|
Name |
Accession |
Description |
Interval |
E-value |
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-216 |
1.50e-48 |
|
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: 160.79 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPE 82
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDLPS-VSLNDYYRSLCKFYPNFSE---KDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTN 156
Cdd:COG4555 82 ERGLYDrLTVRENIRYFAELYGLFDEelkKRIEELIELLGLEefLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 157 GLDIASKNVFRDIISNFKN--KIVFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINNSY 216
Cdd:COG4555 162 GLDVMARRLLREILRALKKegKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-203 |
2.91e-38 |
|
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: 132.14 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPE 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDlpsvslndyyrslckFYPNFSEKDfkeyllkfeidiNLKFgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIAS 162
Cdd:cd03230 81 EPS---------------LYENLTVRE------------NLKL---SGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500096509 163 KNVFRDIISNFK--NKIVFVTGHNVRDLVDIVDHLTIIGNNNI 203
Cdd:cd03230 131 RREFWELLRELKkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-210 |
3.46e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.64 E-value: 3.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPE 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDLP---SVSLN-DYYRSLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTN 156
Cdd:COG1131 81 EPALYpdlTVRENlRFFARLYGLPRKEARERIDELLELFGLTdaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 157 GLDIASKNVFRDIISNFK--NKIVFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVS 210
Cdd:COG1131 161 GLDPEARRELWELLRELAaeGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPD 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-206 |
2.84e-28 |
|
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: 107.28 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSkPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfPRNPLNLVNLF-FVP 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIgYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 82 EEFDlpsvslndyyrslckFYPNFSEKDFKEYL----------LKFEID-----INL------KFGSSSYGQRKKSIIAF 140
Cdd:cd03264 79 QEFG---------------VYPNFTVREFLDYIawlkgipskeVKARVDevlelVNLgdrakkKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 141 SLATDVPILIFDEPTNGLDIASKNVFRDIISNF-KNKIVFVTGHNVRDLVDIVDHLTIIGNNNILFS 206
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-207 |
3.94e-27 |
|
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: 104.54 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 4 EFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVlfnslKVFPRNPLNLVNLF-FVPE 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----RVFGKPLEKERKRIgYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 ----EFDLP-----SVSLNDYYRslCKFYPNFSEKDFK--EYLLK----FEIdINLKFGSSSYGQRKKSIIAFSLATDVP 147
Cdd:cd03235 76 rrsiDRDFPisvrdVVLMGLYGH--KGLFRRLSKADKAkvDEALErvglSEL-ADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 148 ILIFDEPTNGLDIASKNVFRDIIS--NFKNKIVFVTGHNVRDLVDIVDHLTIIgNNNILFSN 207
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRelRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-200 |
1.69e-26 |
|
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: 101.17 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 4 EFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVpeE 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 84 FDLpsvslndyyrslckfypnfsekdfkeyllkfeidinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK 163
Cdd:cd00267 79 PQL------------------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASR 116
|
170 180 190
....*....|....*....|....*....|....*....
gi 500096509 164 NVFRDIISNF--KNKIVFVTGHNVRDLVDIVDHLTIIGN 200
Cdd:cd00267 117 ERLLELLRELaeEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-183 |
1.69e-26 |
|
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: 102.56 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFV 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDL-PSVSLNDYYRSLCKFYP-NFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTN 156
Cdd:COG4133 81 GHADGLkPELTVRENLRFWAALYGlRADREAIDEALEAVGLAglADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180
....*....|....*....|....*....
