveqnaraalsVASHGY-----------IMEQGKVVL 239
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVL-----------IATHDLelvdrmpkrvlELEDGRLVR 217
|
..
gi 501488905 240 DG 241
Cdd:COG2884 218 DE 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-185 |
2.37e-32 |
|
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: 116.59 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGtDPDKIVRRGIFQVMEGRRIVSDM 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP-----TEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501488905 118 TSLENLRLGA--FTRSDREVGRDIEMVYNYFPR---LKERTGLAGY-LSGGEQQMLAIGRALMARPKMILMDEP 185
Cdd:pfam00005 75 TVRENLRLGLllKGLSKREKDARAEEALEKLGLgdlADRPVGERPGtLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
37-258 |
2.82e-32 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 118.84 E-value: 2.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEvtrgeIVFDGERIDGTDPDKIVRRGIFQVMEGRRIVSD 116
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGN-----IIIDDEDISLLPLHARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLENLRLGAFTRSD--REVGRD-IEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLL 193
Cdd:PRK10895 93 LSVYDNLMAVLQIRDDlsAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 194 VKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKEFYLG 258
Cdd:PRK10895 173 VIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-238 |
7.97e-32 |
|
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: 117.22 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDD---VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPD 97
Cdd:cd03257 1 LLEVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRRG-----IFQ---------------VMEGRRIVSDMTSLENLRLGAFtRSDREVGRDIEmVYNYFPRlkErtglag 157
Cdd:cd03257 76 LRKIRRkeiqmVFQdpmsslnprmtigeqIAEPLRIHGKLSKKEARKEAVL-LLLVGVGLPEE-VLNRYPH--E------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 158 yLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:cd03257 146 -LSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
.
gi 501488905 238 V 238
Cdd:cd03257 225 V 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
22-255 |
2.51e-31 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 116.63 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKIvR 101
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-----EPTSGEIFIDGEDIREQDPVEL-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLRL------GAFTRSDREVGRDIEMVynyfpRLKERTGLAGY---LSGGEQQMLAIGRA 172
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALvpkllkWPKEKIRERADELLALV-----GLDPAEFADRYpheLSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 173 LMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADE-LRD--N 249
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEiLRSpaN 229
|
....*.
gi 501488905 250 EDVKEF 255
Cdd:cd03295 230 DFVAEF 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
22-238 |
2.85e-31 |
|
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: 115.65 E-value: 2.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDD---VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDK 98
Cdd:cd03293 1 LEVRNVSKTYGGgggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER-----PTSGEVLVDGEPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVrrgIFQvmegrrivSD-----MTSLENLRLGAFTR--SDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQ 164
Cdd:cd03293 76 GY---VFQ--------QDallpwLTVLDNVALGLELQgvPKAEARERAE-------ELLELVGLSGFenayphqLSGGMR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQ--GKVV 238
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
37-255 |
4.52e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.96 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktedGEVTRGEIVFDGERIDGTDPD-KIVRRGIFQVMEGRRIVS 115
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDeRLIRQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 116 DMTSLENLRLGAF-TR-SDREVGRDIEMvynyfpRLKERTGLA-------GYLSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:PRK09493 91 HLTALENVMFGPLrVRgASKEEAEKQAR------ELLAKVGLAerahhypSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 187 MGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN---EDVKEF 255
Cdd:PRK09493 165 SALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNppsQRLQEF 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
22-249 |
7.23e-31 |
|
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: 115.03 E-value: 7.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktedGEVTRGEIVFDGERIDGTDPDKivr 101
Cdd:cd03300 1 IELENVSKFYGGFV-ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-----ETPTSGEILLDGKDITNLPPHK--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLEN----LRLGAFTRSD--REVGRDIEMVynyfprlkertGLAGY-------LSGGEQQMLA 168
Cdd:cd03300 72 RPVNTVFQNYALFPHLTVFENiafgLRLKKLPKAEikERVAEALDLV-----------QLEGYanrkpsqLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 169 IGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRD 248
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
.
gi 501488905 249 N 249
Cdd:cd03300 221 E 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-258 |
7.50e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 114.85 E-value: 7.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILvlrGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKivr 101
Cdd:COG3840 2 LRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFL-----PPDSGRILWNGQDLTALPPAE--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGI---FQvmegrrivsD------MTSLENLRLG-----AFTRSDREvgRDIEMVynyfprlkERTGLAGY-------LS 160
Cdd:COG3840 71 RPVsmlFQ---------EnnlfphLTVAQNIGLGlrpglKLTAEQRA--QVEQAL--------ERVGLAGLldrlpgqLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRAL-MARPkMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVL 239
Cdd:COG3840 132 GGQRQRVALARCLvRKRP-ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
250 260
....*....|....*....|.
gi 501488905 240 DGTADELRDNEDVKEF--YLG 258
Cdd:COG3840 211 DGPTAALLDGEPPPALaaYLG 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
22-237 |
1.46e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 113.37 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKIvr 101
Cdd:COG4619 1 LELEGLSFRVGGKPI-LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLD-----PPTSGEIYLDGKPLSAMPPPEW-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 rgifqvmegRRIVS---------DMTSLENLRlgaFTRSDREVGRDIEMVYNYFPRLkertGL--------AGYLSGGEQ 164
Cdd:COG4619 73 ---------RRQVAyvpqepalwGGTVRDNLP---FPFQLRERKFDRERALELLERL----GLppdildkpVERLSGGER 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:COG4619 137 QRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
37-241 |
2.15e-30 |
|
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: 113.08 E-value: 2.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGEriDGTDPDKIVRRgIFQVMEGRRIVSD 116
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT-----FDGK--SYQKNIEALRR-IGALIEAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLENLRLGA--FTRSDREVGRDIEMVynyfpRLKERTGL-AGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLL 193
Cdd:cd03268 87 LTARENLRLLArlLGIRKKRIDEVLDVV-----GLKDSAKKkVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 194 VKEVFAIIQQInRDLGVTILL-------VEQnaraalsVASHGYIMEQGKVVLDG 241
Cdd:cd03268 162 IKELRELILSL-RDQGITVLIsshllseIQK-------VADRIGIINKGKLIEEG 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-215 |
9.87e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 9.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 18 PAPLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPD 97
Cdd:COG1129 1 AEPLLEMRGISKSFGGV-KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQP-----DSGEILLDGEPVRFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRRGIFQVMEGRRIVSDMTSLENLRLGAFTRS-----DREVGRDIEmvynyfpRLKERTGL-------AGYLSGGEQQ 165
Cdd:COG1129 75 DAQAAGIAIIHQELNLVPNLSVAENIFLGREPRRgglidWRAMRRRAR-------ELLARLGLdidpdtpVGDLSVAQQQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501488905 166 MLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLV 215
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYI 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-249 |
1.14e-29 |
|
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: 112.05 E-value: 1.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKivrRG 103
Cdd:cd03296 5 VRNVSKRFGDFV-ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERP-----DSGTILFGGEDATDVPVQE---RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 104 IFQVMEGRRIVSDMTSLENLRLG--AFTRSDREVGRDIEMVYNYFPRLKERTGLA----GYLSGGEQQMLAIGRALMARP 177
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGlrVKPRSERPPEAEIRAKVHELLKLVQLDWLAdrypAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 178 KMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN 249
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
22-238 |
1.80e-29 |
|
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: 110.81 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKivr 101
Cdd:cd03301 1 VELENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE-----EPTSGRIYIGGRDVTDLPPKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLEN----LRLGAFTRSD-----REVGR--DIEMVYNYFPRlkertglagYLSGGEQQMLAIG 170
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNiafgLKLRKVPKDEidervREVAEllQIEHLLDRKPK---------QLSGGQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVV 238
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-262 |
2.03e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.89 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDKIvr 101
Cdd:COG4152 2 LELKGLTKRFGDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVL-----WDGEPLDPEDRRRI-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 rgifqvmeG-----RRIVSDMTSLENLRlgaftrsdrevgrdiemvynYFPRLK---------------ERTGLAGY--- 158
Cdd:COG4152 74 --------GylpeeRGLYPKMKVGEQLV--------------------YLARLKglskaeakrradewlERLGLGDRank 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 ----LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPL---LVKEVfaIIQQINRdlGVTIL-------LVEQnaraals 224
Cdd:COG4152 126 kveeLSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVnveLLKDV--IRELAAK--GTTVIfsshqmeLVEE------- 194
|
250 260 270
....*....|....*....|....*....|....*...
gi 501488905 225 VASHGYIMEQGKVVLDGTADELRDNEDVKEFYLGGAGD 262
Cdd:COG4152 195 LCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGD 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-246 |
3.53e-29 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 116.47 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYD-DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDkIV 100
Cdd:COG2274 474 IELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY-----EPTSGRILIDGIDLRQIDPA-SL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDmTSLENLRLGAFTRSDREV---------GRDIE---MVYNYfpRLKERtglAGYLSGGEQQMLA 168
Cdd:COG2274 548 RRQIGVVLQDVFLFSG-TIRENITLGDPDATDEEIieaarlaglHDFIEalpMGYDT--VVGEG---GSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 169 IGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLVEQNaraaLSVASHG---YIMEQGKVVLDGTADE 245
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR----LSTIRLAdriIVLDKGRIVEDGTHEE 695
|
.
gi 501488905 246 L 246
Cdd:COG2274 696 L 696
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-262 |
7.70e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 110.62 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 15 STAPAPLLSVRNI------EVVYDDVilvlrglSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtRGEIVFDG 88
Cdd:PRK11831 1 EQSVANLVDMRGVsftrgnRCIFDNI-------SLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-----HGEILFDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 ERIDGTDPDKI--VRRGIFQVMEGRRIVSDMTSLENLR--LGAFTRSDREVGRDIEMVynyfpRLkERTGLAGY------ 158
Cdd:PRK11831 69 ENIPAMSRSRLytVRKRMSMLFQSGALFTDMNVFDNVAypLREHTQLPAPLLHSTVMM-----KL-EAVGLRGAaklmps 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 -LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:PRK11831 143 eLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
250 260
....*....|....*....|....*..
gi 501488905 238 VLDGTADELRDNED--VKEFyLGGAGD 262
Cdd:PRK11831 223 VAHGSAQALQANPDprVRQF-LDGIAD 248
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-214 |
9.46e-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: 108.72 E-value: 9.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDki 99
Cdd:COG4133 1 MMLEAENLSCRRGER-LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP-----PSAGEVLWNGEPIRDARED-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQQMLAIGRA 172
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAID-------EALEAVGLAGLadlpvrqLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501488905 173 LMARPKMILMDEPSMGLSPLLVKEVFAIIQQiNRDLGVTILL 214
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLL 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-256 |
1.28e-28 |
|
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: 109.40 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLL-KTEDGEVTrgeiVFdGERIDGTDPDK 98
Cdd:COG1119 2 PLLELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVR----LF-GERRGGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRR-GIFQVMEGRRIVSDMTSLENLRLGAF---------TRSDREVGRdiemvynyfpRLKERTGLA-------GYLSG 161
Cdd:COG1119 76 LRKRiGLVSPALQLRFPRDETVLDVVLSGFFdsiglyrepTDEQRERAR----------ELLELLGLAhladrpfGTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 162 GEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
250
....*....|....*
gi 501488905 242 TADELRDNEDVKEFY 256
Cdd:COG1119 226 PKEEVLTSENLSEAF 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-215 |
2.47e-28 |
|
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: 107.62 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIvfdgeRIDGTDPDKIVRR 102
Cdd:cd03235 1 EVEDLTVSYGGHP-VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-----TSGSI-----RVFGKPLEKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 -G----IFQVMEGRRI-VSDMTSLENL-RLGAFTRSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQQMLA 168
Cdd:cd03235 70 iGyvpqRRSIDRDFPIsVRDVVLMGLYgHKGLFRRLSKADKAKVD-------EALERVGLSELadrqigeLSGGQQQRVL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 501488905 169 IGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLV 215
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVV 188
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-246 |
9.86e-28 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 106.90 E-value: 9.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDV---ILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPD 97
Cdd:cd03258 1 MIELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERP-----TSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIV--RRGIFQVMEGRRIVSDMTSLEN----LRLGAFTRSDREvgrdiEMVYnyfpRLKERTGLAG----Y---LSGGEQ 164
Cdd:cd03258 76 ELRkaRRRIGMIFQHFNLLSSRTVFENvalpLEIAGVPKAEIE-----ERVL----ELLELVGLEDkadaYpaqLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTAD 244
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
..
gi 501488905 245 EL 246
Cdd:cd03258 227 EV 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-246 |
1.06e-27 |
|
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: 111.77 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 6 ELHPPQPGASTAPAPL-----LSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVT 80
Cdd:COG4988 316 DAPEPAAPAGTAPLPAagppsIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL-----PPY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 RGEIVFDGERIDGTDPDKIvRRGIFQVMEGRRIVSDmTSLENLRLGAFTRSDREVGRDIEMVY-----NYFPR-LKERTG 154
Cdd:COG4988 391 SGSILINGVDLSDLDPASW-RRQIAWVPQNPYLFAG-TIRENLRLGRPDASDEELEAALEAAGldefvAALPDgLDTPLG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 155 LAGY-LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLVEQNArAALSVASHGYIME 233
Cdd:COG4988 469 EGGRgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRL-ALLAQADRILVLD 545
|
250
....*....|...
gi 501488905 234 QGKVVLDGTADEL 246
Cdd:COG4988 546 DGRIVEQGTHEEL 558
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-237 |
1.85e-27 |
|
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: 107.83 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktEDGEVTRGEIVFDGERIDGTDPD 97
Cdd:COG0444 1 LLEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLL--PPPGITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVR-RG-----IFQvmegrrivsD-MTSL-----------ENLRL-GAFTRSDREvGRDIEMVynyfprlkERTGLAG- 157
Cdd:COG0444 79 ELRKiRGreiqmIFQ---------DpMTSLnpvmtvgdqiaEPLRIhGGLSKAEAR-ERAIELL--------ERVGLPDp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 158 ------Y---LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNaraaLSVASH 228
Cdd:COG0444 141 errldrYpheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD----LGVVAE 216
|
250
....*....|....*....
gi 501488905 229 ----------GYIMEQGKV 237
Cdd:COG0444 217 iadrvavmyaGRIVEEGPV 235
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-238 |
3.51e-27 |
|
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: 104.65 E-value: 3.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIdgtdPDKIVRR 102
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-----SSGSILLNGKPI----KAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 GIFQVME--GRRIVSDmTSLENLRLGAftrsdREVGRDIEMVYNYFPRL-----KERTGLAgyLSGGEQQMLAIGRALMA 175
Cdd:cd03226 72 SIGYVMQdvDYQLFTD-SVREELLLGL-----KELDAGNEQAETVLKDLdlyalKERHPLS--LSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVV 238
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-246 |
4.11e-27 |
|
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: 107.88 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 33 DVILVLRGLSLDV----PQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT-RGEIVFDGERidgtdpdkivrrGIFQV 107
Cdd:COG4148 6 DFRLRRGGFTLDVdftlPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlGGEVLQDSAR------------GIFLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 108 MEGRRI--V-------SDMTSLENLRLGAfTRSDREVGRDiemvynYFPRLKERTGLA-------GYLSGGEQQMLAIGR 171
Cdd:COG4148 74 PHRRRIgyVfqearlfPHLSVRGNLLYGR-KRAPRAERRI------SFDEVVELLGIGhlldrrpATLSGGERQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 172 ALMARPKMILMDEPsmgLSPLLVK---EVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:COG4148 147 ALLSSPRLLLMDEP---LAALDLArkaEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
41-246 |
6.59e-27 |
|
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: 107.12 E-value: 6.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGE-VTRGEIVFDGERIDGTDPDKivrRGIFQVMEGRRIVSDMTS 119
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEiVLNGRTLFDSRKGIFLPPEK---RRIGYVFQEARLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 120 LENLRLG-AFTR-SDREVGRD--IEMVyNYFPRLKERTGlagYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVK 195
Cdd:TIGR02142 93 RGNLRYGmKRARpSERRISFErvIELL-GIGHLLGRLPG---RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501488905 196 EVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-215 |
7.34e-27 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 102.90 E-value: 7.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIevvydDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDK 98
Cdd:cd03215 2 EPVLEVRGL-----SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRRGIFQVMEGRR---IVSDMTSLENLRLGAFtrsdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMA 175
Cdd:cd03215 72 AIRAGIAYVPEDRKregLVLDLSVAENIALSSL------------------------------LSGGNQQKVVLARWLAR 121
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLV 215
Cdd:cd03215 122 DPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLI 160
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
22-249 |
8.78e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.77 E-value: 8.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGtdpDKIVR 101
Cdd:COG1118 3 IEVRNISKRFGSFTL-LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETP-----DSGRIVLNGRDLFT---NLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 -RGI---FQvmegrrivsD------MTSLENLrlgAF-----TRSDREVGRDIEmvynyfpRLKERTGLAGY-------L 159
Cdd:COG1118 74 eRRVgfvFQ---------HyalfphMTVAENI---AFglrvrPPSKAEIRARVE-------ELLELVQLEGLadrypsqL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 160 SGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVL 239
Cdd:COG1118 135 SGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
250
....*....|
gi 501488905 240 DGTADELRDN 249
Cdd:COG1118 215 VGTPDEVYDR 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-246 |
1.03e-26 |
|
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: 108.70 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 2 TEAAELHPPQPGASTAPaPLLSVRNIEVVYDDVI-LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVT 80
Cdd:COG4987 315 APPAVTEPAEPAPAPGG-PSLELEDVSFRYPGAGrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL-----DPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 RGEIVFDGERIDGTDPDKIvrRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEMVY--NYFPRLKE----RTG 154
Cdd:COG4987 389 SGSITLGGVDLRDLDEDDL--RRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGlgDWLAALPDgldtWLG 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 155 LAGY-LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLgvTILLVeQNARAALSVASHGYIME 233
Cdd:COG4987 467 EGGRrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLI-THRLAGLERMDRILVLE 543
|
250
....*....|...
gi 501488905 234 QGKVVLDGTADEL 246
Cdd:COG4987 544 DGRIVEQGTHEEL 556
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-255 |
3.53e-26 |
|
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: 102.80 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDviLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtRGEIVFDGERIDGTDPDKivr 101
Cdd:cd03299 1 LKVENLSKDWKE--FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-----SGKILLNGKDITNLPPEK--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLRLGAFTRS------DREVgRDIEMVYNYFPRL--KERTglagyLSGGEQQMLAIGRAL 173
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLKKRKvdkkeiERKV-LEIAEMLGIDHLLnrKPET-----LSGGEQQRVAIARAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 174 MARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL---RDNE 250
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVfkkPKNE 224
|
....*
gi 501488905 251 DVKEF 255
Cdd:cd03299 225 FVAEF 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-215 |
4.99e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.60 E-value: 4.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 8 HPPQPGASTAPAPLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFD 87
Cdd:TIGR02857 308 LAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV-----DPTEGSIAVN 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 88 GERIDGTDPDKIvRRGIFQVMEGRRIVSDmTSLENLRLGAFTRSDREVGRDIEMVY-----NYFPR-LKERTGLAGY-LS 160
Cdd:TIGR02857 383 GVPLADADADSW-RDQIAWVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAGldefvAALPQgLDTPIGEGGAgLS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLV 215
Cdd:TIGR02857 461 GGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLV 513
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
17-244 |
2.04e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 104.72 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 17 APAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDP 96
Cdd:COG3845 1 MMPPALELRGITKRFGGVV-ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ-----PDSGEILIDGKPVRIRSP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKIVRRGI---FQ-VMegrrIVSDMTSLENLRLGA-----FTRSDREVGRDIEmvynyfpRLKERTGLA-------GYLS 160
Cdd:COG3845 75 RDAIALGIgmvHQhFM----LVPNLTVAENIVLGLeptkgGRLDRKAARARIR-------ELSERYGLDvdpdakvEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVld 240
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVV-- 220
|
....
gi 501488905 241 GTAD 244
Cdd:COG3845 221 GTVD 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-241 |
2.64e-25 |
|
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: 99.66 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKI-- 99
Cdd:cd03269 1 LEVENVTKRFGRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILP-----DSGEVLFDGKPLDIAARNRIgy 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 --VRRGIFQVMEGRRIVSDMTSLENLrlgaftrSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQQMLAIG 170
Cdd:cd03269 75 lpEERGLYPKMKVIDQLVYLAQLKGL-------KKEEARRRID-------EWLERLELSEYankrveeLSKGNQQKVQFI 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
22-246 |
2.83e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.46 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktEdgEVTRGEIVFDGERIDGTDPDK 98
Cdd:COG1135 2 IELENLSKTFptkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL---E--RPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 I--VRRGI---FQ---VMEGRrivsdmTSLEN----LRLGAFTRSDRE--VGRDIEMVynyfprlkertGLAG----Y-- 158
Cdd:COG1135 77 LraARRKIgmiFQhfnLLSSR------TVAENvalpLEIAGVPKAEIRkrVAELLELV-----------GLSDkadaYps 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 -LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:COG1135 140 qLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
....*....
gi 501488905 238 VLDGTADEL 246
Cdd:COG1135 220 VEQGPVLDV 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-241 |
5.58e-25 |
|
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: 98.98 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDV---ILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDPD 97
Cdd:cd03266 1 MITADALTKRFRDVkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT----------VDGFDVV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 K---IVRRGIFQVMEGRRIVSDMTSLENLRL---------GAFTRSDREVGRDIEMVynyfPRLKERTglaGYLSGGEQQ 165
Cdd:cd03266 71 KepaEARRRLGFVSDSTGLYDRLTARENLEYfaglyglkgDELTARLEELADRLGME----ELLDRRV---GGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 166 MLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-215 |
8.22e-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: 103.21 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 10 PQPGASTAPAPLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGE 89
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT-----LDGV 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 90 RIDGTDPDKIVRRgiFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEMV--YNYFPRLKER-----TGLAGYLSGG 162
Cdd:TIGR02868 398 PVSSLDQDEVRRR--VSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVglADWLRALPDGldtvlGEGGARLSGG 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501488905 163 EQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLV 215
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLI 526
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
37-246 |
8.57e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.44 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKI--VRRGIFQVMEGRRIV 114
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIrqLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDMTSLENLRLGAFTRSDREVGRDIEMVYnyfpRLKERTGLAG-------YLSGGEQQMLAIGRALMARPKMILMDEPSM 187
Cdd:PRK11264 98 PHRTVLENIIEGPVIVKGEPKEEATARAR----ELLAKVGLAGketsyprRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 188 GLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-236 |
2.03e-24 |
|
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: 96.30 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDD-VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKIv 100
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY-----DPTSGEILIDGVDLRDLDLESL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 rrgifqvmegRRIVS---------DMTSLENLrlgaftrsdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGR 171
Cdd:cd03228 75 ----------RKNIAyvpqdpflfSGTIRENI-----------------------------------LSGGQRQRIAIAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLVEQNaRAALSVASHGYIMEQGK 236
Cdd:cd03228 110 ALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHR-LSTIRDADRIIVLDDGR 171
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-245 |
2.41e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.62 E-value: 2.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYD----DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPD 97
Cdd:COG1101 2 LELKNLSKTFNpgtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP-----PDSGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 K----IVRrgIFQ-VMEGrrIVSDMTSLENLRLG-----------AFTRSDRE--------VGRDIEmvyNyfpRLKERT 153
Cdd:COG1101 77 KrakyIGR--VFQdPMMG--TAPSMTIEENLALAyrrgkrrglrrGLTKKRRElfrellatLGLGLE---N---RLDTKV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 154 GLagyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIME 233
Cdd:COG1101 147 GL---LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMH 223
|
250
....*....|..
gi 501488905 234 QGKVVLDGTADE 245
Cdd:COG1101 224 EGRIILDVSGEE 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-250 |
3.34e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.28 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 16 TAPAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLkTEDGevtrGEIVFDGERIDGTD 95
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVE-VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIV-PPDS----GTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 96 PDKIVRRGIFQVMEGRRIVSDMTSLENLRLGaFTRSDREVGRDIEMVYNYFPRLKERTgLAGYLSGGEQQMLAIGRALMA 175
Cdd:PRK15439 80 PAKAHQLGIYLVPQEPLLFPNLSVKENILFG-LPKRQASMQKMKQLLAALGCQLDLDS-SAGSLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNE 250
Cdd:PRK15439 158 DSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-259 |
3.66e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.68 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:PRK14247 4 IEIRDLKVSFGQV-EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 R--GIFQVMEGrriVSDMTSLENLRLGA----FTRSDREVGRDIEMVY---NYFPRLKERTGL-AGYLSGGEQQMLAIGR 171
Cdd:PRK14247 83 RvqMVFQIPNP---IPNLSIFENVALGLklnrLVKSKKELQERVRWALekaQLWDEVKDRLDApAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLgvTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN-- 249
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNpr 237
|
250
....*....|
gi 501488905 250 EDVKEFYLGG 259
Cdd:PRK14247 238 HELTEKYVTG 247
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
10-249 |
3.82e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.91 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 10 PQPGASTAPAPLLSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGE 89
Cdd:PRK11607 8 PQAKTRKALTPLLEIRNLTKSFDG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQP-----TAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 90 RIDGTDPdkiVRRGIFQVMEGRRIVSDMTSLENLRLGafTRSDR--------EVGRDIEMVY-NYFPRLKERTglagyLS 160
Cdd:PRK11607 82 DLSHVPP---YQRPINMMFQSYALFPHMTVEQNIAFG--LKQDKlpkaeiasRVNEMLGLVHmQEFAKRKPHQ-----LS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPsMG-----LSPLLVKEVFAIIQQInrdlGVTILLVEQNARAALSVASHGYIMEQG 235
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEP-MGaldkkLRDRMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
250
....*....|....
gi 501488905 236 KVVLDGTADELRDN 249
Cdd:PRK11607 227 KFVQIGEPEEIYEH 240
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
25-236 |
3.94e-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: 96.55 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKI--VRR 102
Cdd:TIGR02673 5 HNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTP-----SRGQVRIAGEDVNRLRGRQLplLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 GIFQVMEGRRIVSDMTSLENLRL-----GAFTRS-DREVGRDIEMVynyfpRLKERT-GLAGYLSGGEQQMLAIGRALMA 175
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALplevrGKKEREiQRRVGAALRQV-----GLEHKAdAFPEQLSGGEQQRVAIARAIVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQINRdLGVTILLVEQNARAALSVASHGYIMEQGK 236
Cdd:TIGR02673 155 SPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-248 |
4.03e-24 |
|
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: 96.44 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktEDGEVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:cd03217 1 LEIKDLHVSVGGK-EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH---PKYEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGI---FQV---MEGrriVSDMTSLENLRLGaftrsdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMA 175
Cdd:cd03217 77 LGIflaFQYppeIPG---VKNADFLRYVNEG--------------------------------FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNAR-AALSVASHGYIMEQGKVVLDGTADELRD 248
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRlLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-246 |
4.76e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.00 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 18 PAPLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTdpd 97
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-----SSGRILFDGKPIDYS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 kivRRGIFQVMEGRRIV--------SDMTSLENLRLGAFTRS--DREVGRDIEmvynyfpRLKERTGLA-------GYLS 160
Cdd:PRK13636 74 ---RKGLMKLRESVGMVfqdpdnqlFSASVYQDVSFGAVNLKlpEDEVRKRVD-------NALKRTGIEhlkdkptHCLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLD 240
Cdd:PRK13636 144 FGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
....*.
gi 501488905 241 GTADEL 246
Cdd:PRK13636 224 GNPKEV 229
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-260 |
6.98e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.22 E-value: 6.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKI-V 100
Cdd:PRK14267 5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIeV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDMTSLEN----LRLGAFTRSDREVGRDIEMVYN---YFPRLKER-TGLAGYLSGGEQQMLAIGRA 172
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNvaigVKLNGLVKSKKELDERVEWALKkaaLWDEVKDRlNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 173 LMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLgvTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN--E 250
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENpeH 241
|
250
....*....|
gi 501488905 251 DVKEFYLGGA 260
Cdd:PRK14267 242 ELTEKYVTGA 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
37-244 |
7.50e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.62 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERidGTDPDKI--VRRGIFQVMEGRRIV 114
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSK--TPSDKAIreLRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDMTSLENLrLGAFTRSdreVGRDIEMVYNYFPRLKERTGLAGY-------LSGGEQQMLAIGRALMARPKMILMDEPSM 187
Cdd:PRK11124 95 PHLTVQQNL-IEAPCRV---LGLSKDQALARAEKLLERLRLKPYadrfplhLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 188 GLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTAD 244
Cdd:PRK11124 171 ALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
41-241 |
1.52e-23 |
|
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: 95.05 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGaIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIV---RRGIFQVMEGRRIVSDM 117
Cdd:cd03297 17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEK-----PDGGTIVLNGTVLFDSRKKINLppqQRKIGLVFQQYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLGAFTRSDREVGRDIEMVYNYF--PRLKERTglAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVK 195
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLDLLglDHLLNRY--PAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501488905 196 EVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
38-256 |
1.72e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.24 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKIVRRG-----IFQVMEgrr 112
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARDIRKSRantgyIFQQFN--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSDMTSLENLRLGA-----FTRSdrevgrdiemVYNYFPRLKE--------RTGLAGY-------LSGGEQQMLAIGRA 172
Cdd:PRK09984 97 LVNRLSVLENVLIGAlgstpFWRT----------CFSWFTREQKqralqaltRVGMVHFahqrvstLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 173 LMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELrDNEDV 252
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF-DNERF 245
|
....
gi 501488905 253 KEFY 256
Cdd:PRK09984 246 DHLY 249
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
24-241 |
2.05e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 94.96 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDV-ILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeivfdgeRIDGTDPDKI--- 99
Cdd:cd03245 5 FRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV----------LLDGTDIRQLdpa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 -VRRGIFQVMEGRRIVSDmTSLENLRLGAFTRSDREVGRDIEM--VYNYFPR----LKERTGLAGY-LSGGEQQMLAIGR 171
Cdd:cd03245 75 dLRRNIGYVPQDVTLFYG-TLRDNITLGAPLADDERILRAAELagVTDFVNKhpngLDLQIGERGRgLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVfaiIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERL---KERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
37-249 |
2.31e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.81 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV------------TRGEI-VFDGERIdgtdpdKIVRRG 103
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdKDGQLkVADKNQL------RLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 104 IFQVMEGRRIVSDMTSLENLR------LGAFTRSDREvgRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARP 177
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLENVMeapiqvLGLSKQEARE--RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 178 KMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN 249
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
2.48e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 3 EAAELHPPQPGASTAPapLLSVRNIEVVYddvilVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRG 82
Cdd:COG1129 240 ELEDLFPKRAAAPGEV--VLEVEGLSVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-----ADSG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 83 EIVFDGERIDGTDPDKIVRRGIFQVMEGRR---IVSDMTSLENL---RLGAFTRS---DRevGRDIEMVYNYFPRLKERT 153
Cdd:COG1129 308 EIRLDGKPVRIRSPRDAIRAGIAYVPEDRKgegLVLDLSIRENItlaSLDRLSRGgllDR--RRERALAEEYIKRLRIKT 385
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 154 G----LAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGlspllV-----KEVFAIIQQINRDlGVTILLV 215
Cdd:COG1129 386 PspeqPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG-----IdvgakAEIYRLIRELAAE-GKAVIVI 450
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
37-244 |
2.85e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISgLLKTED-GEVTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRRIVS 115
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLETPDsGQLNIAGHQFDFSQKPSEKAIRLLRQKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 116 DMTSLENLrLGAFTR---SDREVGRDIEMvynyfpRLKERTGLAGY-------LSGGEQQMLAIGRALMARPKMILMDEP 185
Cdd:COG4161 96 HLTVMENL-IEAPCKvlgLSKEQAREKAM------KLLARLRLTDKadrfplhLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 186 SMGLSPLLVKEVFAIIQQINrDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTAD 244
Cdd:COG4161 169 TAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
37-246 |
5.71e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.33 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGEriDGTDpDKIVRRGIFQVMEGRRIVSD 116
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP-----TEGQIFIDGE--DVTH-RSIQQRDICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLEN----LRLGAFTRSDRE--VGRDIEMVynyfprlkertGLAGY-------LSGGEQQMLAIGRALMARPKMILMD 183
Cdd:PRK11432 93 MSLGENvgygLKMLGVPKEERKqrVKEALELV-----------DLAGFedryvdqISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 184 EPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-220 |
1.31e-22 |
|
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: 92.86 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKI--VRR 102
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP-----TSGTIRVNGQDVSDLRGRAIpyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 GIFQVMEGRRIVSDMTSLEN--LRLGAFTRSDREVGRDIEMVYNYFP-RLKERTgLAGYLSGGEQQMLAIGRALMARPKM 179
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENvaFALEVTGVPPREIRKRVPAALELVGlSHKHRA-LPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501488905 180 ILMDEPSMGLSPLLVKEVFAIIQQINrDLGVTILLVEQNAR 220
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKE 197
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
20-245 |
1.55e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktedGEVTRGEIVFDGERIDGTDPDKi 99
Cdd:PRK09452 13 PLVELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-----ETPDSGRIMLDGQDITHVPAEN- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 vrRGIFQVMEGRRIVSDMTSLEN----LRLGAFTRSD--REVGRDIEMVynyfpRLKErtgLAGY----LSGGEQQMLAI 169
Cdd:PRK09452 86 --RHVNTVFQSYALFPHMTVFENvafgLRMQKTPAAEitPRVMEALRMV-----QLEE---FAQRkphqLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 170 GRALMARPKMILMDEPsmgLSPL---LVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADE 245
Cdd:PRK09452 156 ARAVVNKPKVLLLDES---LSALdykLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
15-215 |
1.66e-22 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 92.88 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 15 STAPAPLLSVRNIEVVYDD---VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERI 91
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTgagELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLD-----RPTSGTVRLAGQDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 92 DGTDPDKI--VRRG----IFQVMegrRIVSDMTSLENLRLGAFTRSDREV-GRDIEMVynyfprlkERTGLA-------G 157
Cdd:COG4181 77 FALDEDARarLRARhvgfVFQSF---QLLPTLTALENVMLPLELAGRRDArARARALL--------ERVGLGhrldhypA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 158 YLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPllvKEVFAIIQ---QINRDLGVTILLV 215
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDA---ATGEQIIDllfELNRERGTTLVLV 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-185 |
2.67e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.00 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYD---DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDP 96
Cdd:COG4525 2 SMLTVRHVSVRYPgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFL-----APSSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKIVrrgIFQvmegrrivSD-----MTSLEN----LRLGAFTRSDREVGRDiemvynyfpRLKERTGLAGY-------LS 160
Cdd:COG4525 77 DRGV---VFQ--------KDallpwLNVLDNvafgLRLRGVPKAERRARAE---------ELLALVGLADFarrriwqLS 136
|
170 180
....*....|....*....|....*
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEP 185
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEP 161
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-245 |
4.55e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDKI 99
Cdd:PRK13548 1 AMLEARNLSVRLGGR-TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR-----LNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRgifqvmegRRIVSDMTSL-------ENLRLGA--FTRSDREVGRDIEMVYnyfprlkERTGLAGY-------LSGGE 163
Cdd:PRK13548 75 ARR--------RAVLPQHSSLsfpftveEVVAMGRapHGLSRAEDDALVAAAL-------AQVDLAHLagrdypqLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 164 QQMLAIGRALM------ARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLV----EQNARAALSVAshgyIME 233
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVlhdlNLAARYADRIV----LLH 215
|
250
....*....|..
gi 501488905 234 QGKVVLDGTADE 245
Cdd:PRK13548 216 QGRLVADGTPAE 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-249 |
6.82e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.28 E-value: 6.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktEDGEVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:COG0396 1 LEIKNLHVSVEGKE-ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH---PKYEVTSGSILLDGEDILELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGI---FQ---------VMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRlkertGLAGYLSGGEQQMLAI 169
Cdd:COG0396 77 AGIflaFQypveipgvsVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDR-----YVNEGFSGGEKKRNEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 170 GRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARA-ALSVASHGYIMEQGKVVLDGT---ADE 245
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHYQRIlDYIKPDFVHVLVDGRIVKSGGkelALE 230
|
....
gi 501488905 246 LRDN 249
Cdd:COG0396 231 LEEE 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-252 |
7.78e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 7.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKI- 99
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKP-----TSGEVLIKGEPIKYDKKSLLe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRR--GI-FQVMEGRRIVSdmTSLENLRLGAFTrsdreVGRDIEMVYNyfpRLKE---RTGLAGY-------LSGGEQQM 166
Cdd:PRK13639 76 VRKtvGIvFQNPDDQLFAP--TVEEDVAFGPLN-----LGLSKEEVEK---RVKEalkAVGMEGFenkpphhLSGGQKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 167 LAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK13639 146 VAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
....*.
gi 501488905 247 RDNEDV 252
Cdd:PRK13639 225 FSDIET 230
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-245 |
1.00e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.33 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPdkiv 100
Cdd:COG4559 1 MLEAENLSVRLGGRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTP-----SSGEVRLNGRPLAAWSP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 rrgifQVMEGRRIV----SDM----TSLENLRLG--AFTRSDREVGRDIEMVYnyfprlkERTGLAGY-------LSGGE 163
Cdd:COG4559 71 -----WELARRRAVlpqhSSLafpfTVEEVVALGraPHGSSAAQDRQIVREAL-------ALVGLAHLagrsyqtLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 164 QQMLAIGRAL-------MARPKMILMDEPSMGLSPLLVKEVFAIIQQI-NRDLGVTILLVEQNArAALsVASHGYIMEQG 235
Cdd:COG4559 139 QQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNL-AAQ-YADRILLLHQG 216
|
250
....*....|
gi 501488905 236 KVVLDGTADE 245
Cdd:COG4559 217 RLVAQGTPEE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-249 |
2.14e-21 |
|
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: 93.21 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 4 AAELHPPQPGASTAPAPLLSVRNIEVVYD----------DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLK 73
Cdd:COG4172 258 AAEPRGDPRPVPPDAPPLLEARDLKVWFPikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 74 TEdgevtrGEIVFDGERIDGTDPDKI--VRRGI---FQ---------------VMEGRRIVsdmtsleNLRLGAFTRSDR 133
Cdd:COG4172 338 SE------GEIRFDGQDLDGLSRRALrpLRRRMqvvFQdpfgslsprmtvgqiIAEGLRVH-------GPGLSAAERRAR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 134 ------EVGRDIEMVYNY---FprlkertglagylSGGEQQMLAIGRALMARPKMILMDEPSmglSPLLV---KEVFAII 201
Cdd:COG4172 405 vaealeEVGLDPAARHRYpheF-------------SGGQRQRIAIARALILEPKLLVLDEPT---SALDVsvqAQILDLL 468
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501488905 202 QQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN 249
Cdd:COG4172 469 RDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
34-241 |
2.15e-21 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 90.08 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 34 VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVfdgeriDGTDPDKIVRRgiFQVMEGRR- 112
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV------PWKRRKKFLRR--IGVVFGQKt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 -IVSDMTSLENLRLGA--FTRSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQQMLAIGRALMARPKMILM 182
Cdd:cd03267 105 qLWWDLPVIDSFYLLAaiYDLPPARFKKRLD-------ELSELLDLEELldtpvrqLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 183 DEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-246 |
2.74e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.46 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVI-LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERI-Dgtdpd 97
Cdd:PRK13635 4 EIIRVEHISFRYPDAAtYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwD----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 kiVRRGIFQVME-------GRRIVSDMtslenlrlgAFTRSDREVGRDiEMVynyfPRLKE---RTGLAGY-------LS 160
Cdd:PRK13635 79 --VRRQVGMVFQnpdnqfvGATVQDDV---------AFGLENIGVPRE-EMV----ERVDQalrQVGMEDFlnrephrLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSvASHGYIMEQGKVVLD 240
Cdd:PRK13635 143 GGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEE 221
|
....*.