gi 500096509 157 GLDIASKNVFRDIISNFKNK--IVFVTGH 183
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARggAVLLTTH 189
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-200 |
1.82e-25 |
|
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: 99.85 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 4 EFIDVSFSYRKIKVYL--DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-------SLKVFPR----- 69
Cdd:cd03225 1 ELKNLSFSYPDGARPAldDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklSLKELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 70 --NP-LNLVN------LFFVPEEFDLPSVSLNDYYRSLCKFypnFSEKDFKEYLLKfeidiNLkfgssSYGQRKKSIIAF 140
Cdd:cd03225 81 fqNPdDQFFGptveeeVAFGLENLGLPEEEIEERVEEALEL---VGLEGLRDRSPF-----TL-----SGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500096509 141 SLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLTIIGN 200
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVT-HDLDLLLELADRVIVLED 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-205 |
4.96e-25 |
|
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: 99.33 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN----- 76
Cdd:COG1122 1 IELENLSFSYPGGTPALdDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRkvglv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 -------LF---------FVPEEFDLP-------------SVSLNDYyrslckfypnfseKDFKEYLLkfeidinlkfgs 127
Cdd:COG1122 81 fqnpddqLFaptveedvaFGPENLGLPreeirerveealeLVGLEHL-------------ADRPPHEL------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 128 sSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:COG1122 136 -SGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVT-HDLDLVAELADRVIVLDDGRIV 213
|
.
gi 500096509 205 F 205
Cdd:COG1122 214 A 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-210 |
9.40e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.01 E-value: 9.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKvfPRNPLNLVNlfFVP- 81
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP--PRRARRRIG--YVPq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 82 -EEFD--LPS-----VSLNDYYRSlcKFYPNFSEKDFK---EYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPI 148
Cdd:COG1121 83 rAEVDwdFPItvrdvVLMGRYGRR--GLFRRPSRADREavdEALERVGLEdlADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500096509 149 LIFDEPTNGLDIASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLTIIgNNNILFSNSVS 210
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRREgktILVVT-HDLGAVREYFDRVLLL-NRGLVAHGPPE 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-198 |
3.86e-24 |
|
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: 97.46 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGevlfNSLKVFPRnPLNLVNLF---- 78
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLFGE-RRGGEDVWelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 ---FVpeefdlpSVSLNDYYRSLCK--------------FYPNFSEKDFK--EYLLK-FEID--INLKFGSSSYGQRKKS 136
Cdd:COG1119 79 rigLV-------SPALQLRFPRDETvldvvlsgffdsigLYREPTDEQREraRELLElLGLAhlADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 137 IIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK----IVFVTgHNVRDLVDIVDHLTII 198
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVT-HHVEEIPPGITHVLLL 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-205 |
1.52e-23 |
|
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: 95.65 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN------ 76
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 -LFFVPEEFDLPSVS------LNDYYRslckfypnFSEKDFKEY-LLKFEI-----DINLKFGSSSYGQRKKSIIAFSLA 143
Cdd:cd03261 81 mLFQSGALFDSLTVFenvafpLREHTR--------LSEEEIREIvLEKLEAvglrgAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 144 TDVPILIFDEPTNGLDIASKNVFRDIISNFKNK----IVFVTgHNVRDLVDIVDHLTIIGNNNILF 205
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElgltSIMVT-HDLDTAFAIADRIAVLYDGKIVA 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-204 |
2.49e-23 |
|
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: 93.27 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLF-FVP---E 82
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIaYVPqalE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDLpsvslndyyrslckfyPNFSEKDFKEyLlkfeidinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIAS 162
Cdd:cd03214 84 LLGL----------------AHLADRPFNE-L--------------SGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500096509 163 KNVFRDIISNF---KNKIVFVTGHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:cd03214 133 QIELLELLRRLareRGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-200 |