gi 501488905 241 GTADEL 246
Cdd:PRK13635 222 GTPEEI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
38-255 |
3.47e-21 |
|
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: 90.01 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGE---RIDGTDPDKIVRRGIFQVMEGRRIV 114
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLI-----EPTSGKVLIDGQdiaAMSRKELRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDMTSLEN----LRLGAFTRSDREvGRDIEMVynyfprlkERTGLAGY-------LSGGEQQMLAIGRALMARPKMILMD 183
Cdd:cd03294 115 PHRTVLENvafgLEVQGVPRAERE-ERAAEAL--------ELVGLEGWehkypdeLSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 184 EPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN---EDVKEF 255
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNpanDYVREF 260
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-222 |
6.87e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.92 E-value: 6.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILVlRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktEDGEVTRGEIVFDGERIDGTDPDKivR 101
Cdd:COG4136 2 LSLENLTITLGGRPLL-APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTL--SPAFSASGEVLLNGRRLTALPAEQ--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 R-GI-FQvmegrrivsD------MTSLENLRLG---AFTRSDREVgRDIEMVynyfprlkERTGLAGY-------LSGGE 163
Cdd:COG4136 77 RiGIlFQ---------DdllfphLSVGENLAFAlppTIGRAQRRA-RVEQAL--------EEAGLAGFadrdpatLSGGQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 164 QQMLAIGRALMARPKMILMDEPSMGLSPLL---VKE-VFAIIqqinRDLGVTILLV---EQNARAA 222
Cdd:COG4136 139 RARVALLRALLAEPRALLLDEPFSKLDAALraqFREfVFEQI----RQRGIPALLVthdEEDAPAA 200
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-246 |
1.77e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 90.61 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 2 TEAAELHPPQPGASTAPAPLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTR 81
Cdd:COG1132 320 EPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY-----DPTS 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 82 GEIvfdgeRIDGTDPDKI----VRRGIfqvmegrRIVS------DMTSLENLRLGAFTRSDREVGRDIEMVY-----NYF 146
Cdd:COG1132 395 GRI-----LIDGVDIRDLtlesLRRQI-------GVVPqdtflfSGTIRENIRYGRPDATDEEVEEAAKAAQahefiEAL 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 147 P-----RLKERtglAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPllvkEVFAIIQQ-INRDL-GVTILLVEQna 219
Cdd:COG1132 463 PdgydtVVGER---GVNLSGGQRQRIAIARALLKDPPILILDEATSALDT----ETEALIQEaLERLMkGRTTIVIAH-- 533
|
250 260
....*....|....*....|....*...
gi 501488905 220 R-AALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:COG1132 534 RlSTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
37-246 |
2.05e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.37 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGE---RIDGTDpdkivRRGIFqVMEGRRI 113
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ-----TSGHIRFHGTdvsRLHARD-----RKVGF-VFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 114 VSDMTSLENLRLG--AFTRSDR--------EVGRDIEMVYnyFPRLKERtgLAGYLSGGEQQMLAIGRALMARPKMILMD 183
Cdd:PRK10851 86 FRHMTVFDNIAFGltVLPRRERpnaaaikaKVTQLLEMVQ--LAHLADR--YPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 184 EPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-215 |
3.86e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 9 PPQPGAstapaPLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDG 88
Cdd:COG3845 250 PAEPGE-----VVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-----PASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 ERIDGTDPDKIVRRGIFQVMEGRR---IVSDMTSLENLRLGAFTRsdREVGR----DIEMVYNYFPRLKE----RTG--- 154
Cdd:COG3845 320 EDITGLSPRERRRLGVAYIPEDRLgrgLVPDMSVAENLILGRYRR--PPFSRggflDRKAIRAFAEELIEefdvRTPgpd 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501488905 155 -LAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSpllVKEVFAIIQQIN--RDLGVTILLV 215
Cdd:COG3845 398 tPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGAIEFIHQRLLelRDAGAAVLLI 458
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
36-241 |
5.81e-20 |
|
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: 85.79 E-value: 5.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 36 LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktEDGEVTRGEIVFDGERIdgtDPDKiVRRGIFQVMEGRRIVS 115
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNGQPR---KPDQ-FQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 116 DMTSLE------NLRLGAFTRSDREVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGL 189
Cdd:cd03234 95 GLTVREtltytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501488905 190 SPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
22-191 |
6.25e-20 |
|
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: 85.32 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGaIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIdGTDPDKIvR 101
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP-----SSGTIRIDGQDV-LKQPQKL-R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLRLGAF------TRSDREVGRDIEMVyNYFPRLKERtglAGYLSGGEQQMLAIGRALMA 175
Cdd:cd03264 72 RRIGYLPQEFGVYPNFTVREFLDYIAWlkgipsKEVKARVDEVLELV-NLGDRAKKK---IGSLSGGMRRRVGIAQALVG 147
|
170
....*....|....*.
gi 501488905 176 RPKMILMDEPSMGLSP 191
Cdd:cd03264 148 DPSILIVDEPTAGLDP 163
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
38-254 |
7.35e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.64 E-value: 7.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKIVrrGI-FQVMEGR----R 112
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKV--GLvFQYPEYQlfeeT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSDMT-SLENLRLGAFTRSDReVGRDIEMVYNYFPRLKERTGLAgyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSP 191
Cdd:PRK13637 101 IEKDIAfGPINLGLSEEEIENR-VKRAMNIVGLDYEDYKDKSPFE--LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 192 LLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKE 254
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
24-240 |
1.06e-19 |
|
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: 84.59 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAIsGLLKTEDgevtRGEIVFDGE---RIDGTDPDKIV 100
Cdd:TIGR03608 1 LKNISKKFGD-KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNII-GLLEKFD----SGQVYLNGQetpPLNSKKASKFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDMTSLENLRLGaFTRSDREVGRDIEMVYNYFprlkERTGLAGY-------LSGGEQQMLAIGRAL 173
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLG-LKYKKLSKKEKREKKKEAL----EKVGLNLKlkqkiyeLSGGEQQRVALARAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 174 MARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNAraalsvashgYIMEQGKVVLD 240
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP----------EVAKQADRVIE 205
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-246 |
1.21e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 88.20 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 17 APAPLLSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLkTEDGEVTRGEIVFDGERIDG 93
Cdd:COG4172 2 MSMPLLSVEDLSVAFgqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 94 TDPDKIVR-RG-----IFQvmEgrrivsDMTSL-----------ENLRL-GAFTRSDREvGRDIEmvynyfprLKERTG- 154
Cdd:COG4172 81 LSERELRRiRGnriamIFQ--E------PMTSLnplhtigkqiaEVLRLhRGLSGAAAR-ARALE--------LLERVGi 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 155 ------LAGY---LSGGEQQ--MLAIgrALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNaraaL 223
Cdd:COG4172 144 pdperrLDAYphqLSGGQRQrvMIAM--ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----L 217
|
250 260
....*....|....*....|....*..
gi 501488905 224 SV----ASHGYIMEQGKVVLDGTADEL 246
Cdd:COG4172 218 GVvrrfADRVAVMRQGEIVEQGPTAEL 244
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-249 |
1.28e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 34 VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeivfdgeRIDGTDP----DKIVRRgIFQVMe 109
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV----------RVLGYVPfkrrKEFARR-IGVVF- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 110 GRRivS----DMTSLENLRL-GAFTR-SDREVGRDIEMvynyfprLKERTGLAGY-------LSGGeQQMLA-IGRALMA 175
Cdd:COG4586 102 GQR--SqlwwDLPAIDSFRLlKAIYRiPDAEYKKRLDE-------LVELLDLGELldtpvrqLSLG-QRMRCeLAAALLH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 176 RPKMILMDEPSMGLSpLLVKE-VFAIIQQINRDLGVTILL-------VEQNARAALsvashgyIMEQGKVVLDGTADELR 247
Cdd:COG4586 172 RPKILFLDEPTIGLD-VVSKEaIREFLKEYNRERGTTILLtshdmddIEALCDRVI-------VIDHGRIIYDGSLEELK 243
|
..
gi 501488905 248 DN 249
Cdd:COG4586 244 ER 245
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
22-241 |
1.33e-19 |
|
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: 83.52 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDD-VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDPDKI- 99
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT----------LDGVPVSDLe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 -VRRGIFQVMEGRRIVSDMTSLENLrlgaftrsdrevGRDiemvynyfprlkertglagyLSGGEQQMLAIGRALMARPK 178
Cdd:cd03247 71 kALSSLISVLNQRPYLFDTTLRNNL------------GRR--------------------FSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 179 MILMDEPSMGLSPLLVKEVFAIIQQINRDlgVTILLVEQNARaALSVASHGYIMEQGKVVLDG 241
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-245 |
1.56e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.45 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDKIVR 101
Cdd:PRK11231 3 LRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVF-----LGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIF--QVM---EG---RRIVSDMTSLENLRLGAFTRSDREVgRDIEMVYNYFPRLKERtgLAGYLSGGEQQMLAIGRAL 173
Cdd:PRK11231 77 RLALlpQHHltpEGitvRELVAYGRSPWLSLWGRLSAEDNAR-VNQAMEQTRINHLADR--RLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 174 MARPKMILMDEPSMGLSPLLVKEVFAIIQQINrDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADE 245
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-252 |
1.66e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPdKIV 100
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP-----TSGSVLIRGEPITKENI-REV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEG--RRIVSDmTSLENLRLGAFTrsdreVGRDIEMVYNYFPRLKERTGLAGY-------LSGGEQQMLAIGR 171
Cdd:PRK13652 77 RKFVGLVFQNpdDQIFSP-TVEQDIAFGPIN-----LGLDEETVAHRVSSALHMLGLEELrdrvphhLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNED 251
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
.
gi 501488905 252 V 252
Cdd:PRK13652 231 L 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
35-237 |
1.74e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.39 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 35 ILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKIV--RRGIFQVMEGRR 112
Cdd:PRK11153 18 IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERP-----TSGRVLVDGQDLTALSEKELRkaRRQIGMIFQHFN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSDMTSLEN----LRLGAftRSDREVGRDIEmvynyfpRLKERTGLAG----Y---LSGGEQQMLAIGRALMARPKMIL 181
Cdd:PRK11153 93 LLSSRTVFDNvalpLELAG--TPKAEIKARVT-------ELLELVGLSDkadrYpaqLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501488905 182 MDEPSMGLSPLLVKEVFAIIQQINRDLGVTILL-------VEQNA-RAAlsVASHGYIMEQGKV 237
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLithemdvVKRICdRVA--VIDAGRLVEQGTV 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-246 |
3.20e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.32 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 13 GASTAPAPLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERI- 91
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDK-QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 92 -DGTDPDKIVRR-G-IFQ--------VME---------GRRIVSDM-----TSLENLRLGaftrsDrEVgRDiemvynyf 146
Cdd:COG1117 82 dPDVDVVELRRRvGmVFQkpnpfpksIYDnvayglrlhGIKSKSELdeiveESLRKAALW-----D-EV-KD-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 147 pRLKERtGLAgyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlgVTILLV----EQNARAA 222
Cdd:COG1117 147 -RLKKS-ALG--LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVthnmQQAARVS 220
|
250 260
....*....|....*....|....
gi 501488905 223 LSVAshgyIMEQGKVVLDGTADEL 246
Cdd:COG1117 221 DYTA----FFYLGELVEFGPTEQI 240
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
17-256 |
3.21e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 85.24 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 17 APAPLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtRGEIVFDGERIDGTDP 96
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD-----AGSISLCGEPVPSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKIVRRGIfqVMEGRRIVSDMTSLENLRLGA--FTRSDREVGRDIEMVYNyFPRLKERT-GLAGYLSGGEQQMLAIGRAL 173
Cdd:PRK13537 77 HARQRVGV--VPQFDNLDPDFTVRENLLVFGryFGLSAAAARALVPPLLE-FAKLENKAdAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 174 MARPKMILMDEPSMGLSPllvkEVFAIIQQINRDL---GVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNE 250
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDP----QARHLMWERLRSLlarGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
....*....
gi 501488905 251 ---DVKEFY 256
Cdd:PRK13537 230 igcDVIEIY 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-248 |
3.61e-19 |
|
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: 83.81 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGerIDGTD-PDKIVRRG 103
Cdd:cd03254 6 ENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFY-----DPQKGQILIDG--IDIRDiSRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 104 IFQVMEGRRIVSDmTSLENLRLGAFTRSDREVGRDIEMV-YNYFPR---------LKERtglAGYLSGGEQQMLAIGRAL 173
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAgAHDFIMklpngydtvLGEN---GGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 174 MARPKMILMDEPSMGLSPllvkEVFAIIQQINRDLgvtillveQNARAALSVASHGYI---------MEQGKVVLDGTAD 244
Cdd:cd03254 155 LRDPKILILDEATSNIDT----ETEKLIQEALEKL--------MKGRTSIIIAHRLSTiknadkilvLDDGKIIEEGTHD 222
|
....
gi 501488905 245 ELRD 248
Cdd:cd03254 223 ELLA 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-215 |
3.76e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGllkteDGEVTRGEIVFDGERIDGTDPDK 98
Cdd:PRK11288 2 SPYLSFDGIGKTFPGV-KALDDISFDCRAGQVHALMGENGAGKSTLLKILSG-----NYQPDAGSILIDGQEMRFASTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDiEMVYNYFPRLkERTGLA-------GYLSGGEQQMLAIGR 171
Cdd:PRK11288 76 ALAAGVAIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRR-LLNYEAREQL-EHLGVDidpdtplKYLSIGQRQMVEIAK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLV 215
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYV 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-246 |
5.38e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.42 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 10 PQPGASTAPAPLLSVRNIEVVYDDVIL-VLRGLSLDVPQGAIVALLGANGAGKSTTLkaisGLLkTEDGEVTRGEIVFDG 88
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLL-TRAWDPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 ERIDGTDpDKIVRRGIFQVMEGRRIVSDmTSLENLRLGAFTRSD---REVGRDIEMVYnyfpRLKERTGLAGY------- 158
Cdd:PRK11160 402 QPIADYS-EAALRQAISVVSQRVHLFSA-TLRDNLLLAAPNASDealIEVLQQVGLEK----LLEDDKGLNAWlgeggrq 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlgVTILLVEQNARaALSVASHGYIMEQGKVV 238
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLT-GLEQFDRICVMDNGQII 552
|
....*...
gi 501488905 239 LDGTADEL 246
Cdd:PRK11160 553 EQGTHQEL 560
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-254 |
5.99e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYD-DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDK 98
Cdd:PRK13632 6 VMIKVENVSFSYPnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP-----QSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRR-GI-FQVMEGRRI---VSD--MTSLENLRLgaftrsDREVGRDIemVYNYfprlKERTGLAGY-------LSGGEQ 164
Cdd:PRK13632 81 IRKKiGIiFQNPDNQFIgatVEDdiAFGLENKKV------PPKKMKDI--IDDL----AKKVGMEDYldkepqnLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALsVASHGYIMEQGKVVLDGTAD 244
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
250
....*....|
gi 501488905 245 ELRDNEDVKE 254
Cdd:PRK13632 228 EILNNKEILE 237
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-226 |
6.51e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 6.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKI- 99
Cdd:PRK14243 10 VLRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDPVe 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGI---FQ------------VMEGRRIVS---DMTSL--ENLRLGAFTRsdrEVgRDiemvynyfpRLKErTGLAgyL 159
Cdd:PRK14243 89 VRRRIgmvFQkpnpfpksiydnIAYGARINGykgDMDELveRSLRQAALWD---EV-KD---------KLKQ-SGLS--L 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 160 SGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLgvTILLVEQNARAALSVA 226
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVS 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
37-246 |
7.58e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 7.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtRGEIVFDGERIDGTDPDKIVRR----GIFQVMEGRR 112
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ-----KGAVLWQGKPLDYSKRGLLALRqqvaTVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPL 192
Cdd:PRK13638 91 FYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501488905 193 LVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK13638 171 GRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
41-241 |
8.17e-19 |
|
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: 82.54 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPdkiVRRGIFQVMEGRRIVSDMTSL 120
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETP-----QSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 121 ENLRLGA-----FTRSDREVGRDIemvynyfprlKERTGLAGY-------LSGGEQQMLAIGRALMARPKMILMDEPSMG 188
Cdd:cd03298 89 QNVGLGLspglkLTAEDRQAIEVA----------LARVGLAGLekrlpgeLSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501488905 189 LSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-246 |
9.81e-19 |
|
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: 82.66 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAisgLLKTEDgeVTRGEIVFDGERIDGTDPDKiVRRGI 104
Cdd:cd03253 4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL---LFRFYD--VSSGSILIDGQDIREVTLDS-LRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 105 FQVMEGRRIVSDmTSLENLRLGAFTRSDREVGR-----DIEMVYNYFP-----RLKERtGLagYLSGGEQQMLAIGRALM 174
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGRPDATDEEVIEaakaaQIHDKIMRFPdgydtIVGER-GL--KLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 175 ARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLVEQNARAALSvASHGYIMEQGKVVLDGTADEL 246
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
35-246 |
1.45e-18 |
|
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: 82.20 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 35 ILVLRGLSLDVPQGAIVALLGANGAGKSTTlkaISGLLKTEDgeVTRGEIVFDGERIDGTDPDKIvrRGIFQVMEGRRIV 114
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLERFYD--PTSGEILLDGVDIRDLNLRWL--RSQIGLVSQEPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDMTSLENLRLGAFTRSDREVGRDIEMVYNY-----FP-RLKERTGLAGY-LSGGEQQMLAIGRALMARPKMILMDEPSM 187
Cdd:cd03249 89 FDGTIAENIRYGKPDATDEEVEEAAKKANIHdfimsLPdGYDTLVGERGSqLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 188 GLSpllvKEVFAIIQQ-INR-DLGVTILLVEQNArAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:cd03249 169 ALD----AESEKLVQEaLDRaMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-185 |
1.46e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIV----FDGERiDGTD 95
Cdd:COG0488 314 KVLELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVkigyFDQHQ-EELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 96 PDKIVrrgiFQVMegRRIVSDMTSLEnLR--LGAF----TRSDREVGRdiemvynyfprlkertglagyLSGGEQQMLAI 169
Cdd:COG0488 392 PDKTV----LDEL--RDGAPGGTEQE-VRgyLGRFlfsgDDAFKPVGV---------------------LSGGEKARLAL 443
|
170
....*....|....*.
gi 501488905 170 GRALMARPKMILMDEP 185
Cdd:COG0488 444 AKLLLSPPNVLLLDEP 459
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
42-246 |
1.68e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.94 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 42 SLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtRGEIVFDGERIDGTDPDkivRRGIFQVMEGRRIVSDMTSLE 121
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA-----SGSLTLNGQDHTTTPPS---RRPVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 122 NLRLG-----AFTRSDREVGRDI--EM-VYNYFPRLkertglAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLL 193
Cdd:PRK10771 91 NIGLGlnpglKLNAAQREKLHAIarQMgIEDLLARL------PGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501488905 194 VKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK10771 165 RQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-244 |
1.84e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.42 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 9 PPQPGASTAPAPLLsVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDG 88
Cdd:PRK11247 1 MMNTARLNQGTPLL-LNAVSKRYGERT-VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 ERIDgtdpdkivRRGIFQvmeGRRIVSDMTSLENLRLG-------AFTRSDREVGrdiemvynyfprLKERTG-LAGYLS 160
Cdd:PRK11247 79 ARED--------TRLMFQ---DARLLPWKKVIDNVGLGlkgqwrdAALQALAAVG------------LADRANeWPAALS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLD 240
Cdd:PRK11247 136 GGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
....
gi 501488905 241 GTAD 244
Cdd:PRK11247 216 LTVD 219
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
43-241 |
1.98e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.77 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 43 LDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGE-IVFDGERIDGTDPDKivrRGIFQVMEGRRIVSDMTSLE 121
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLPPEK---RRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 122 NLRLGaFTRSDRE-----VGR-DIEMVYNYFPrlkertglaGYLSGGEQQMLAIGRALMARPKMILMDEPsmgLSPLLV- 194
Cdd:PRK11144 96 NLRYG-MAKSMVAqfdkiVALlGIEPLLDRYP---------GSLSGGEKQRVAIGRALLTAPELLLMDEP---LASLDLp 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501488905 195 --KEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:PRK11144 163 rkRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
33-257 |
2.12e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.05 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 33 DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV-TRGEIVFdgeridgtdpdkivrrgIFQVMEGr 111
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVeVNGRVSA-----------------LLELGAG- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 112 rIVSDMTSLENLRLGA----FTRSD-REVGRDIEmvynyfprlkERTGLAGYL-------SGGEQQMLAIGRALMARPKM 179
Cdd:COG1134 99 -FHPELTGRENIYLNGrllgLSRKEiDEKFDEIV----------EFAELGDFIdqpvktySSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 180 ILMDEpsmGLSpllV------KEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADElrdnedVK 253
Cdd:COG1134 168 LLVDE---VLA---VgdaafqKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE------VI 234
|
....
gi 501488905 254 EFYL 257
Cdd:COG1134 235 AAYE 238
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
38-254 |
2.48e-18 |
|
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: 81.36 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKIVrrgifqVMEGRRIVSDM 117
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQP-----TSGGVILEGKQITEPGPDRMV------VFQNYSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLGA------FTRSDRE--VGRDIEMVynyfprlkertGLA-------GYLSGGEQQMLAIGRALMARPKMILM 182
Cdd:TIGR01184 70 TVRENIALAVdrvlpdLSKSERRaiVEEHIALV-----------GLTeaadkrpGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 183 DEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKV-----VLDGTADELRDNEDVKE 254
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAanigqILEVPFPRPRDRLEVVE 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-208 |
2.90e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEvtrGEIVFDGERIDGTDPDKI 99
Cdd:PRK13549 4 YLLEMKNITKTFGGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYE---GEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLENLRLGaftrsdREVGR----DIEMVYNYFPRLKERTGLA-------GYLSGGEQQMLA 168
Cdd:PRK13549 80 ERAGIAIIHQELALVKELSVLENIFLG------NEITPggimDYDAMYLRAQKLLAQLKLDinpatpvGNLGLGQQQLVE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 501488905 169 IGRALMARPKMILMDEPSmglSPLLVKEVfAIIQQINRDL 208
Cdd:PRK13549 154 IAKALNKQARLLILDEPT---ASLTESET-AVLLDIIRDL 189
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-256 |
3.28e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.67 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDKIVRR 102
Cdd:COG4604 3 EIKNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVL-----VDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 gifqvmegrrivsdMTSLE-----NLRL---------------GAFTRSDREVgrdIEMVYNYFprlkERTGLAG-Y--- 158
Cdd:COG4604 77 --------------LAILRqenhiNSRLtvrelvafgrfpyskGRLTAEDREI---IDEAIAYL----DLEDLADrYlde 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 LSGGEQQmlaigRALMArpkM--------ILMDEPsmgLSPLLVKEVFAIIQQINR---DLGVTILLV--EQNARAALS- 224
Cdd:COG4604 136 LSGGQRQ-----RAFIA---MvlaqdtdyVLLDEP---LNNLDMKHSVQMMKLLRRladELGKTVVIVlhDINFASCYAd 204
|
250 260 270
....*....|....*....|....*....|....
gi 501488905 225 --VAshgyiMEQGKVVLDGTADELRDNEDVKEFY 256
Cdd:COG4604 205 hiVA-----MKDGRVVAQGTPEEIITPEVLSDIY 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-258 |
5.23e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 30 VYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV-TRGEIVFDGERIDGTDPDKIvRRGIFQVM 108
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIkVDGKVLYFGKDIFQIDAIKL-RKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 109 EGRRIVSDMTSLENLRLGAFT---RSDREVGRDIEMVYNYFPRLKE----RTGLAGYLSGGEQQMLAIGRALMARPKMIL 181
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAYPLKShgiKEKREIKKIVEECLRKVGLWKEvydrLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 182 MDEPSMGLSPLLVKEVFAIIQQINRDlgVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL---RDNEDVKEFYLG 258
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftsPKNELTEKYVIG 254
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-218 |
6.58e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 6.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDdVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdGEV-TRGEIVFDGERIDGTDPD- 97
Cdd:PRK14258 6 PAIKVNNLSFYYD-TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVrVEGRVEFFNQNIYERRVNl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRRGIFQVMEGRRIVSdMTSLENLRLGAFT---RSDREVGRDIEMVY---NYFPRLKERTGLAGY-LSGGEQQMLAIG 170
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwRPKLEIDDIVESALkdaDLWDEIKHKIHKSALdLSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQN 218
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-236 |
1.23e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktEDgeVTRGEIVFDGERIDGTDPDKivrR 102
Cdd:PRK11000 5 TLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL---ED--ITSGDLFIGEKRMNDVPPAE---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 GIFQVMEGRRIVSDMTSLENLRLG------AFTRSDREVGRDIEMVYnyFPRLKERTGLAgyLSGGEQQMLAIGRALMAR 176
Cdd:PRK11000 76 GVGMVFQSYALYPHLSVAENMSFGlklagaKKEEINQRVNQVAEVLQ--LAHLLDRKPKA--LSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 177 PKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVA------SHGYIMEQGK 236
Cdd:PRK11000 152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLAdkivvlDAGRVAQVGK 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
15-249 |
1.45e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 80.93 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 15 STAPAPLLSVRNIEVVYDdvilVLRGL--------------SLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVT 80
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFP----VRGGLfgrtvgvvkavdgvSFDIRRGETLGLVGESGCGKSTLGRLLLRLE-----EPT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 RGEIVFDGERIDGTDPDKI--VRRG---IFQ----VMEGRRIVSDMTSlENLRL-GAFTRSDRE--VGRDIEMV------ 142
Cdd:COG4608 72 SGEILFDGQDITGLSGRELrpLRRRmqmVFQdpyaSLNPRMTVGDIIA-EPLRIhGLASKAERRerVAELLELVglrpeh 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 143 YNYFPRlkErtglagyLSGGEQQMLAIGRALMARPKMILMDEPsmgLSPLLVKevfaiIQ-QI-N------RDLGVTILL 214
Cdd:COG4608 151 ADRYPH--E-------FSGGQRQRIGIARALALNPKLIVCDEP---VSALDVS-----IQaQVlNlledlqDELGLTYLF 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 501488905 215 VEQNaraaLSVASHgyI------MEQGKVVLDGTADELRDN 249
Cdd:COG4608 214 ISHD----LSVVRH--IsdrvavMYLGKIVEIAPRDELYAR 248
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-253 |
1.66e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKI 99
Cdd:PRK09700 4 PYISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIH-----EPTKGTITINNINYNKLDHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLENLRLGAF-TRsdREVGRDI----EMVYNYFPRLKeRTGL-------AGYLSGGEQQML 167
Cdd:PRK09700 78 AQLGIGIIYQELSVIDELTVLENLYIGRHlTK--KVCGVNIidwrEMRVRAAMMLL-RVGLkvdldekVANLSISHKQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 168 AIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELR 247
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
....*.
gi 501488905 248 DNEDVK 253
Cdd:PRK09700 234 NDDIVR 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
37-215 |
2.21e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRG---EIVFDGERIDGTDPDKIVRRGIfqVMEGRRi 113
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAggaRVAYVPQRSEVPDSLPLTVRDL--VAMGRW- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 114 vsdmtslenLRLGAFTRSDREVGRDIEmvynyfpRLKERTGLAGY-------LSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:NF040873 84 ---------ARRGLWRRLTRDDRAAVD-------DALERVGLADLagrqlgeLSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180
....*....|....*....|....*....
gi 501488905 187 MGLSPLLVKEVFAIIQQINRDlGVTILLV 215
Cdd:NF040873 148 TGLDAESRERIIALLAEEHAR-GATVVVV 175
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
36-258 |
3.24e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 79.68 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 36 LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGeridGTDPD--KIVRR--GI-FQVMEG 110
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITA----GKKNKklKPLRKkvGIvFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 111 RriVSDMTSLENLRLGA--FTRSDREVGRdiemvynyfpRLKERTGLAGY-----------LSGGEQQMLAIGRALMARP 177
Cdd:PRK13634 97 Q--LFEETVEKDICFGPmnFGVSEEDAKQ----------KAREMIELVGLpeellarspfeLSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 178 KMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL-RDNEDVKEFY 256
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfADPDELEAIG 244
|
..
gi 501488905 257 LG 258
Cdd:PRK13634 245 LD 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-237 |
3.28e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.20 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRR---IV 114
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP-----RTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDMTSLENLRLGAFTRSDREVGR----DIEMVYNYFPRL-----KERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEP 185
Cdd:PRK10762 343 LGMSVKENMSLTALRYFSRAGGSlkhaDEQQAVSDFIRLfniktPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501488905 186 SMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:PRK10762 423 TRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
19-189 |
4.88e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDK 98
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP-----TAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRRgIFQVMEGRRIVSDMTSLENLRLGA---FTRSDREVGRDIEMVynyfPRLKERTGLAGY-------LSGGEQQMLA 168
Cdd:PRK09536 75 ASRR-VASVPQDTSLSFEFDVRQVVEMGRtphRSRFDTWTETDRAAV----ERAMERTGVAQFadrpvtsLSGGERQRVL 149
|
170 180
....*....|....*....|.
gi 501488905 169 IGRALMARPKMILMDEPSMGL 189
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASL 170
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-208 |
6.26e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.25 E-value: 6.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEvtrGEIVFDGERIDGTDPDKIV 100
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWD---GEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRLKE-------RTGLAGYLSGGEQQMLAIGRAL 173
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRElqldadnVTRPVGDYGGGQQQLVEIAKAL 156
|
170 180 190
....*....|....*....|....*....|....*
gi 501488905 174 MARPKMILMDEPSmglSPLLVKEVfAIIQQINRDL 208
Cdd:TIGR02633 157 NKQARLLILDEPS---SSLTEKET-EILLDIIRDL 187
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-215 |
6.53e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.24 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 1 MTEAAELHPPQPGASTAPAPLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT 80
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 R---GEIVFDGER---IDGT---------DPDKIVRRGIFQVmegrrivsdmtsLENLRLGAFTrsdrevgrdiemvyny 145
Cdd:COG4178 422 RpagARVLFLPQRpylPLGTlreallypaTAEAFSDAELREA------------LEAVGLGHLA---------------- 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 146 fPRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQinRDLGVTILLV 215
Cdd:COG4178 474 -ERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISV 540
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
36-246 |
1.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 36 LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeIVFDGERIDGTDPDKIVRRG--IFQVMEGR-- 111
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV----YVDGLDTSDEENLWDIRNKAgmVFQNPDNQiv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 112 -RIVSDMTSLENLRLGAFTRSDRE-VGRDIEMV--YNY---FPRLkertglagyLSGGEQQMLAIGRALMARPKMILMDE 184
Cdd:PRK13633 100 aTIVEEDVAFGPENLGIPPEEIRErVDESLKKVgmYEYrrhAPHL---------LSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 185 PSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSvASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-222 |
1.17e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.77 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTtLKAISGLLKtedgEVTRGEIVFDGERIDGTD 95
Cdd:PRK10535 2 TALLELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKST-LMNILGCLD----KPTSGTYRVAGQDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 96 PDKI--VRRGIFQVMEGR-RIVSDMTSLENLRL-----GAFTRSDREVGRDiemvynyfprLKERTGLA-------GYLS 160
Cdd:PRK10535 77 ADALaqLRREHFGFIFQRyHLLSHLTAAQNVEVpavyaGLERKQRLLRAQE----------LLQRLGLEdrveyqpSQLS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAA 222
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVA 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-246 |
2.03e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDP 96
Cdd:PRK15134 4 PLLAIENLSVAFrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKIvrRGIfqvmEGRRIV----SDMTSL-----------ENLRLGAFTRsdREVGRDiEMVynyfpRLKERTG------- 154
Cdd:PRK15134 84 QTL--RGV----RGNKIAmifqEPMVSLnplhtlekqlyEVLSLHRGMR--REAARG-EIL-----NCLDRVGirqaakr 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 155 LAGY---LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYI 231
Cdd:PRK15134 150 LTDYphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAV 229
|
250
....*....|....*
gi 501488905 232 MEQGKVVLDGTADEL 246
Cdd:PRK15134 230 MQNGRCVEQNRAATL 244
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-237 |
2.11e-16 |
|
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: 74.95 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVI-LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIv 100
Cdd:cd03246 1 LEVENVSFRYPGAEpPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR-----PTSGRVRLDGADISQWDPNEL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDmTSLENLrlgaftrsdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMARPKMI 180
Cdd:cd03246 75 GDHVGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 181 LMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNaRAALSVASHGYIMEQGKV 237
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-258 |
3.74e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 3.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV-TRGeivfdgerIDGTDPDKI 99
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlVSG--------IDTGDFSKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 --VRR--GI-FQVME----GRRIVSDMT-SLENLRLGAFtrsdrEVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAI 169
Cdd:PRK13644 73 qgIRKlvGIvFQNPEtqfvGRTVEEDLAfGPENLCLPPI-----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 170 GRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARaALSVASHGYIMEQGKVVLDGTADELRDN 249
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
....*....
gi 501488905 250 EDVKefYLG 258
Cdd:PRK13644 226 VSLQ--TLG 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
37-256 |
3.91e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeiVFDGERIDGTDPDKIVRRgIFQVMEGRRIVSD 116
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-----WLDGEHIQHYASKEVARR-IGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLENLRLG------AFTRSDREvgrDIEMVyNYFPRLKERTGLAGY----LSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:PRK10253 96 ITVQELVARGryphqpLFTRWRKE---DEEAV-TKAMQATGITHLADQsvdtLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 187 MGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKEFY 256
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-222 |
4.53e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 75.24 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIL---VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktedGEVTRGEIVFDGE---RIDG 93
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQpmsKLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 94 TDPDKIVRRGIFQVMEGRRIVSDMTSLEN----LRLGAFTRSD-REVGRDIEMVYNYFPRLKERtglAGYLSGGEQQMLA 168
Cdd:PRK11629 79 AAKAELRNQKLGFIYQFHHLLPDFTALENvampLLIGKKKPAEiNSRALEMLAAVGLEHRANHR---PSELSGGERQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501488905 169 IGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAA 222
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
38-258 |
4.82e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.94 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDK---IVRRGI---FQVMEGR 111
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVP-----TQGSVRVDDTLITSTSKNKdikQIRKKVglvFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 112 riVSDMTSLENLRLGA--FTRSDREVGRdiemvynyfpRLKERTGLAGY-----------LSGGEQQMLAIGRALMARPK 178
Cdd:PRK13649 98 --LFEETVLKDVAFGPqnFGVSQEEAEA----------LAREKLALVGIseslfeknpfeLSGGQMRRVAIAGILAMEPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 179 MILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGT-ADELRDNEDVKEFYL 257
Cdd:PRK13649 166 ILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKpKDIFQDVDFLEEKQL 244
|
.
gi 501488905 258 G 258
Cdd:PRK13649 245 G 245
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-258 |
6.26e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 76.41 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 8 HPPQPGASTAPAPLLSVRNIEVV-----YDDVILVlRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT-R 81
Cdd:PRK13536 23 HQGISEAKASIPGSMSTVAIDLAgvsksYGDKAVV-NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 82 GEIVFDGERIdgtdpdkiVRRGIFQVMEGRRIVSDMTSLENLRLgaFTRSDREVGRDIEMVYNY---FPRLKERTGL-AG 157
Cdd:PRK13536 102 GVPVPARARL--------ARARIGVVPQFDNLDLEFTVRENLLV--FGRYFGMSTREIEAVIPSlleFARLESKADArVS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 158 YLSGGEQQMLAIGRALMARPKMILMDEPSMGLSP----LLVKEVFAIIQQinrdlGVTILLVEQNARAALSVASHGYIME 233
Cdd:PRK13536 172 DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPharhLIWERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLE 246
|
250 260
....*....|....*....|....*...
gi 501488905 234 QGKVVLDGTADELRDNE---DVKEFYLG 258
Cdd:PRK13536 247 AGRKIAEGRPHALIDEHigcQVIEIYGG 274
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
32-222 |
6.39e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.82 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 32 DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktEDGevTRGEIVFDGERIDGTDPD---KIVRRGIFQVM 108
Cdd:PRK10584 20 EHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGL---DDG--SSGEVSLVGQPLHQMDEEaraKLRAKHVGFVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 109 EGRRIVSDMTSLENLRLGAFTR--SDREVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:PRK10584 95 QSFMLIPTLNALENVELPALLRgeSSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 501488905 187 MGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAA 222
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-185 |
1.06e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEivfdGERI------DGTDPD 97
Cdd:COG0488 1 LENLSKSFGGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GLRIgylpqePPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRRGIFQVM-EGRRIVSDMTSLENlRLGAFTRSDREVGR---DIEMV--YNYFPRLKE---RTGLAGY--------LS 160
Cdd:COG0488 76 LTVLDTVLDGDaELRALEAELEELEA-KLAEPDEDLERLAElqeEFEALggWEAEARAEEilsGLGFPEEdldrpvseLS 154
|
170 180
....*....|....*....|....*
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEP 185
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-245 |
1.80e-15 |
|
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: 75.94 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 8 HPPQPGASTAPAP--LLSVRNIEVVY--DDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGE 83
Cdd:COG4618 315 VPAEPERMPLPRPkgRLSVENLTVVPpgSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP-----TAGS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 84 IVFDGERIDGTDPDKIvrrgifqvmeGRRI------VS--DMTSLENL-RLGAFTRSD-----REVGRDiEMVyNYFPRl 149
Cdd:COG4618 389 VRLDGADLSQWDREEL----------GRHIgylpqdVElfDGTIAENIaRFGDADPEKvvaaaKLAGVH-EMI-LRLPD- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 150 kertglaGY----------LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNa 219
Cdd:COG4618 456 -------GYdtrigeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHR- 526
|
250 260
....*....|....*....|....*.
gi 501488905 220 RAALSVASHGYIMEQGKVVLDGTADE 245
Cdd:COG4618 527 PSLLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
41-258 |
2.77e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGerIDGTDPDKIVRRG---IFQVMEGRriVSDM 117
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSS--TSKQKEIKPVRKKvgvVFQFPESQ--LFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLG------AFTRSDREVGRDIEMVyNYFPRLKERTGLAgyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSP 191
Cdd:PRK13643 101 TVLKDVAFGpqnfgiPKEKAEKIAAEKLEMV-GLADEFWEKSPFE--LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 192 LLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGT-ADELRDNEDVKEFYLG 258
Cdd:PRK13643 178 KARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTpSDVFQEVDFLKAHELG 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-238 |
2.85e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.57 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIL--------VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT-RGEIV--FDG 88
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLsgkhqhqtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwRGEPLakLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 ERIdgtdpdKIVRRGI---FQVMEG----RRIVSDMTSlENLR-LGAFTRSDREVgRDIEMVYNYFPRLKERTGLAGYLS 160
Cdd:PRK10419 82 AQR------KAFRRDIqmvFQDSISavnpRKTVREIIR-EPLRhLLSLDKAERLA-RASEMLRAVDLDDSVLDKRPPQLS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 161 GGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVV 238
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-258 |
3.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.66 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIvfdgeRIDGTDPDKIVRR-----GI-FQVMEGR 111
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDI-----TITHKTKDKYIRPvrkriGMvFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 112 rIVSDMTSLEnLRLGAftrsdREVGRDIEMVYNYFPRLKERTGLAG--------YLSGGEQQMLAIGRALMARPKMILMD 183
Cdd:PRK13646 98 -LFEDTVERE-IIFGP-----KNFKMNLDEVKNYAHRLLMDLGFSRdvmsqspfQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 184 EPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL-RDNEDVKEFYLG 258
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfKDKKKLADWHIG 246
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
10-241 |
3.81e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 10 PQPGASTAPaPLLSVRNIEVVYD----------DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgev 79
Cdd:PRK15134 265 PVPLPEPAS-PLLDVEQLQVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS----- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 80 tRGEIVFDGERIDGTDPDKI--VRRGI---FQ--------VMEGRRIVSDMTSLENLRLGAFTRSDR------EVGRDIE 140
Cdd:PRK15134 339 -QGEIWFDGQPLHNLNRRQLlpVRHRIqvvFQdpnsslnpRLNVLQIIEEGLRVHQPTLSAAQREQQviavmeEVGLDPE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 141 MVYNYfprlkertglAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNAR 220
Cdd:PRK15134 418 TRHRY----------PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
250 260
....*....|....*....|.