3.05e-23 |
|
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: 93.02 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSlkvfprNPLNLVNLFFVPE 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG------EDLTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDLPSVslndyYRSLCKFyPNFSEKDfkeyllkfeidiNLKFGSSSyGQRKKSIIAFSLATDVPILIFDEPTNGLDIAS 162
Cdd:cd03229 75 RRRIGMV-----FQDFALF-PHLTVLE------------NIALGLSG-GQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500096509 163 KNVFRDIISNFKNK----IVFVTgHNVRDLVDIVDHLTIIGN 200
Cdd:cd03229 136 RREVRALLKSLQAQlgitVVLVT-HDLDEAARLADRVVVLRD 176
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-206 |
1.23e-21 |
|
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: 89.58 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVF-PRNPLNLVNlffvp 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkNIEALRRIG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 82 eefdlpsvSLNDYYrslcKFYPNFSEKDFKEYLLKF------EID-----INL------KFGSSSYGQRKKSIIAFSLAT 144
Cdd:cd03268 76 --------ALIEAP----GFYPNLTARENLRLLARLlgirkkRIDevldvVGLkdsakkKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500096509 145 DVPILIFDEPTNGLDIASKNVFRDIISNFKN--KIVFVTGHNVRDLVDIVDHLTIIGNNNILFS 206
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDqgITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-205 |
5.53e-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: 88.54 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 12 YRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPEE-----FDL 86
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQktqlwWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 87 PSVslnDYYRSLCKFYpNFSEKDFKEY------LLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDI 160
Cdd:cd03267 111 PVI---DSFYLLAAIY-DLPPARFKKRldelseLLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 500096509 161 ASKNVFRDIISNF---KNKIVFVTGHNVRDLVDIVDHLTIIGNNNILF 205
Cdd:cd03267 187 VAQENIRNFLKEYnreRGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-203 |
1.16e-20 |
|
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: 86.93 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 6 IDVSFSYRK-IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVnlFFVPEEF 84
Cdd:cd03226 3 ENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI--GYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 85 D--LPSVS-LNDYYRSLcKFYPNfSEKDFKEYLLKFEIDInLKFG---SSSYGQRKKSIIAFSLATDVPILIFDEPTNGL 158
Cdd:cd03226 81 DyqLFTDSvREELLLGL-KELDA-GNEQAETVLKDLDLYA-LKERhplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500096509 159 DIASK----NVFRDIISnfKNKIVFVTGHNVRDLVDIVDHLTIIGNNNI 203
Cdd:cd03226 158 DYKNMervgELIRELAA--QGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-156 |
1.61e-20 |
|
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: 85.01 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNL-VNLFFVPEE-FDLPSVSL--NDYY 95
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYVFQDpQLFPRLTVreNLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 96 RSLCKFYPNF-SEKDFKEYLLKFEID------INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTN 156
Cdd:pfam00005 83 GLLLKGLSKReKDARAEEALEKLGLGdladrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-194 |
5.85e-20 |
|
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: 84.36 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPLNLvNLF 78
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDgvDLRDLDLESLRK-NIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDLPSVSLndyyrslckfypnfsekdfKEYLLkfeidinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGL 158
Cdd:cd03228 80 YVPQDPFLFSGTI-------------------RENIL-------------SGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190
....*....|....*....|....*....|....*..
gi 500096509 159 DIASKNVFRDIISNF-KNKIVFVTGHNVrDLVDIVDH 194
Cdd:cd03228 128 DPETEALILEALRALaKGKTVIVIAHRL-STIRDADR 163
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-188 |
8.31e-20 |
|
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: 85.87 E-value: 8.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-------SLKVFPRnplnlv 75
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslSRRELAR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 NLFFVPEEFDLPS-------VSLNDY-YRSlckFYPNFSEKDFK---EYLLKFEIDiNLK---FGSSSYGQRKKSIIAFS 141