gi 501488905 221 AALSVASHGYIMEQGKVVLDG 241
Cdd:PRK15134 488 VVRALCHQVIVLRQGEVVEQG 508
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
36-258 |
5.30e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 74.30 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 36 LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDG---ERIDGTDPDKIVRRGIFQVMEGRR 112
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLI-----EPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSDMTSLEN----LRLGAFTRSDREvgrdiEMVYNYFPRLKERTGLAGY---LSGGEQQMLAIGRALMARPKMILMDEP 185
Cdd:PRK10070 117 LMPHMTVLDNtafgMELAGINAEERR-----EKALDALRQVGLENYAHSYpdeLSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 186 SMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRD---NEDVKEFYLG 258
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNnpaNDYVRTFFRG 267
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-222 |
6.20e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.50 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDKI 99
Cdd:PRK14239 4 PILQVSDLSVYYNKK-KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 -VRRGIFQVMEGRRIVSdMTSLEN----LRLGAF---TRSDREVGRDIEMVyNYFPRLKER---TGLAgyLSGGEQQMLA 168
Cdd:PRK14239 83 dLRKEIGMVFQQPNPFP-MSIYENvvygLRLKGIkdkQVLDEAVEKSLKGA-SIWDEVKDRlhdSALG--LSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501488905 169 IGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLgvTILLVEQNARAA 222
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQA 210
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
41-246 |
6.39e-15 |
|
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: 74.48 E-value: 6.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRR---IVSDM 117
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGK----FEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLGAF----TRSDREVGRDIEMVYNYFPRLKERTGLA----GYLSGGEQQMLAIGRALMARPKMILMDEPSMGL 189
Cdd:TIGR02633 355 GVGKNITLSVLksfcFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 190 SPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL 490
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
24-257 |
6.53e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.20 E-value: 6.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDD----VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgEIVFDGERIDGTDP--- 96
Cdd:PRK13651 5 VKNIVKIFNKklptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI---EWIFKDEKNKKKTKeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 ---DKIV-----RRGIFQVMEGRRIVS-----------DMTSLENLRLGAFT-----RSDREVGRD-IEMV---YNYFPR 148
Cdd:PRK13651 82 kvlEKLViqktrFKKIKKIKEIRRRVGvvfqfaeyqlfEQTIEKDIIFGPVSmgvskEEAKKRAAKyIELVgldESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 149 LKERtglagyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASH 228
Cdd:PRK13651 162 SPFE------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKR 234
|
250 260 270
....*....|....*....|....*....|
gi 501488905 229 GYIMEQGKVVLDG-TADELRDNEDVKEFYL 257
Cdd:PRK13651 235 TIFFKDGKIIKDGdTYDILSDNKFLIENNM 264
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
33-250 |
7.52e-15 |
|
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: 72.13 E-value: 7.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 33 DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeiVFDGERIDGTDPDKIvRRGIFQVMEGRR 112
Cdd:cd03252 13 DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-----LVDGHDLALADPAWL-RRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSDmTSLENLRLGAFTRSDREVGRDIEM--VYNYFPRLKErtglaGY----------LSGGEQQMLAIGRALMARPKMI 180
Cdd:cd03252 87 LFNR-SIRDNIALADPGMSMERVIEAAKLagAHDFISELPE-----GYdtivgeqgagLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 181 LMDEPSMGLSpllvKEVFAIIQQINRDL--GVTILLVEQNArAALSVASHGYIMEQGKVVLDGTADELRDNE 250
Cdd:cd03252 161 IFDEATSALD----YESEHAIMRNMHDIcaGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-212 |
8.57e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.88 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLkTEDGevtrGEIVFDGERIDGTDPDKI 99
Cdd:PRK10762 3 ALLQLKGIDKAFPGV-KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIY-TRDA----GSILYLGKEVTFNGPKSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLENLRLG-AFTRSdreVGR-DIEMVYNYFPRLKERTG-------LAGYLSGGEQQMLAIG 170
Cdd:PRK10762 77 QEAGIGIIHQELNLIPQLTIAENIFLGrEFVNR---FGRiDWKKMYAEADKLLARLNlrfssdkLVGELSIGEQQMVEIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTI 212
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGI 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-238 |
9.66e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 9.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVYD-------DVILVLRGL---------SLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDG 88
Cdd:PRK11288 240 REIGDIYGyrprplgEVRLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATR-----RTAGQVYLDG 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 ERIDGTDPDKIVRRGIFQVMEGRR---IVSDMTSLEN---------LRLGAFTRSDREvgrdIEMVYNYFPRLKERT--- 153
Cdd:PRK11288 315 KPIDIRSPRDAIRAGIMLCPEDRKaegIIPVHSVADNinisarrhhLRAGCLINNRWE----AENADRFIRSLNIKTpsr 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 154 -GLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIM 232
Cdd:PRK11288 391 eQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVM 469
|
....*.
gi 501488905 233 EQGKVV 238
Cdd:PRK11288 470 REGRIA 475
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
38-252 |
1.29e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 72.35 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGErIDGTDPDKIVRRGI---FQVMEgRRIV 114
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAN-LKKIKEVKRLRKEIglvFQFPE-YQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDmTSLENLRLGAFtrsdrEVGRDIEMVYNYFPRLKERTGLAG--------YLSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:PRK13645 105 QE-TIEKDIAFGPV-----NLGENKQEAYKKVPELLKLVQLPEdyvkrspfELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 187 MGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDV 252
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-186 |
1.39e-14 |
|
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: 73.43 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILVlRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIV----FDGERiDGTDPD 97
Cdd:TIGR03719 323 IEAENLTKAFGDKLLI-DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVklayVDQSR-DALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVrrgiFQVmegrriVSDmtSLENLRLGAFTRSDRE-VGRdiemvYNYfpRLKERTGLAGYLSGGEQQMLAIGRALMAR 176
Cdd:TIGR03719 401 KTV----WEE------ISG--GLDIIKLGKREIPSRAyVGR-----FNF--KGSDQQKKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|
gi 501488905 177 PKMILMDEPS 186
Cdd:TIGR03719 462 GNVLLLDEPT 471
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-251 |
1.42e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 71.71 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYD-DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDK 98
Cdd:PRK13648 6 SIIVFKNVSFQYQsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEK-----VKSGEIFYNNQAITDDNFEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRR-GI-FQVMEGRRIVSDMT-----SLENLRL--GAFTRSDREVGRDIEMV--YNYFPRlkertglagYLSGGEQQML 167
Cdd:PRK13648 81 LRKHiGIvFQNPDNQFVGSIVKydvafGLENHAVpyDEMHRRVSEALKQVDMLerADYEPN---------ALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 168 AIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSvASHGYIMEQGKVVLDGTADELR 247
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
....
gi 501488905 248 DNED 251
Cdd:PRK13648 231 DHAE 234
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-246 |
1.56e-14 |
|
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: 71.11 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYD-DVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKIv 100
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFY-----DVDSGRILIDGHDVRDYTLASL- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVSDmTSLENLRLGAFTRSDREVGRDIEMVY----------NYFPRLKERtglAGYLSGGEQQMLAIG 170
Cdd:cd03251 75 RRQIGLVSQDVFLFND-TVAENIAYGRPGATREEVEEAARAANahefimelpeGYDTVIGER---GVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlgvtillveqnaRAALSVAsHG----------YIMEQGKVVLD 240
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKN------------RTTFVIA-HRlstienadriVVLEDGKIVER 217
|
....*.
gi 501488905 241 GTADEL 246
Cdd:cd03251 218 GTHEEL 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
24-254 |
1.70e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 71.69 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIdgtdpdKIVRRG 103
Cdd:PRK13647 7 VEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE------KWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 104 ---IFQVMEGRriVSDMTSLE-------NLRLGAfTRSDREVGRDIEMVynyfpRLKERTGLAGY-LSGGEQQMLAIGRA 172
Cdd:PRK13647 81 vglVFQDPDDQ--VFSSTVWDdvafgpvNMGLDK-DEVERRVEEALKAV-----RMWDFRDKPPYhLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 173 LMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGtADELRDNEDV 252
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDI 230
|
..
gi 501488905 253 KE 254
Cdd:PRK13647 231 VE 232
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
22-186 |
1.76e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 69.01 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGeivfdgeridgtdpdkivr 101
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 rgifqvmegrrivsdmtslENLRLGaftrsdrevgrdiemvynYFPRlkertglagyLSGGEQQMLAIGRALMARPKMIL 181
Cdd:cd03221 61 -------------------STVKIG------------------YFEQ----------LSGGEKMRLALAKLLLENPNLLL 93
|
....*
gi 501488905 182 MDEPS 186
Cdd:cd03221 94 LDEPT 98
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
48-246 |
2.09e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 48 GAIVALLGANGAGKSTTLKAISGLLKTedGEVTRGEIVFDGERIDGtdpDKIVRRGIFqVMEGRRIVSDMTSLENLRLGA 127
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGMPIDA---KEMRAISAY-VQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 128 FTRSDREVGRD--IEMVYNYFPRL------KERTGLAGY---LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKE 196
Cdd:TIGR00955 125 HLRMPRRVTKKekRERVDEVLQALglrkcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 501488905 197 VFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-241 |
2.24e-14 |
|
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: 69.89 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEV-----VYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedGEVTRGEIVFDGERIDgtdP 96
Cdd:cd03213 4 LSFRNLTVtvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRT---GLGVSGEVLINGRPLD---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKIVRRGIFqVMEGRRIVSDMTSLENLRLGAFTRSdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMAR 176
Cdd:cd03213 78 RSFRKIIGY-VPQDDILHPTLTVRETLMFAAKLRG---------------------------LSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 177 PKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAAL-SVASHGYIMEQGKVVLDG 241
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-218 |
2.65e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtRGEIVFDGERIDGTdpdkiv 100
Cdd:PRK13540 1 MLDVIELDFDYHDQPL-LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-----KGEILFERQSIKKD------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 rRGIFQ---VMEGRR--IVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRLKERTGLagyLSGGEQQMLAIGRALMA 175
Cdd:PRK13540 69 -LCTYQkqlCFVGHRsgINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL---LSSGQKRQVALLRLWMS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQN 218
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
37-256 |
2.87e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.97 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISgllktEDGEVTRGEIVFDGERIDGTDPDKIVRRGIF--------QVM 108
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLG-----RHQPPSEGEILLDAQPLESWSSKAFARKVAYlpqqlpaaEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 109 EGRRIVSDMTSLENLRLGAFTRSDRE-VGRDIEMVynYFPRLKERtgLAGYLSGGEQQMLAIGRALMARPKMILMDEPSM 187
Cdd:PRK10575 101 TVRELVAIGRYPWHGALGRFGAADREkVEEAISLV--GLKPLAHR--LVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 188 GLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNEDVKEFY 256
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-246 |
2.92e-14 |
|
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: 72.53 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGllkTEDGEVTRGEIV---------------- 85
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRG---MDQYEPTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 86 FDGER------------IDGTDPDKIVRRGI-----------FQVMEGRRIVSD-MTSLENLRLGAFTRSDREVgRDIEM 141
Cdd:TIGR03269 77 KVGEPcpvcggtlepeeVDFWNLSDKLRRRIrkriaimlqrtFALYGDDTVLDNvLEALEEIGYEGKEAVGRAV-DLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 142 VynyfpRLKER-TGLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNAR 220
Cdd:TIGR03269 156 V-----QLSHRiTHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPE 230
|
250 260
....*....|....*....|....*.
gi 501488905 221 AALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:TIGR03269 231 VIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-246 |
3.55e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.50 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIeVVYDDVILVlRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedG-EVTRGEIVFDGERIdgtDPDKIV 100
Cdd:PRK10418 5 IELRNI-ALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GvRQTAGRVLLDGKPV---APCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRI----VSDMTS--LENLRLGAFTRSD-------REVG-RDIEMVYNYFPRlkertglagYLSGGEQQM 166
Cdd:PRK10418 78 GRKIATIMQNPRSafnpLHTMHThaRETCLALGKPADDatltaalEAVGlENAARVLKLYPF---------EMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 167 LAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQN----ARAALSVAshgyIMEQGKVVLDGT 242
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDmgvvARLADDVA----VMSHGRIVEQGD 224
|
....
gi 501488905 243 ADEL 246
Cdd:PRK10418 225 VETL 228
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
25-241 |
3.64e-14 |
|
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: 69.87 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDpdkivrRGI 104
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT----------VRGRV------SSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 105 FQVMEGrrIVSDMTSLENLRLGAftrsdREVGRDIEMVYNYFPRLKERTGLAGYL-------SGGEQQMLAIGRALMARP 177
Cdd:cd03220 89 LGLGGG--FNPELTGRENIYLNG-----RLLGLSRKEIDEKIDEIIEFSELGDFIdlpvktySSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501488905 178 KMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDG 241
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
38-214 |
4.94e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.52 E-value: 4.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEvtrgeIVFDGERIDGTDPDKI--VRRGIFQVMEGRRIVS 115
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGK-----IWFSGHDITRLKNREVpfLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 116 DMTSLENLRL-----GAftrSDREVGRDIEMVYNYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLS 190
Cdd:PRK10908 93 DRTVYDNVAIpliiaGA---SGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180
....*....|....*....|....
gi 501488905 191 PLLVKEVFAIIQQINRdLGVTILL 214
Cdd:PRK10908 170 DALSEGILRLFEEFNR-VGVTVLM 192
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-246 |
5.20e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.51 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 11 QPGAST--APAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDG 88
Cdd:PRK14271 9 QSGAADvdAAAPAMAAVNLTLGFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 eridgtdpdkivrRGIFQ---VMEGRRIVS---------DMTSLENLRLGAFT------RSDREVGRDIEMVYNYFPRLK 150
Cdd:PRK14271 88 -------------RSIFNyrdVLEFRRRVGmlfqrpnpfPMSIMDNVLAGVRAhklvprKEFRGVAQARLTEVGLWDAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 151 ERTGLAGY-LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLgvTILLVEQNARAALSVASHG 229
Cdd:PRK14271 155 DRLSDSPFrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRA 232
|
250
....*....|....*..
gi 501488905 230 YIMEQGKVVLDGTADEL 246
Cdd:PRK14271 233 ALFFDGRLVEEGPTEQL 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
37-215 |
5.68e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.22 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedGEVTRGEIVFDGERIDGTDP--DKIVRRGIF-QVMEgrri 113
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGCVDVPDNQFGREASliDAIGRKGDFkDAVE---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 114 vsdmtslenlRLGAFTRSDrevgrdiemVYNYFPRLKErtglagyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLL 193
Cdd:COG2401 118 ----------LLNAVGLSD---------AVLWLRRFKE-------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|..
gi 501488905 194 VKEVFAIIQQINRDLGVTILLV 215
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVA 193
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
40-249 |
5.87e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 40 GLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDGTDPDKI--VRRGIfqvmegRRIVSD- 116
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA-----TDGEVAWLGKDLLGMKDDEWraVRSDI------QMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLeNLRLgaftrsdrEVGRDI-EMVYNYFPRL-----KERT-------GLAGYL--------SGGEQQMLAIGRALMA 175
Cdd:PRK15079 108 LASL-NPRM--------TIGEIIaEPLRTYHPKLsrqevKDRVkammlkvGLLPNLinryphefSGGQCQRIGIARALIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNaraaLSVASH----GYIMEQGKVVLDGTADELRDN 249
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHD----LAVVKHisdrVLVMYLGHAVELGTYDEVYHN 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-252 |
6.13e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 70.65 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 17 APAPL-----LSVRNIEVVYDD----VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFD 87
Cdd:PRK13631 12 VPNPLsddiiLRVKNLYCVFDEkqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 88 GERIDGTDPDKIVRRGIFQVMEGRRIVSDMTSLENLRLGAFTrsdreVGRDIEM------VYNYFPRLK-----ERTGLa 156
Cdd:PRK13631 92 DKKNNHELITNPYSKKIKNFKELRRRVSMVFQFPEYQLFKDT-----IEKDIMFgpvalgVKKSEAKKLakfylNKMGL- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 157 GY---------LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVAS 227
Cdd:PRK13631 166 DDsylerspfgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVAD 244
|
250 260
....*....|....*....|....*
gi 501488905 228 HGYIMEQGKVVLDGTADELRDNEDV 252
Cdd:PRK13631 245 EVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
37-247 |
7.01e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLL---KTEDGEVTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRRI 113
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 114 ----VSDMTSL----ENLRLGAFTRSDREVG-RDIEmvynyfprLKERTGLAG----YLSGGEQQMLAIGRAL------- 173
Cdd:PRK13547 96 fafsAREIVLLgrypHARRAGALTHRDGEIAwQALA--------LAGATALVGrdvtTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 174 --MARPKMILMDEPSMGLSPLLVKEVFAIIQQINRD--LGVTILLVEQN--ARAALSVAshgyIMEQGKVVLDGT-ADEL 246
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnLGVLAIVHDPNlaARHADRIA----MLADGAIVAHGApADVL 243
|
.
gi 501488905 247 R 247
Cdd:PRK13547 244 T 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-250 |
7.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.76 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVY--DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDgevtrGEIVFDGERIDGTDPDK 98
Cdd:PRK13650 4 IIEVKNLTFKYkeDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAES-----GQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IvRRGIFQVMEgrrivsdmtSLENLRLGAFTRSDREVGRD------IEMVynyfPRLKERTGLAGY----------LSGG 162
Cdd:PRK13650 79 I-RHKIGMVFQ---------NPDNQFVGATVEDDVAFGLEnkgiphEEMK----ERVNEALELVGMqdfkereparLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 163 EQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNA-RAALSvaSHGYIMEQGKVVLDG 241
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLdEVALS--DRVLVMKNGQVESTS 222
|
250
....*....|.
gi 501488905 242 TADEL--RDNE 250
Cdd:PRK13650 223 TPRELfsRGND 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-186 |
8.11e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.92 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDVILVlRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIV----FDGERiDGTDPDKI 99
Cdd:PRK11819 327 AENLSKSFGDRLLI-DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVklayVDQSR-DALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VrrgiFQVmegrriVSDmtSLENLRLGAFTRSDRE-VGRdiemvYNYfprlkerTG-----LAGYLSGGEQQMLAIGRAL 173
Cdd:PRK11819 405 V----WEE------ISG--GLDIIKVGNREIPSRAyVGR-----FNF-------KGgdqqkKVGVLSGGERNRLHLAKTL 460
|
170
....*....|...
gi 501488905 174 MARPKMILMDEPS 186
Cdd:PRK11819 461 KQGGNVLLLDEPT 473
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-215 |
9.75e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 9.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlktEdgEVTRGEIVFDGERIDGTDPDKivr 101
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL---E--RITSGEIWIGGRVVNELEPAD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRRIVSDMTSLENLrlgAFTRSDREVGRD-IEMvynyfpRLKE--RT-GLAGY-------LSGGEQQMLAIG 170
Cdd:PRK11650 76 RDIAMVFQNYALYPHMSVRENM---AYGLKIRGMPKAeIEE------RVAEaaRIlELEPLldrkpreLSGGQRQRVAMG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 501488905 171 RALMARPKMILMDEPsmgLSPLLVK-------EvfaiIQQINRDLGVTILLV 215
Cdd:PRK11650 147 RAIVREPAVFLFDEP---LSNLDAKlrvqmrlE----IQRLHRRLKTTSLYV 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-238 |
1.61e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.14 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDgevtrGEIVFDGERIDGTDPDKIVRRGIFQVMEGRRIVSDM 117
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS-----GSILFQGKEIDFKSSKEALENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLGAFTRS-----DREVGRDIEMVYNYF-----PRLKERTglagyLSGGEQQMLAIGRALMARPKMILMDEPSM 187
Cdd:PRK10982 89 SVMDNMWLGRYPTKgmfvdQDKMYRDTKAIFDELdididPRAKVAT-----LSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501488905 188 GLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGYIMEQGKVV 238
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-257 |
1.67e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.09 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERID---GTDPDKIVRRGI---FQVMEGR 111
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKP-----SSGTITIAGYHITpetGNKNLKKLRKKVslvFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 112 riVSDMTSLENLRLGA--FTRSDREVGrdiEMVYNYFPRLKERTGLAGY----LSGGEQQMLAIGRALMARPKMILMDEP 185
Cdd:PRK13641 98 --LFENTVLKDVEFGPknFGFSEDEAK---EKALKWLKKVGLSEDLISKspfeLSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 186 SMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADEL-RDNEDVKEFYL 257
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIfSDKEWLKKHYL 244
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
20-244 |
1.95e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.13 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGllkTEDGEVTRGEIVFDGERIDGTDPDKI 99
Cdd:CHL00131 6 PILEIKNLHASVNE-NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HPAYKILEGDILFKGESILDLEPEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRDIEMVyNYFPRLKERTGLAGY------------LSGGEQQML 167
Cdd:CHL00131 82 AHLGIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPL-EFLEIINEKLKLVGMdpsflsrnvnegFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 168 AIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARaALSVASHGY--IMEQGKVVLDGTAD 244
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYQR-LLDYIKPDYvhVMQNGKIIKTGDAE 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
37-227 |
2.48e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.19 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDKIVrrgIFQvMEGR---RI 113
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSIT-----LDGKPVEGPGAERGV---VFQ-NEGLlpwRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 114 VSDMTSLeNLRLGAFTRSDREVgRDIEMVynyfprlkERTGLAGY-------LSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:PRK11248 87 VQDNVAF-GLQLAGVEKMQRLE-IAHQML--------KKVGLEGAekryiwqLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501488905 187 MGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVAS 227
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMAT 197
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
22-250 |
3.99e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.90 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDV-ILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRgeIVFDGEridgtdpdKIV 100
Cdd:PRK13640 6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSK--ITVDGI--------TLT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RRGIFQVMEGRRIVsdMTSLENLRLG-------AFTRSDREVGRDiEMVyNYFPRLKERTGLAGY-------LSGGEQQM 166
Cdd:PRK13640 76 AKTVWDIREKVGIV--FQNPDNQFVGatvgddvAFGLENRAVPRP-EMI-KIVRDVLADVGMLDYidsepanLSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 167 LAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAAlSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
|
....
gi 501488905 247 RDNE 250
Cdd:PRK13640 231 FSKV 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-257 |
7.70e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILV--LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDK 98
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK-----IDGELLTAENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IvRRGIFQVMEgrrivsdmtSLENLRLGAFTRSDREVGRDIEMV--YNYFPRLKE----------RTGLAGYLSGGEQQM 166
Cdd:PRK13642 79 L-RRKIGMVFQ---------NPDNQFVGATVEDDVAFGMENQGIprEEMIKRVDEallavnmldfKTREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 167 LAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSvASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
250
....*....|..
gi 501488905 247 -RDNEDVKEFYL 257
Cdd:PRK13642 228 fATSEDMVEIGL 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-246 |
1.43e-12 |
|
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: 67.13 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVY----DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgEIVFDGERIDGTD 95
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV---NVRVGDEWVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 96 PDKIVR----RGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGRdIEMVYNY----FPRLKERTGLAGY---LSGGEQ 164
Cdd:TIGR03269 355 PGPDGRgrakRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELAR-MKAVITLkmvgFDEEKAEEILDKYpdeLSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTAD 244
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
..
gi 501488905 245 EL 246
Cdd:TIGR03269 514 EI 515
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
10-184 |
1.82e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.05 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 10 PQPGASTAPAPLLS----VRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIV 85
Cdd:PRK10790 325 PRQQYGNDDRPLQSgridIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 86 FDGeRIDGTDPDKIVRRGIFQVMEGRRIVSDmTSLENLRLGaftR--SDREVGRDIEMV-YNYFPR-----LKERTGLAG 157
Cdd:PRK10790 400 LDG-RPLSSLSHSVLRQGVAMVQQDPVVLAD-TFLANVTLG---RdiSEEQVWQALETVqLAELARslpdgLYTPLGEQG 474
|
170 180
....*....|....*....|....*...
gi 501488905 158 -YLSGGEQQMLAIGRALMARPKMILMDE 184
Cdd:PRK10790 475 nNLSVGQKQLLALARVLVQTPQILILDE 502
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-259 |
1.86e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 25 RNIEVVyDDVILVLRglsldvpQGAIVALLGANGAGKSTTLKAISGLLKTEdgevTRGEIVFDGERIDGTDPDKIVRRGI 104
Cdd:PRK13549 273 PHIKRV-DDVSFSLR-------RGEILGIAGLVGAGRTELVQCLFGAYPGR----WEGEIFIDGKPVKIRNPQQAIAQGI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 105 FQVMEGRR---IVSDMTSLENLRLGA---FTRSDR-EVGRDIEMVYNYFPRLKERTG---LA-GYLSGGEQQMLAIGRAL 173
Cdd:PRK13549 341 AMVPEDRKrdgIVPVMGVGKNITLAAldrFTGGSRiDDAAELKTILESIQRLKVKTAspeLAiARLSGGNQQKAVLAKCL 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 174 MARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELrDNEDVK 253
Cdd:PRK13549 421 LLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNL-TQEQVM 498
|
....*.
gi 501488905 254 EFYLGG 259
Cdd:PRK13549 499 EAALRS 504
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
41-238 |
1.94e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEvtrgeIVFDGERIDGTDPDKI--VRRG---IFQ----VMEGR 111
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGE-----IIFNGQRIDTLSPGKLqaLRRDiqfIFQdpyaSLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 112 RIVSDmTSLENLRLGAFTRSDREVGRDIEMVynyfprlkERTGL--------AGYLSGGEQQMLAIGRALMARPKMILMD 183
Cdd:PRK10261 418 QTVGD-SIMEPLRVHGLLPGKAAAARVAWLL--------ERVGLlpehawryPHEFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 184 EPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVV 238
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
38-245 |
2.07e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.25 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLkteDGEvtrGEIVFDGERIDGTDPDKIVR-RGIF--QVMEgrriV 114
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL---PGQ---GEILLNGRPLSDWSAAELARhRAYLsqQQSP----P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDMTSLENLRLGAftrsdrEVGRDIEMVYNYFPRLKERTGLA-------GYLSGGEQQ-------MLAIGRALMARPKMI 180
Cdd:COG4138 82 FAMPVFQYLALHQ------PAGASSEAVEQLLAQLAEALGLEdklsrplTQLSGGEWQrvrlaavLLQVWPTINPEGQLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 181 LMDEPSMGLSpllvkevfaIIQQ------INR--DLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADE 245
Cdd:COG4138 156 LLDEPMNSLD---------VAQQaaldrlLRElcQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-185 |
2.29e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.44 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivFDGERIDGTDPDkiv 100
Cdd:PRK13538 1 MLEARNLACERDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL-----WQGEPIRRQRDE--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 rrgIFQVM------EGrrIVSDMTSLENLR--LGAFTRSDREVGRDIemvynyfprLkERTGLAGY-------LSGGEQQ 165
Cdd:PRK13538 72 ---YHQDLlylghqPG--IKTELTALENLRfyQRLHGPGDDEALWEA---------L-AQVGLAGFedvpvrqLSAGQQR 136
|
170 180
....*....|....*....|
gi 501488905 166 MLAIGRALMARPKMILMDEP 185
Cdd:PRK13538 137 RVALARLWLTRAPLWILDEP 156
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-278 |
2.44e-12 |
|
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: 66.86 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtrGEIvfdgeRIDGTDPDKIV 100
Cdd:TIGR01271 1218 MDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE------GEI-----QIDGVSWNSVT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 R---RGIFQVMEGRRIVSDMTSLENLRLGAfTRSDREVGRDIEMV-----YNYFP-RLKERTGLAGY-LSGGEQQMLAIG 170
Cdd:TIGR01271 1287 LqtwRKAFGVIPQKVFIFSGTFRKNLDPYE-QWSDEEIWKVAEEVglksvIEQFPdKLDFVLVDGGYvLSNGHKQLMCLA 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 171 RALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlgVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDNE 250
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN--CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS 1443
|
250 260 270
....*....|....*....|....*....|
gi 501488905 251 DVKEFYlgGAGDQRKSF--KNLKSFKRRKR 278
Cdd:TIGR01271 1444 LFKQAM--SAADRLKLFplHRRNSSKRKPQ 1471
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-237 |
3.27e-12 |
|
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: 65.26 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtrGEIvfdgeRIDGTDPDKIV 100
Cdd:cd03289 3 MTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE------GDI-----QIDGVSWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 R---RGIFQVMEGRRIVSDMTSLENLR-LGAFtrSDREVGR-----DIEMVYNYFP-RLKERTGLAGY-LSGGEQQMLAI 169
Cdd:cd03289 72 LqkwRKAFGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKvaeevGLKSVIEQFPgQLDFVLVDGGCvLSHGHKQLMCL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 170 GRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlgVTILLVEQNARAALSVASHgYIMEQGKV 237
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRF-LVIEENKV 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
18-248 |
6.63e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 18 PAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT-RGEivfDGERIDGTDP 96
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRK-GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyRMR---DGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 97 DKIVRRGIFQV---------MEG-RRIVSD--------MTSLE----NLRLGAFTRSDR-EVGRDiemvynyfpRLKErt 153
Cdd:PRK11701 79 SEAERRRLLRTewgfvhqhpRDGlRMQVSAggnigerlMAVGArhygDIRATAGDWLERvEIDAA---------RIDD-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 154 gLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIME 233
Cdd:PRK11701 148 -LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250
....*....|....*
gi 501488905 234 QGKVVLDGTADELRD 248
Cdd:PRK11701 227 QGRVVESGLTDQVLD 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-215 |
7.73e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGeivfDGERIdGTDPDKI 99
Cdd:PRK09544 3 SLVSLENVSVSFGQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRI-GYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRivsdmtslenLRLGAFTRSDrevgrDIemvynyFPRLKERTglAGY--------LSGGEQQMLAIGR 171
Cdd:PRK09544 77 YLDTTLPLTVNRF----------LRLRPGTKKE-----DI------LPALKRVQ--AGHlidapmqkLSGGETQRVLLAR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLV 215
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMV 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-247 |
7.89e-12 |
|
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: 65.42 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGllkteDGEVTRGEIVFDGERIDGTDPDkiVRRGIFQVMEGRRIVSDMTSL 120
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSILTNISD--VHQNMGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 121 ENLRLGAFTRSdrEVGRDIEMVYNY------FPRLKERtgLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLV 194
Cdd:TIGR01257 2031 EHLYLYARLRG--VPAEEIEKVANWsiqslgLSLYADR--LAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501488905 195 KEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELR 247
Cdd:TIGR01257 2107 RMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLK 2158
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-247 |
8.38e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.15 E-value: 8.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 23 SVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeiVFDGERIDGTDPDKIVRR 102
Cdd:NF033858 3 RLEGVSHRYGKT-VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVE----VLGGDMADARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 ------GIfqvmeGRRIVSDMTSLENL----RLGAFTRSDREvgRDIEmvynyfpRLKERTGL-------AGYLSGGEQQ 165
Cdd:NF033858 78 iaympqGL-----GKNLYPTLSVFENLdffgRLFGQDAAERR--RRID-------ELLRATGLapfadrpAGKLSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 166 MLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlgvtillveqnaRAALSV-ASHGYI-----------ME 233
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAE------------RPGMSVlVATAYMeeaerfdwlvaMD 211
|
250
....*....|....
gi 501488905 234 QGKVVLDGTADELR 247
Cdd:NF033858 212 AGRVLATGTPAELL 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-252 |
8.99e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.13 E-value: 8.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTD----PDKIVRRGIFQVMEGRR 112
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLY-----QPTGGQVLLDGVPLVQYDhhylHRQVALVGQEPVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSDMT-SLENLRLGAFTRSDREVGRD---IEMVYNYFPRLKERTGLagyLSGGEQQMLAIGRALMARPKMILMDEPSMG 188
Cdd:TIGR00958 571 VRENIAyGLTDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVGEKGSQ---LSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 189 LSpllvKEVFAIIQQINRDLGVTILLVEQNaraaLSV---ASHGYIMEQGKVVLDGTADELRDNEDV 252
Cdd:TIGR00958 648 LD----AECEQLLQESRSRASRTVLLIAHR----LSTverADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
40-247 |
1.24e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.99 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 40 GLSLDVPQGAIVALLGANGAGKSTtlKAISGLLKTED-GEVTRGEIVFDGERidgtdpdKIVRRGIFQ---VMEGRRivS 115
Cdd:NF000106 31 GVDLDVREGTVLGVLGP*GAA**R--GALPAHV*GPDaGRRPWRF*TWCANR-------RALRRTIG*hrpVR*GRR--E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 116 DMTSLENL----RLGAFTRSDREVGRDiEMVYNYfpRLKERTG-LAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLS 190
Cdd:NF000106 100 SFSGRENLymigR*LDLSRKDARARAD-ELLERF--SLTEAAGrAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 191 PLLVKEVFAIIQQINRDlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELR 247
Cdd:NF000106 177 PRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-189 |
1.45e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDViLVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdgevtRGEIVFDGERIDGTDPdki 99
Cdd:PRK13539 1 MMLEGEDLACVRGGR-VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPA-----AGTIKLDGGDIDDPDV--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 vrrgiFQVME--GRR--IVSDMTSLENLRLGAFTRSDREvgRDIEmvynyfpRLKERTGL-------AGYLSGGEQQMLA 168
Cdd:PRK13539 72 -----AEACHylGHRnaMKPALTVAENLEFWAAFLGGEE--LDIA-------AALEAVGLaplahlpFGYLSAGQKRRVA 137
|
170 180
....*....|....*....|..
gi 501488905 169 IGRALMA-RPKMILmDEPSMGL 189
Cdd:PRK13539 138 LARLLVSnRPIWIL-DEPTAAL 158
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
10-246 |
1.74e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.59 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 10 PQPGASTAPAPLLSVRNIEVVY---DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLkTEDGEVTrGEIVF 86
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFstpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIG-GSATF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 87 DGERIDGTdPDKIVRR-------GIFQvmegrrivSDMTSLEN-LRLG-----------------AFTRSDREVGRdIEM 141
Cdd:PRK09473 79 NGREILNL-PEKELNKlraeqisMIFQ--------DPMTSLNPyMRVGeqlmevlmlhkgmskaeAFEESVRMLDA-VKM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 142 vynyfPRLKERTGLAGY-LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNAR 220
Cdd:PRK09473 149 -----PEARKRMKMYPHeFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLG 223
|
250 260
....*....|....*....|....*.
gi 501488905 221 AALSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK09473 224 VVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
41-242 |
3.83e-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: 63.49 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgevTRGEIVFDGERIDgTDPDkIVRRGIFQVMEGRRIVSDMTSL 120
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPP-----TSGTVLVGGKDIE-TNLD-AVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 121 ENLRLGAFTRSDREVGRDIEMvynyfPRLKERTGL-------AGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLL 193
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEM-----EAMLEDTGLhhkrneeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 501488905 194 VKEVFAIIQQINRdlGVTILLVEQNARAALSVASHGYIMEQGKVVLDGT 242
Cdd:TIGR01257 1097 RRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-244 |
5.50e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDPDK 98
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS----------ILGQPTRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRRGIFQVMEGRR--------IVSDMTSLEnlRLGAFTRSDREVGRDIEMVYNYFPR---LKERTGLAGYLSGGEQQML 167
Cdd:PRK15056 74 ALQKNLVAYVPQSEevdwsfpvLVEDVVMMG--RYGHMGWLRRAKKRDRQIVTAALARvdmVEFRHRQIGELSGGQKKRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 168 AIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARAALSVASHGyIMEQGKVVLDGTAD 244
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTE 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-215 |
5.52e-11 |
|
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: 60.97 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKIV 100
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV-----ELSSGSILIDGVDISKIGLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 101 RR--GIFQ---VMEGrrivsdmTSLENlrLGAFTR-SDREVGRDIEMVynyfpRLKERTGLAGY------------LSGG 162
Cdd:cd03244 78 SRisIIPQdpvLFSG-------TIRSN--LDPFGEySDEELWQALERV-----GLKEFVESLPGgldtvveeggenLSVG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 163 EQQMLAIGRALMARPKMILMDEPSMGLSPllvkEVFAIIQQINRDL--GVTILLV 215
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDP----ETDALIQKTIREAfkDCTVLTI 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
34-185 |
5.55e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.91 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 34 VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeIVFDGERID--GTDPDKIV---RRGIFQVM 108
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL---VRHDGGWVDlaQASPREILalrRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 109 EGRRIVSDMTSLEN-----LRLGAftrsDREVGRDI-EMVYNYFpRLKER-------TglagyLSGGEQQMLAIGRALMA 175
Cdd:COG4778 100 QFLRVIPRVSALDVvaeplLERGV----DREEARARaRELLARL-NLPERlwdlppaT-----FSGGEQQRVNIARGFIA 169
|
170
....*....|
gi 501488905 176 RPKMILMDEP 185
Cdd:COG4778 170 DPPLLLLDEP 179
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
48-213 |
6.27e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 48 GAIVALLGANGAGKSTTLKAISGLLKTedGEVTRGEIVFDGERIDGTdpdkivrrgiFQvmegRRI---------VSDMT 118
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTT--GVITGGDRLVNGRPLDSS----------FQ----RSIgyvqqqdlhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 119 SLENLRLGAFTRSDREVGRDIEMVY-NYFPRLKERTGLAGYLSG--GE------QQMLAIGRALMARPKMIL-MDEPSMG 188
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKSEKMEYvEEVIKLLEMESYADAVVGvpGEglnveqRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180
....*....|....*....|....*..
gi 501488905 189 LSPllvKEVFAIIQQINR--DLGVTIL 213
Cdd:TIGR00956 933 LDS---QTAWSICKLMRKlaDHGQAIL 956
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
39-254 |
6.62e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 39 RGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedgeVTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRR------ 112
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngffp 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 ---IVSDMTSLENLRLGAFTRS-----DREVGRDIEmvynyfprlKERTGLA----------GYLSGGEQQMLAIGRALM 174
Cdd:PRK09700 355 nfsIAQNMAISRSLKDGGYKGAmglfhEVDEQRTAE---------NQRELLAlkchsvnqniTELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 175 ARPKMILMDEPSMGLSPLLVKEVFAIIQQINrDLGVTILLVEQNARAALSVASHGYIMEQGKVvldgtADELRDNEDVKE 254
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRL-----TQILTNRDDMSE 499
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
37-189 |
7.36e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.20 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeiVFDGERIDGTDPdkIVRRGIFQVMEGRRIVSD 116
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-----LLNGGPLDFQRD--SIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLENLRLGAFTRSDREVGRDIEMVynyfprlkertGLAGY-------LSGGEQQMLAIGRALMARPKMILMDEPSMGL 189
Cdd:cd03231 88 LSVLENLRFWHADHSDEQVEEALARV-----------GLNGFedrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-184 |
8.41e-11 |
|
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: 62.14 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDDVIL-------VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIvfdgeRI 91
Cdd:COG5265 348 APPLVVGGGEVRFENVSFgydperpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY-----DVTSGRI-----LI 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 92 DGTDPDKI----VRRGIfqvmeGrrIVSDMTSL------ENLRLGAFTRSDREVGRDIEMVY----------NYFPRLKE 151
Cdd:COG5265 418 DGQDIRDVtqasLRAAI-----G--IVPQDTVLfndtiaYNIAYGRPDASEEEVEAAARAAQihdfieslpdGYDTRVGE 490
|
170 180 190
....*....|....*....|....*....|...
gi 501488905 152 RtGLAgyLSGGEQQMLAIGRALMARPKMILMDE 184
Cdd:COG5265 491 R-GLK--LSGGEKQRVAIARTLLKNPPILIFDE 520
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
41-246 |
1.15e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.57 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV-------TRGEIVFDGERIDG--TDPDKIV--RRGIFQVME 109
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplHFGDYSYRSQRIRMifQDPSTSLnpRQRISQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 110 -GRRIVSDMTSLEnlRLGAFTRSDREVGRDIEMVYnYFPRLkertglagyLSGGEQQMLAIGRALMARPKMILMDEPSMG 188
Cdd:PRK15112 112 fPLRLNTDLEPEQ--REKQIIETLRQVGLLPDHAS-YYPHM---------LAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 501488905 189 LSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDG-TADEL 246
Cdd:PRK15112 180 LDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGsTADVL 238
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-237 |
1.72e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 1 MTEAAELHPPQPG---ASTAPAPLLSVRNievvyddvilvLRG-----LSLDVPQGAIVALLGANGAGKSTTLKAISGLL 72
Cdd:PRK15439 245 LSASQKLWLELPGnrrQQAAGAPVLTVED-----------LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 73 KtedgeVTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRR---------IVSDMTSLENLRLGAFTRSDREVGRdiemvy 143
Cdd:PRK15439 314 P-----ARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQssglyldapLAWNVCALTHNRRGFWIKPARENAV------ 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 144 nyFPRLKERTGL--------AGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDlGVTILLV 215
Cdd:PRK15439 383 --LERYRRALNIkfnhaeqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFI 459
|
250 260
....*....|....*....|..
gi 501488905 216 EQNARAALSVASHGYIMEQGKV 237
Cdd:PRK15439 460 SSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
22-238 |
2.00e-10 |
|
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: 58.96 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDPDKI- 99
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIE----------IDGIDISTIp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 ---VRRGIFQVMEGRRIVSDmTSLENL-RLGAFtrSDREVgrdiemvynyFPRLKERTGlAGYLSGGEQQMLAIGRALMA 175
Cdd:cd03369 77 ledLRSSLTIIPQDPTLFSG-TIRSNLdPFDEY--SDEEI----------YGALRVSEG-GLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501488905 176 RPKMILMDEPSMGLSpllvKEVFAIIQQINRDL--GVTILLVEQNARaalSVASHGYI--MEQGKVV 238
Cdd:cd03369 143 RPRVLVLDEATASID----YATDALIQKTIREEftNSTILTIAHRLR---TIIDYDKIlvMDAGEVK 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-246 |
2.52e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDD---VILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVF---DGERID-G 93
Cdd:PRK10261 12 VLAVENLNIAFMQeqqKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrSRQVIElS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 94 TDPDKIVR--RG-----IFQvmegrrivSDMTSL-----------ENLRL-GAFTRSD--REVGRDIEMVynyfpRLKE- 151
Cdd:PRK10261 92 EQSAAQMRhvRGadmamIFQ--------EPMTSLnpvftvgeqiaESIRLhQGASREEamVEAKRMLDQV-----RIPEa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 152 RTGLAGY---LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASH 228
Cdd:PRK10261 159 QTILSRYphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADR 238
|
250
....*....|....*...