Cdd:COG1120 76 RIAYVPQEPPAPFgltvrelVALGRYpHLG---LFGRPSAEDREaveEALERTGLE-HLAdrpVDELSGGERQRVLIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500096509 142 LATDVPILIFDEPTNGLDIASK----NVFRDiISNFKNKIVFVTGHnvrDL 188
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQlevlELLRR-LARERGRTVVMVLH---DL 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-219 |
1.57e-19 |
|
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: 84.52 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 11 SYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-----SLKVFPRNPLNLVNLffvPEEfd 85
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditKLPMHKRARLGIGYL---PQE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 86 lPSVslndyYRSLC----------KFYPNFSEKDFK-EYLLK-FEID-INLKFGSS-SYGQRKKSIIAFSLATDVPILIF 151
Cdd:cd03218 84 -ASI-----FRKLTveenilavleIRGLSKKEREEKlEELLEeFHIThLRKSKASSlSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 152 DEPTNGLD-IASKNVfRDIISNFKNK-I-VFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINNSYKVK 219
Cdd:cd03218 158 DEPFAGVDpIAVQDI-QKIIKILKDRgIgVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-215 |
1.90e-19 |
|
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: 84.65 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEV----------------------- 59
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlvdgqditglsekelyelrrrig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 60 -------LFNSLKVFpRN---PLNlvnlffvpEEFDLP-------------SVSLndyyRSLCKFYPNfsekdfkeyllk 116
Cdd:COG1127 86 mlfqggaLFDSLTVF-ENvafPLR--------EHTDLSeaeirelvlekleLVGL----PGAADKMPS------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 117 fEIdinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK----IVFVTgHNVRDLVDIV 192
Cdd:COG1127 141 -EL---------SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElgltSVVVT-HDLDSAFAIA 209
|
250 260
....*....|....*....|...
gi 500096509 193 DHLTIIGNNNILFSNSVSYINNS 215
Cdd:COG1127 210 DRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
33-206 |
2.96e-19 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 83.57 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFpRNPLN-LVNLFFVPEEFDL-PSVSLND---YYRSLCKFYPNFSE 107
Cdd:cd03266 36 LLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV-KEPAEaRRRLGFVSDSTGLyDRLTAREnleYFAGLYGLKGDELT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 108 KDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKN--KIVFVTGH 183
Cdd:cd03266 115 ARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgKCILFSTH 194
|
170 180
....*....|....*....|...
gi 500096509 184 NVRDLVDIVDHLTIIGNNNILFS 206
Cdd:cd03266 195 IMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-198 |
1.04e-18 |
|
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: 81.94 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPLNlvnlfFV 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgkPLDIAARNRIG-----YL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDL-PSVSLND---YYRSLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEP 154
Cdd:cd03269 76 PEERGLyPKMKVIDqlvYLAQLKGLKKEEARRRIDEWLERLELSeyANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500096509 155 TNGLDIASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLTII 198
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAgktVILST-HQMELVEELCDRVLLL 201
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-183 |
1.07e-18 |
|
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: 85.27 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL--DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLkvfPRNPLNLVNLF-- 78
Cdd:COG2274 474 IELENVSFRYPGDSPPVldNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI---DLRQIDPASLRrq 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 --FVPEEFDLPSVSLndyYRSLCKFYPNFSEKDFKEYLLKFEID---------INLKFGSS----SYGQRKKSIIAFSLA 143
Cdd:COG2274 551 igVVLQDVFLFSGTI---RENITLGDPDATDEEIIEAARLAGLHdfiealpmgYDTVVGEGgsnlSGGQRQRLAIARALL 627
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 144 TDVPILIFDEPTNGLDIASKNVFRDIISN-FKNKIVFVTGH 183
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRlLKGRTVIIIAH 668
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-203 |
6.68e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 6.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS-LKV--FPRNplnlvnlff 79
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtVKIgyFDQH--------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 vPEEFDlPSVSLNDYyrsLCKFYPNFSEKDFKEYLLKF----EiDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPT 155