gi 501488905 229 GYIMEQGKVVLDGTADEL 246
Cdd:PRK10261 239 VLVMYQGEAVETGSVEQI 256
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-213 |
2.88e-10 |
|
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: 58.43 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 35 ILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGllKTEDGEVTRGEIVFDGERIDGTdpDKIVRRGIFQVMEGRRIV 114
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN--RTEGNVSVEGDIHYNGIPYKEF--AEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 115 SDMTSLENLRLGAFTRSDREVgRDIemvynyfprlkertglagylSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLV 194
Cdd:cd03233 96 PTLTVRETLDFALRCKGNEFV-RGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170
....*....|....*....
gi 501488905 195 KEVFAIIQQINRDLGVTIL 213
Cdd:cd03233 155 LEILKCIRTMADVLKTTTF 173
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-215 |
3.29e-10 |
|
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: 57.55 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV---TRGEIVFdgeridgtdpdk 98
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmpEGEDLLF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 99 IVRRGifqvmegrrivsdmtslenlrlgaftrsdrevgrdiemvynYFPRLKERTGLAgY-----LSGGEQQMLAIGRAL 173
Cdd:cd03223 69 LPQRP-----------------------------------------YLPLGTLREQLI-YpwddvLSGGEQQRLAFARLL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501488905 174 MARPKMILMDEPSMGLSPllvkEVFAIIQQINRDLGVTILLV 215
Cdd:cd03223 107 LHKPKFVFLDEATSALDE----ESEDRLYQLLKELGITVISV 144
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
22-236 |
3.48e-10 |
|
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: 58.25 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDV----ILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT----------------- 80
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSvpgsiayvsqepwiqng 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 --RGEIVFdGERID-----------GTDPDkivrrgiFQVMEGRrivsDMTslenlrlgaftrsdrEVGrdiemvynyfp 147
Cdd:cd03250 81 tiRENILF-GKPFDeeryekvikacALEPD-------LEILPDG----DLT---------------EIG----------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 148 rlkERtGLAgyLSGGEQQMLAIGRALMARPKMILMDEPsmgLSPLLVKEVFAIIQQ-INRDL--GVTILLVEQNArAALS 224
Cdd:cd03250 123 ---EK-GIN--LSGGQKQRISLARAVYSDADIYLLDDP---LSAVDAHVGRHIFENcILGLLlnNKTRILVTHQL-QLLP 192
|
250
....*....|..
gi 501488905 225 VASHGYIMEQGK 236
Cdd:cd03250 193 HADQIVVLDNGR 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
33-237 |
7.53e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 33 DVILVLRGL-----------SLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIDGTDPDKIVR 101
Cdd:PRK10982 248 EVILEVRNLtslrqpsirdvSFDLHKGEILGIAGLVGAKRTDIVETLFGIR-----EKSAGTITLHGKKINNHNANEAIN 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 RGIFQVMEGRR--------------IVSDMTSLENlRLGAFtrSDREVGRDIEMVYNYFpRLK---ERTGLaGYLSGGEQ 164
Cdd:PRK10982 323 HGFALVTEERRstgiyayldigfnsLISNIRNYKN-KVGLL--DNSRMKSDTQWVIDSM-RVKtpgHRTQI-GSLSGGNQ 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501488905 165 QMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQI-NRDLGvtILLVEQNARAALSVASHGYIMEQGKV 237
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKG--IIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-246 |
9.88e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.70 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 3 EAAELHPPQPGASTAP-APL-LSVRNIEVV-YDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTedgev 79
Cdd:PRK11174 329 ETPLAHPQQGEKELASnDPVtIEAEDLEILsPDGKTL-AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY----- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 80 tRGEIVFDGERIDGTDPDKIvRRGIF------QVMEGrrivsdmTSLENLRLGAFTRSDREVGRDIEMVY--NYFPRLKE 151
Cdd:PRK11174 403 -QGSLKINGIELRELDPESW-RKHLSwvgqnpQLPHG-------TLRDNVLLGNPDASDEQLQQALENAWvsEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 152 rtGL-------AGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRdlGVTILLV----EQnar 220
Cdd:PRK11174 474 --GLdtpigdqAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVthqlED--- 546
|
250 260
....*....|....*....|....*.
gi 501488905 221 aaLSVASHGYIMEQGKVVLDGTADEL 246
Cdd:PRK11174 547 --LAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-249 |
1.40e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.99 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRN--IEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtEDGEVTRGEIVFDGE---RIDG 93
Cdd:COG4170 2 PLLDIRNltIEIDTpQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRFRWNGIdllKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 94 TDPDKIVRRG---IFQ---------VMEGRRIvsdMTSLENLRLG------AFTRSDR------EVG-RDIEMVYNYFPR 148
Cdd:COG4170 81 RERRKIIGREiamIFQepsscldpsAKIGDQL---IEAIPSWTFKgkwwqrFKWRKKRaiellhRVGiKDHKDIMNSYPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 149 lkertglagYLSGGEQQ--MLAIgrALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVA 226
Cdd:COG4170 158 ---------ELTEGECQkvMIAM--AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWA 226
|
250 260
....*....|....*....|...
gi 501488905 227 SHGYIMEQGKVVLDGTADELRDN 249
Cdd:COG4170 227 DTITVLYCGQTVESGPTEQILKS 249
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-246 |
1.60e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRN--IEVVYDD--VILVLRgLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtEDGEVTRGEIVFDG---ERID 92
Cdd:PRK15093 2 PLLDIRNltIEFKTSDgwVKAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDidlLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 93 GTDPDKIVRRG---IFQVME---------GRRIVSDMTSLeNLRLGAFTRSDREVGRDIEMVYnyfprlkeRTGLAGY-- 158
Cdd:PRK15093 80 PRERRKLVGHNvsmIFQEPQscldpservGRQLMQNIPGW-TYKGRWWQRFGWRKRRAIELLH--------RVGIKDHkd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 --------LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGY 230
Cdd:PRK15093 151 amrsfpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKIN 230
|
250
....*....|....*.
gi 501488905 231 IMEQGKVVLDGTADEL 246
Cdd:PRK15093 231 VLYCGQTVETAPSKEL 246
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-105 |
1.67e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGllkTEDGEVTRGEIVFDGERIDGTDPDKIV 100
Cdd:PRK09580 1 MLSIKDLHVSVEDKA-ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG---REDYEVTGGTVEFKGKDLLELSPEDRA 76
|
....*
gi 501488905 101 RRGIF 105
Cdd:PRK09580 77 GEGIF 81
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-185 |
1.78e-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: 58.02 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDG--ERIDGTDPDKIVRRgifQVMEG-RRI 113
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGylPQEPQLDPTKTVRE---NVEEGvAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 114 VSDMTSLENLRLgAFTRSDRE----------------------VGRDIEMVYNYFpRLKERTGLAGYLSGGEQQMLAIGR 171
Cdd:TIGR03719 97 KDALDRFNEISA-KYAEPDADfdklaaeqaelqeiidaadawdLDSQLEIAMDAL-RCPPWDADVTKLSGGERRRVALCR 174
|
170
....*....|....
gi 501488905 172 ALMARPKMILMDEP 185
Cdd:TIGR03719 175 LLLSKPDMLLLDEP 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-212 |
1.79e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 32 DDVilvlrglSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeiVFdGERIDGTDpdkivrrgifqvMEGR 111
Cdd:NF033858 283 DHV-------SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAW----LF-GQPVDAGD------------IATR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 112 RIVSDMT---SL-------ENLRLGA--FTRSDREVGRDI-EMVynyfprlkERTGLAGY-------LSGGEQQMLAIGR 171
Cdd:NF033858 339 RRVGYMSqafSLygeltvrQNLELHArlFHLPAAEIAARVaEML--------ERFDLADVadalpdsLPLGIRQRLSLAV 410
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTI 212
Cdd:NF033858 411 AVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTI 451
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
36-189 |
2.70e-09 |
|
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: 55.94 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 36 LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeiVFDGERIDGTDpDKIVRRGIFQVMEgRRIVS 115
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-----LLDGKPISQYE-HKYLHSKVSLVGQ-EPVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 116 DMTSLENLRLGAFTRSDREV----------GRDIEMVYNYFPRLKERTGLagyLSGGEQQMLAIGRALMARPKMILMDEP 185
Cdd:cd03248 101 ARSLQDNIAYGLQSCSFECVkeaaqkahahSFISELASGYDTEVGEKGSQ---LSGGQKQRVAIARALIRNPQVLILDEA 177
|
....
gi 501488905 186 SMGL 189
Cdd:cd03248 178 TSAL 181
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
38-246 |
3.46e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.28 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLkaisGLLKTedgevtrgeiVFDGE----RIDGTDPDKIVRRG-------IFQ 106
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLQR----------VFDPQsgriLIDGTDIRTVTRASlrrniavVFQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 107 -VMEGRRIVSDmtsleNLRLGAFTRSDREVGRDIEMVY----------NYFPRLKERtglAGYLSGGEQQMLAIGRALMA 175
Cdd:PRK13657 417 dAGLFNRSIED-----NIRVGRPDATDEEMRAAAERAQahdfierkpdGYDTVVGER---GRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 176 RPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTI----LLVEQNARAALsvashgyIMEQGKVVLDGTADEL 246
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELMKGRTTFIiahrLSTVRNADRIL-------VFDNGRVVESGSFDEL 556
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
20-215 |
6.98e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 20 PLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVTRGEIVFDGERIdGTDPDKI 99
Cdd:PRK10247 6 PLLQLQNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLI-----SPTSGTLLFEGEDI-STLKPEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDmTSLENLRLGAFTRSDREvgrdiEMvyNYFPRLKERTGLA--------GYLSGGEQQMLAIGR 171
Cdd:PRK10247 79 YRQQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQP-----DP--AIFLDDLERFALPdtiltkniAELSGGEKQRISLIR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 501488905 172 ALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLV 215
Cdd:PRK10247 151 NLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWV 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-235 |
7.01e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 17 APAPLLSVRNIEVVYD---------DVILVLRGLSLDVPQGAIVALLGANGAGKSTTlkaisGLLKTEDGEVTRGEIVFD 87
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTL-----ARLLTMIETPTGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 88 GERIDGTDP--DKIVRRGI---FQVMEG----RRIVSDMtsLE-----NLRLGAFTRSDR------EVGRDIEMvYNYFP 147
Cdd:PRK11308 76 GQDLLKADPeaQKLLRQKIqivFQNPYGslnpRKKVGQI--LEeplliNTSLSAAERREKalammaKVGLRPEH-YDRYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 148 RLkertglagyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNaraaLSVAS 227
Cdd:PRK11308 153 HM---------FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD----LSVVE 219
|
250
....*....|....*...
gi 501488905 228 H----------GYIMEQG 235
Cdd:PRK11308 220 HiadevmvmylGRCVEKG 237
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
48-213 |
1.42e-08 |
|
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: 53.40 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 48 GAIVALLGANGAGKSTTLKAISGllKTEDGEVTrGEIvfdgeRIDGTDPDKIVRRGIFQVMEGRRIVSDMTSLENLRLGA 127
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAG--RKTAGVIT-GEI-----LINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRFSA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 128 FTRSdrevgrdiemvynyfprlkertglagyLSGGEQQMLAIGRALMARPKMILMDEPSMGLSPllvKEVFAIIQQINR- 206
Cdd:cd03232 105 LLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS---QAAYNIVRFLKKl 154
|
....*...
gi 501488905 207 -DLGVTIL 213
Cdd:cd03232 155 aDSGQAIL 162
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
21-246 |
1.87e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 21 LLSVRNIEVVYDDVILVLRG---LSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEdGEVTRGEIVFDGE---RIDGT 94
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAvdrISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQdlqRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 95 DPDKIVRRG---IFQvmegrrivSDMTSL-----------ENLRL--GAFTRSDREvgRDIEMVYNY-FPRLKERtgLAG 157
Cdd:PRK11022 82 ERRNLVGAEvamIFQ--------DPMTSLnpcytvgfqimEAIKVhqGGNKKTRRQ--RAIDLLNQVgIPDPASR--LDV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 158 Y---LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTILLVEQNARAALSVASHGYIMEQ 234
Cdd:PRK11022 150 YphqLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA 229
|
250
....*....|..
gi 501488905 235 GKVVLDGTADEL 246
Cdd:PRK11022 230 GQVVETGKAHDI 241
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
30-189 |
2.42e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 30 VYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLlKTedGEVTRGEIvfdgeRIDGTDPDKIVRRGIFQVME 109
Cdd:PLN03140 888 VTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR-KT--GGYIEGDI-----RISGFPKKQETFARISGYCE 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 110 GRRIVS-DMTSLENLRLGAFTRSDREVGRDIEMVYN-------YFPRLKER-TGLAGY--LSGGEQQMLAIGRALMARPK 178
Cdd:PLN03140 960 QNDIHSpQVTVRESLIYSAFLRLPKEVSKEEKMMFVdevmelvELDNLKDAiVGLPGVtgLSTEQRKRLTIAVELVANPS 1039
|
170
....*....|.
gi 501488905 179 MILMDEPSMGL 189
Cdd:PLN03140 1040 IIFMDEPTSGL 1050
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-225 |
2.94e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 15 STAPaPLLSVRNIEVVYDDvILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeivfdgeRIDGt 94
Cdd:PRK13543 6 HTAP-PLLAAHALAFSRNE-EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI----------QIDG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 95 DPDKIVRRGIFQVMEGR--RIVSDMTSLENLR-LGAF--TRSDREVGRDIEMVynyfprlkertGLAGY-------LSGG 162
Cdd:PRK13543 73 KTATRGDRSRFMAYLGHlpGLKADLSTLENLHfLCGLhgRRAKQMPGSALAIV-----------GLAGYedtlvrqLSAG 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 163 EQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVFAIIQQINRDLGVTiLLVEQNARAALSV 225
Cdd:PRK13543 142 QKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAA-LVTTHGAYAAPPV 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-235 |
4.19e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.87 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDV-ILVLRGLSLDVPQGAIVALLGANGAGKSTtlkaISGLLkTEDGEVTRGEIVFDGERI-DGTDPDki 99
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKST----IANLL-TRFYDIDEGEILLDGHDLrDYTLAS-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VRRGIFQVMEGRRIVSDmTSLENLrlgAFTRSDREVGRDIE----MVY--NYFPRLKErtGL-------AGYLSGGEQQM 166
Cdd:PRK11176 415 LRNQVALVSQNVHLFND-TIANNI---AYARTEQYSREQIEeaarMAYamDFINKMDN--GLdtvigenGVLLSGGQRQR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501488905 167 LAIGRALMARPKMILMDEPSMGL---SPLLVKEVFAIIQQiNRdlgvTILLVE------QNARAALsVASHGYIMEQG 235
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALdteSERAIQAALDELQK-NR----TSLVIAhrlstiEKADEIL-VVEDGEIVERG 560
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
26-217 |
4.24e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.98 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 26 NIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT---RGEIVFDGER---IDGTDPDKI 99
Cdd:TIGR00954 456 NIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTkpaKGKLFYVPQRpymTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VR-RGIFQVMegRRIVSD---MTSLENLRLGAFTRsdREVGRDIemVYNYfprlkertglAGYLSGGEQQMLAIGRALMA 175
Cdd:TIGR00954 536 IYpDSSEDMK--RRGLSDkdlEQILDNVQLTHILE--REGGWSA--VQDW----------MDVLSGGEKQRIAMARLFYH 599
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501488905 176 RPKMILMDEPSMGLSPllvkEVFAIIQQINRDLGVTILLVEQ 217
Cdd:TIGR00954 600 KPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-186 |
1.39e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 18 PAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGeivfdgeridgtdpd 97
Cdd:PRK10636 309 PNPLLKMEKVSAGYGDRI-ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA--------------- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 98 KIVRRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVgRDIEMVYNYfpRLKERTGLAGYLSGGEQQMLAIGRALMARP 177
Cdd:PRK10636 373 KGIKLGYFAQHQLEFLRADESPLQHLARLAPQELEQKL-RDYLGGFGF--QGDKVTEETRRFSGGEKARLVLALIVWQRP 449
|
....*....
gi 501488905 178 KMILMDEPS 186
Cdd:PRK10636 450 NLLLLDEPT 458
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-245 |
1.93e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 41 LSLDVPQGAIVALLGANGAGKSTTLKAISGLLkteDGEvtrGEIVFDGERIDG-TDPDKIVRRGIF--QVmegrRIVSDM 117
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL---PGS---GSIQFAGQPLEAwSAAELARHRAYLsqQQ----TPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLgafTRSDREVGRDIEMVYNYfprLKERTGL-------AGYLSGGEQQ-------MLAIGRALMARPKMILMD 183
Cdd:PRK03695 85 PVFQYLTL---HQPDKTRTEAVASALNE---VAEALGLddklgrsVNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501488905 184 EPSmglSPLLVKEVFAIIQQINR--DLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADE 245
Cdd:PRK03695 159 EPM---NSLDVAQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
38-190 |
2.83e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEvtrGEIVFDGERIDGTDPDKIVRRGIFQVMEGRRIVSDM 117
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYE---GEILFDGEVCRFKDIRDSEALGIVIIHQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLGaftrsdREVGR----DIEMVYNYFPRLKERTGLA-------GYLSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:NF040905 94 SIAENIFLG------NERAKrgviDWNETNRRARELLAKVGLDespdtlvTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
....
gi 501488905 187 MGLS 190
Cdd:NF040905 168 AALN 171
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
159-251 |
2.91e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 LSGGEQQMLAIGRALMARPKMI--LMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNARaALSVASH------GY 230
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQ-MISLADRiidigpGA 554
|
90 100
....*....|....*....|.
gi 501488905 231 IMEQGKVVLDGTADELRDNED 251
Cdd:PRK00635 555 GIFGGEVLFNGSPREFLAKSD 575
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-195 |
3.47e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 3 EAAElhPPQPGASTAPAPLLSVRNIEVVYDDVIlVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISG-----------L 71
Cdd:PRK10938 244 EPDE--PSARHALPANEPRIVLNNGVVSYNDRP-ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltL 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 72 LKTEDGEvtrGEIVFDgeridgtdpdkiVRRGIFQV-----MEGRriVSdmTSLENLRLGAF--------TRSDREvgRD 138
Cdd:PRK10938 321 FGRRRGS---GETIWD------------IKKHIGYVssslhLDYR--VS--TSVRNVILSGFfdsigiyqAVSDRQ--QK 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501488905 139 IEMVYNYFPRLKERTGLAGY--LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPL---LVK 195
Cdd:PRK10938 380 LAQQWLDILGIDKRTADAPFhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLnrqLVR 441
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-189 |
3.55e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 82 GEIVFDGerIDGTDPDKIVRRGIFQVMEGRRIVSDMTSLENLRLGAFTRSDREVGR-----DIEMVYNYFPRlKERTGLA 156
Cdd:PTZ00265 1277 GKILLDG--VDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRackfaAIDEFIESLPN-KYDTNVG 1353
|
90 100 110
....*....|....*....|....*....|....*.
gi 501488905 157 GY---LSGGEQQMLAIGRALMARPKMILMDEPSMGL 189
Cdd:PTZ00265 1354 PYgksLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-228 |
4.07e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDPDKIVRRGIFQVMEGRRIVSD 116
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY----------YKNCNINNIAKPYCTYIGHNLGLKLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLENLRLGAftrsdrEVGRDIEMVY---NYFpRLKERTGLAGY-LSGGEQQMLAIGRALMARPKMILMDEPSMGLSpl 192
Cdd:PRK13541 85 MTVFENLKFWS------EIYNSAETLYaaiHYF-KLHDLLDEKCYsLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-- 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 501488905 193 lvKEvfaiiqqiNRDLGVTILLVEQNARAALSVASH 228
Cdd:PRK13541 156 --KE--------NRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-185 |
1.00e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 24 VRNIEVVYDDVILVlRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRG---EIV-FDGERIDgTDPDKI 99
Cdd:PRK11147 322 MENVNYQIDGKQLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtklEVAyFDQHRAE-LDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 100 VrrgifqvmegrrivsdmtsLENLRLGaftRSDREV-GRDiEMVYNY-----FPRLKERTGLAGyLSGGEQQMLAIGRAL 173
Cdd:PRK11147 400 V-------------------MDNLAEG---KQEVMVnGRP-RHVLGYlqdflFHPKRAMTPVKA-LSGGERNRLLLARLF 455
|
170
....*....|..
gi 501488905 174 MARPKMILMDEP 185
Cdd:PRK11147 456 LKPSNLLILDEP 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-185 |
1.41e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 22 LSVRNIEVVYDDVILvLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEIVFDGERIDGTDPDkivr 101
Cdd:PRK15064 320 LEVENLTKGFDNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAYD---- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 102 rgiFQvmegrrivSDMTSLEnlrlgaFTRSDREVGRDIEMVYNYFPRL----KERTGLAGYLSGGEQQMLAIGRALMARP 177
Cdd:PRK15064 395 ---FE--------NDLTLFD------WMSQWRQEGDDEQAVRGTLGRLlfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
....*...
gi 501488905 178 KMILMDEP 185
Cdd:PRK15064 458 NVLVMDEP 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
51-185 |
3.28e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 51 VALLGANGAGKSTTLKAISGLLKTEDGEvtrgeIVFDGE----RIDgTDPDKIVRRGIFQ-VMEGRRIVSDMtsLEN--- 122
Cdd:PRK11147 32 VCLVGRNGAGKSTLMKILNGEVLLDDGR-----IIYEQDlivaRLQ-QDPPRNVEGTVYDfVAEGIEEQAEY--LKRyhd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 123 -LRLGAFTRSDREVGR--------DIEMVYNYFPRLKERTGLAGY--------LSGGEQQMLAIGRALMARPKMILMDEP 185
Cdd:PRK11147 104 iSHLVETDPSEKNLNElaklqeqlDHHNLWQLENRINEVLAQLGLdpdaalssLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-198 |
3.84e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 8 HPP-QPGAstapaPLLSVRNIEVVYDDVIL--VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLK-TEDGEVT-RG 82
Cdd:PLN03232 605 NPPlQPGA-----PAISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVViRG 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 83 EIVFdgeridgtdpdkivrrgIFQVmegrRIVSDMTSLENLRLGAFTRSDReVGRDIEMV-----YNYFP-RLKERTGLA 156
Cdd:PLN03232 680 SVAY-----------------VPQV----SWIFNATVRENILFGSDFESER-YWRAIDVTalqhdLDLLPgRDLTEIGER 737
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 501488905 157 GY-LSGGEQQMLAIGRALMARPKMILMDEPSMGLSPLLVKEVF 198
Cdd:PLN03232 738 GVnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
37-189 |
3.86e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.95 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKtedGEVTRGEIVFDGERIdgtdPDKIVRRGIFqVMEGRRIVSD 116
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQ---GNNFTGTILANNRKP----TKQILKRTGF-VTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 117 MTSLENLRLGAFTRSDREVGRDI-----EMVYNYFPRLKERTGLAGY-----LSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:PLN03211 155 LTVRETLVFCSLLRLPKSLTKQEkilvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
...
gi 501488905 187 MGL 189
Cdd:PLN03211 235 SGL 237
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
38-218 |
3.98e-06 |
|
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: 46.16 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAisGLLKTEDGEVTRGEIVFDgeridgtdPDKIVRrgifqvmegrriVSDM 117
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE--GLYASGKARLISFLPKFS--------RNKLIF------------IDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 118 TSLENLRLGAFTrsdreVGRDiemvynyfprlkertglAGYLSGGEQQMLAIGRALMARPK--MILMDEPSMGLSPllvK 195
Cdd:cd03238 69 QFLIDVGLGYLT-----LGQK-----------------LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ---Q 123
|
170 180
....*....|....*....|....*
gi 501488905 196 EVFAIIQQINR--DLGVTILLVEQN 218
Cdd:cd03238 124 DINQLLEVIKGliDLGNTVILIEHN 148
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-202 |
6.80e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 19 APLLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGE----IVFDGERIDGT 94
Cdd:PLN03073 506 PPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkvrmAVFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 95 D----PDKIVRRGIFQVMEGRrivsdmtslenLR--LGAFTRSDREVgrdIEMVYNyfprlkertglagyLSGGEQQMLA 168
Cdd:PLN03073 586 DlssnPLLYMMRCFPGVPEQK-----------LRahLGSFGVTGNLA---LQPMYT--------------LSGGQKSRVA 637
|
170 180 190
....*....|....*....|....*....|....
gi 501488905 169 IGRALMARPKMILMDEPSMGLSpllVKEVFAIIQ 202
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLD---LDAVEALIQ 668
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-201 |
1.10e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 2 TEAAelHPPQPGASTAPAPLLSVRNIEVVYDDVI-LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLktedgEVT 80
Cdd:PTZ00243 1291 IEPA--SPTSAAPHPVQAGSLVFEGVQMRYREGLpLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMV-----EVC 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 RGEIVFDGERIdgtdpdkivrrGIFQVMEGRRIVS---------DMTSLENLR--LGAftrSDREVGRDIEMVynyfpRL 149
Cdd:PTZ00243 1364 GGEIRVNGREI-----------GAYGLRELRRQFSmipqdpvlfDGTVRQNVDpfLEA---SSAEVWAALELV-----GL 1424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 150 KERT-------------GLAGYlSGGEQQMLAIGRALMAR-PKMILMDEPSMGLSPLLVKEVFAII 201
Cdd:PTZ00243 1425 RERVasesegidsrvleGGSNY-SVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATV 1489
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-250 |
1.62e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 31 YDDVIL--------VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTrgeivfdgerIDGTDPDKivrr 102
Cdd:PLN03232 1237 FEDVHLryrpglppVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM----------IDDCDVAK---- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 103 giFQVMEGRRIVSDM-------TSLENLRLGAFTR-SDREVGRDIEMVY-------NYFPRLKERTGLAGYLSGGEQQML 167
Cdd:PLN03232 1303 --FGLTDLRRVLSIIpqspvlfSGTVRFNIDPFSEhNDADLWEALERAHikdvidrNPFGLDAEVSEGGENFSVGQRQLL 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 168 AIGRALMARPKMILMDEPSMGLSpllvKEVFAIIQQINRD--LGVTILLVEQNARAALSvASHGYIMEQGKVVLDGTADE 245
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVD----VRTDSLIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQE 1455
|
....*
gi 501488905 246 LRDNE 250
Cdd:PLN03232 1456 LLSRD 1460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-184 |
1.98e-05 |
|
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: 46.09 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 12 PGASTAPAPLLSVRNIEVVY-DDVILVLRGLSLDVPQGAIVALLGANGAGKST-TLkaisGLLKTEdgEVTRGEIvfdge 89
Cdd:TIGR00957 1275 PPSGWPPRGRVEFRNYCLRYrEDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSlTL----GLFRIN--ESAEGEI----- 1343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 90 RIDGTDPDKI----VRRGIFQVMEGRRIVSDmtSLEnLRLGAFTR-SDREVGRDIEMVY-----NYFP-RLKERTGLAGY 158
Cdd:TIGR00957 1344 IIDGLNIAKIglhdLRFKITIIPQDPVLFSG--SLR-MNLDPFSQySDEEVWWALELAHlktfvSALPdKLDHECAEGGE 1420
|
170 180
....*....|....*....|....*..
gi 501488905 159 -LSGGEQQMLAIGRALMARPKMILMDE 184
Cdd:TIGR00957 1421 nLSVGQRQLVCLARALLRKTKILVLDE 1447
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
37-203 |
2.20e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKsTTLkAISGLLKTEdGEVTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRR---- 112
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGR-TEL-AMSVFGRSY-GRNISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRKgygl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVSD----MTSLENLRlgafTRSDREV---GRDIEMVYNYFPRLKERTG----LAGYLSGGEQQMLAIGRALMARPKMIL 181
Cdd:NF040905 352 NLIDdikrNITLANLG----KVSRRGVideNEEIKVAEEYRKKMNIKTPsvfqKVGNLSGGNQQKVVLSKWLFTDPDVLI 427
|
170 180
....*....|....*....|..
gi 501488905 182 MDEPSMGLSPLLVKEVFAIIQQ 203
Cdd:NF040905 428 LDEPTRGIDVGAKYEIYTIINE 449
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
156-259 |
2.38e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.39 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 156 AGYLSGGEQQMLA----IGRALMArpKMILMDEPSMGLSPllvKEVFAIIQQIN--RDLGVTILLVEQNARaALSVASH- 228
Cdd:TIGR00630 486 AGTLSGGEAQRIRlatqIGSGLTG--VLYVLDEPSIGLHQ---RDNRRLINTLKrlRDLGNTLIVVEHDED-TIRAADYv 559
|
90 100 110
....*....|....*....|....*....|....*..
gi 501488905 229 -----GYIMEQGKVVLDGTADELRDNED-VKEFYLGG 259
Cdd:TIGR00630 560 idigpGAGEHGGEVVASGTPEEILANPDsLTGQYLSG 596
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-198 |
3.03e-05 |
|
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: 45.32 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVT-RGEIVFDGERIdGTDPDKIVRRGIF----------Q 106
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHmKGSVAYVPQQA-WIQNDSLRENILFgkalnekyyqQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 107 VMEGRRIVSDmtsLENLRLGAFTrsdrEVGrdiEMVYNyfprlkertglagyLSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:TIGR00957 733 VLEACALLPD---LEILPSGDRT----EIG---EKGVN--------------LSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170
....*....|..
gi 501488905 187 MGLSPLLVKEVF 198
Cdd:TIGR00957 789 SAVDAHVGKHIF 800
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
42-216 |
3.19e-05 |
|
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: 45.16 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 42 SLDVPQ-GAIVALLGANGAGKSTTLKAISGLLKTEDGEVTR-------------------------GEI----------- 84
Cdd:COG1245 92 GLPVPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEepswdevlkrfrgtelqdyfkklanGEIkvahkpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 85 ---VFDG---ERIDGTDpdkivRRGIFqvmegrRIVSDMTSLENLRlgaftrsDREVgrdiemvynyfprlkertglaGY 158
Cdd:COG1245 172 ipkVFKGtvrELLEKVD-----ERGKL------DELAEKLGLENIL-------DRDI---------------------SE 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 159 LSGGEQQMLAIGRALMARPKMILMDEPSmglSPLLVKE---VFAIIQQINRDlGVTILLVE 216
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPS---SYLDIYQrlnVARLIRELAEE-GKYVLVVE 269
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-185 |
4.55e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTRGEivfdGERIdG-------TDPDKIVRRgifQVME 109
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP----GIKV-GylpqepqLDPEKTVRE---NVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 110 GRRIVSD-------------------------MTSLENL--RLGAFtrsdrEVGRDIEMVYNYFpRLKERTGLAGYLSGG 162
Cdd:PRK11819 94 GVAEVKAaldrfneiyaayaepdadfdalaaeQGELQEIidAADAW-----DLDSQLEIAMDAL-RCPPWDAKVTKLSGG 167
|
170 180
....*....|....*....|...
gi 501488905 163 EQQMLAIGRALMARPKMILMDEP 185
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEP 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
37-198 |
5.43e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 37 VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEVTR-GEIVFDGER---IDGTDPDKIvrrgIFQVmegrr 112
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHsGRISFSPQTswiMPGTIKDNI----IFGL----- 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 ivsdmtSLENLRLGAFTRSdREVGRDIEMvynyFPRlKERTGLAG---YLSGGEQQMLAIGRALMARPKMILMDEPSMGL 189
Cdd:TIGR01271 512 ------SYDEYRYTSVIKA-CQLEEDIAL----FPE-KDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
....*....
gi 501488905 190 SPLLVKEVF 198
Cdd:TIGR01271 580 DVVTEKEIF 588
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
38-216 |
6.29e-05 |
|
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: 43.02 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKST----TLKA---------ISGLLKTEDGEVTRGEIvfdgERIDGTDPdkivrrgi 104
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlafdTIYAegqrryvesLSAYARQFLGQMDKPDV----DSIEGLSP-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 105 fqvmegrrivsdMTSLENLRLGAFTRSdrEVGRDIEmVYNYFPRLKERTGL--------------------AGYLSGGEQ 164
Cdd:cd03270 79 ------------AIAIDQKTTSRNPRS--TVGTVTE-IYDYLRLLFARVGIrerlgflvdvglgyltlsrsAPTLSGGEA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501488905 165 QMLA----IGRALMArpKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVE 216
Cdd:cd03270 144 QRIRlatqIGSGLTG--VLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVE 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-186 |
7.46e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 6 ELHPPQPGAStapapllsvRNIEVVYDDVILVLRGLSLDVPQGAI-----VALLGANGAGKSTTLKAISGLLKTEDGEVT 80
Cdd:PRK13409 327 EERPPRDESE---------RETLVEYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 RGEIVfdgeridGTDPDKIvrrgifqvmegrRIVSDMTSLENLrlgaftrsdREVGRDIEMVYnYFPRLKERTGLA---- 156
Cdd:PRK13409 398 PELKI-------SYKPQYI------------KPDYDGTVEDLL---------RSITDDLGSSY-YKSEIIKPLQLErlld 448
|
170 180 190
....*....|....*....|....*....|...
gi 501488905 157 ---GYLSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:PRK13409 449 knvKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-216 |
7.87e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 42 SLDVPQ-GAIVALLGANGAGKSTTLKAISGLLK----TEDGEVTRGEIV--FDG-------------------------- 88
Cdd:PRK13409 92 GLPIPKeGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWDEVLkrFRGtelqnyfkklyngeikvvhkpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 89 --ERIDGTDPD---KIVRRGIFqvmegrRIVSDMTSLENLrlgaftrsdreVGRDIEmvynyfprlkertglagYLSGGE 163
Cdd:PRK13409 172 ipKVFKGKVREllkKVDERGKL------DEVVERLGLENI-----------LDRDIS-----------------ELSGGE 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501488905 164 QQMLAIGRALMARPKMILMDEPSmglSPLLVKEVFAIIQQInRDL--GVTILLVE 216
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPT---SYLDIRQRLNVARLI-RELaeGKYVLVVE 268
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
38-204 |
8.05e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 8.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGaIVALLGANGAGKSTTLKAISGLL--------------KTEDGEVTRGEIVFD---------GERIDGT 94
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLgpsssrkfdeedfyLGDDPDLPEIEIELTfgsllsrllRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 95 DPDKI----------VRRGIFQVMEG-RRIVSDMTSLENLRLGAFTRSDREVGRDIEMVYNYFPRLKERtglagYLSGGE 163
Cdd:COG3593 93 DKEELeealeelneeLKEALKALNELlSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLD-----RLGSGF 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501488905 164 QQM--LAIGRALM-----ARPKMILMDEPSMGLSPLLVKEVFAIIQQI 204
Cdd:COG3593 168 QRLilLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKEL 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-97 |
1.03e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.42 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 6 ELHPPQPGASTAPAP----LLSVRNIEVVYDDVILVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDgevtr 81
Cdd:PRK10522 303 ALAPYKAEFPRPQAFpdwqTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS----- 377
|
90
....*....|....*.
gi 501488905 82 GEIVFDGERIDGTDPD 97
Cdd:PRK10522 378 GEILLDGKPVTAEQPE 393
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-186 |
1.06e-04 |
|
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: 43.23 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 6 ELHPPQPGASTAPApllsvrnieVVYDDVILVLRGLSLDVPQGAI-----VALLGANGAGKSTTLKAISGLLKTEDGEVT 80
Cdd:COG1245 328 EVHAPRREKEEETL---------VEYPDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 81 RG-EIVFDGERIdgtDPDkivrrgifqvmegrrivSDMTSLENLRlgaftrsdREVGRDIEMVYnYFPRLKERTGL---- 155
Cdd:COG1245 399 EDlKISYKPQYI---SPD-----------------YDGTVEEFLR--------SANTDDFGSSY-YKTEIIKPLGLekll 449
|
170 180 190
....*....|....*....|....*....|....
gi 501488905 156 ---AGYLSGGEQQMLAIGRALMARPKMILMDEPS 186
Cdd:COG1245 450 dknVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
38-249 |
1.06e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKT-EDGEVT-RGEIVFDGER---IDGTDPDKIVRRGIFQVMEGRR 112
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVViRGTVAYVPQVswiFNATVRDNILFGSPFDPERYER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 113 IVsDMTSLE-NLRL---GAFTrsdrEVGrdiemvynyfprlkERtGLAgyLSGGEQQMLAIGRALMARPKMILMDEPSMG 188
Cdd:PLN03130 713 AI-DVTALQhDLDLlpgGDLT----EIG--------------ER-GVN--ISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501488905 189 LSPLLVKEVFAiiQQINRDLGVTILLVEQNARAALSVASHGYIMEQGKVVLDGTADELRDN 249
Cdd:PLN03130 771 LDAHVGRQVFD--KCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
120-251 |
4.71e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 120 LENLRLgafTRSDREVGRDIemvynyfprLKE---------RTGL--------AGYLSGGEQQ--MLA--IGRALMArpk 178
Cdd:COG0178 442 FENLEL---TEREAEIAERI---------LKEirsrlgflvDVGLdyltldrsAGTLSGGEAQriRLAtqIGSGLVG--- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 179 mIL--MDEPSMGLSP-----LLvkevfAIIQQInRDLGVTILLVEQNA---RAALSV------A-SHGyimeqGKVVLDG 241
Cdd:COG0178 507 -VLyvLDEPSIGLHQrdndrLI-----ETLKRL-RDLGNTVIVVEHDEdtiRAADYIidigpgAgEHG-----GEVVAQG 574
|
170
....*....|
gi 501488905 242 TADELRDNED 251
Cdd:COG0178 575 TPEEILKNPD 584
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
47-215 |
6.05e-04 |
|
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: 39.28 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 47 QGAIVALLGANGAGKSTTLKAISGLLKTEDGEVtrgeIVFDGERIDGTDPDKIvrrgifqvmegrrivsdmtslenlrlg 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV----IYIDGEDILEEVLDQL--------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 127 aftrsdrevgrdiemvynyfpRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDEPSMGLSP-----LLVKEVFAII 201
Cdd:smart00382 50 ---------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAeqealLLLLEELRLL 108
|
170
....*....|....
gi 501488905 202 QQINRDLGVTILLV 215
Cdd:smart00382 109 LLLKSEKNLTVILT 122
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
12-79 |
6.49e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 6.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501488905 12 PGASTAPAPLLSVRNIEVVYDDVI-----LVLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV 79
Cdd:PTZ00243 645 GGHEATPTSERSAKTPKMKTDDFFelepkVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV 717
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
159-246 |
1.77e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 159 LSGGEQQMLAIGRALMAR---PKMILMDEPSMGLSPLLVKEVFAIIQQInRDLGVTILLVEQNaraaLSV-ASHGYIME- 233
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIEHN----LDViKTADYIIDl 904
|
90 100
....*....|....*....|
gi 501488905 234 -------QGKVVLDGTADEL 246
Cdd:TIGR00630 905 gpeggdgGGTVVASGTPEEV 924
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
156-250 |
2.11e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 156 AGYLSGGEQQMLAIGRALMARPKMILMDEPSmglSPLLVKEVFAIIQQINRDLG----VTILLVEQ-------NARAALS 224
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEAT---SSLDNKSEYLVQKTINNLKGnenrITIIIAHRlstiryaNTIFVLS 653
|
90 100
....*....|....*....|....*.
gi 501488905 225 VASHGYIMEQGKVVLDGTADELRDNE 250
Cdd:PTZ00265 654 NRERGSTVDVDIIGEDPTKDNKENNN 679
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-184 |
2.59e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.34 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 6 ELHPPQPGASTAPApllsvrnieVVYDDVIL--------VLRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDG 77
Cdd:PLN03130 1224 ENNRPPPGWPSSGS---------IKFEDVVLryrpelppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERG 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 78 EVTrgeivfdgerIDGTDPDKivrrgiFQVMEGRRIVSDMTSLENL-------RLGAFTR-SDREVGRDIEMVY------ 143
Cdd:PLN03130 1295 RIL----------IDGCDISK------FGLMDLRKVLGIIPQAPVLfsgtvrfNLDPFNEhNDADLWESLERAHlkdvir 1358
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 501488905 144 -NYFPRLKERTGLAGYLSGGEQQMLAIGRALMARPKMILMDE 184
Cdd:PLN03130 1359 rNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-79 |
3.96e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.33 E-value: 3.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 501488905 38 LRGLSLDVPQGAIVALLGANGAGKSTTLKAISGLLKTEDGEV 79
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
50-143 |
7.04e-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: 37.37 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501488905 50 IVALLGANGAGKSTTLKAISGLLKTE-------DGEVTRGEIVFDGERIDGTDPDKIVRRGIFQVMEGRRIVSDMTSLEN 122
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDalvigltDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYGLDLER 80
|
90 100
....*....|....*....|.
gi 501488905 123 LRLGAFTRSDREVGRDIEMVY 143
Cdd:pfam13304 81 EDVEEKLSSKPTLLEKRLLLR 101
|
|
| |