Cdd:COG0488 387 -QEELD-PDKTVLDE---LRDGAPGGTEQEVRGYLGRFlfsgD-DAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500096509 156 NGLDIASKNVFRDIISNFKNKIVFVTgHNvRDLVD-IVDHLTIIGNNNI 203
Cdd:COG0488 461 NHLDIETLEALEEALDDFPGTVLLVS-HD-RYFLDrVATRILEFEDGGV 507
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
1.27e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.54 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSlkvFPRNPLNLVNLFFVPE 82
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EfdlpsvslndyyRSLckfYPNFS-------------------EKDFKEYLLKFEID--INLKFGSSSYG-QRKKSIIAf 140
Cdd:COG4152 79 E------------RGL---YPKMKvgeqlvylarlkglskaeaKRRADEWLERLGLGdrANKKVEELSKGnQQKVQLIA- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 141 SLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK---IVFVTgHNVrDLVD-IVDHLTIIGNNNILFSNSVSYINNSY 216
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgttVIFSS-HQM-ELVEeLCDRIVIINKGRKVLSGSVDEIRRQF 220
|
....*
gi 500096509 217 KVKIV 221
Cdd:COG4152 221 GRNTL 225
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-190 |
2.55e-17 |
|
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: 78.32 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYR----KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNslkvfPRNPLNLVNLF 78
Cdd:cd03257 2 LEVKNLSVSFPtgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-----GKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 ---------FVPEEfdlPSVSLNDYYR-------SLCKFYPNFSEKDFKEYLLKFEIDINL--KFGSS-----SYGQRKK 135
Cdd:cd03257 77 rkirrkeiqMVFQD---PMSSLNPRMTigeqiaePLRIHGKLSKKEARKEAVLLLLVGVGLpeEVLNRyphelSGGQRQR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 136 SIIAFSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIVFVTgHN---VRDLVD 190
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQaqilDLLKKLQEELGLTLLFIT-HDlgvVAKIAD 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-198 |
3.13e-17 |
|
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: 78.02 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNL-VNLF 78
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLrRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDLPSVSLNDyyrSLCKFYPNFSEKDF---------KEYLLK----FEIDINLKFGSSSYGQRKKSIIAFSLATD 145
Cdd:cd03245 82 YVPQDVTLFYGTLRD---NITLGAPLADDERIlraaelagvTDFVNKhpngLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 146 VPILIFDEPTNGLDIASKnvfRDIISNFKN----KIVFVTGHNVRdLVDIVDHLTII 198
Cdd:cd03245 159 PPILLLDEPTSAMDMNSE---ERLKERLRQllgdKTLIIITHRPS-LLDLVDRIIVM 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-206 |
1.19e-16 |
|
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: 76.54 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLK---GEVLFNSLkvfPRNP-LNLVNLFFVPE-EFDLPSVSLND- 93
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPdQFQKCVAYVRQdDILLPGLTVREt 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 94 -YYRSLC-------KFYPNFSEKDFKEYLLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNV 165
Cdd:cd03234 102 lTYTAILrlprkssDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 500096509 166 FRDIISNF--KNKIVFVTGHNVR-DLVDIVDHLTIIGNNNILFS 206
Cdd:cd03234 182 LVSTLSQLarRNRIVILTIHQPRsDLFRLFDRILLLSSGEIVYS 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-184 |
5.65e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.53 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 32 LILGKNGMGKTTLLKLISGLLNPLKGEVLFNslkvfprnplnlvnlffvPEEFDLPSVSLNDYY---RSLCK-------- 100
Cdd:PRK13539 32 VLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD------------------GGDIDDPDVAEACHYlghRNAMKpaltvaen 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 101 --FYPNF---SEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNF 173
Cdd:PRK13539 94 leFWAAFlggEELDIAAALEAVGLAplAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|...
gi 500096509 174 --KNKIVFVTGHN 184
Cdd:PRK13539 174 laQGGIVIAATHI 186
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-183 |
1.06e-15 |
|
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: 73.12 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNslkvfprnplnlvnlffv 80
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 peefDLPSVSLNDYYRSLCKFYPNfsekdfKEYLLKFEIDINL--KFgssSYGQRKKSIIAFSLATDVPILIFDEPTNGL 158
Cdd:cd03247 63 ----GVPVSDLEKALSSLISVLNQ------RPYLFDTTLRNNLgrRF---SGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180
....*....|....*....|....*..
gi 500096509 159 D-IASKNVFRDIISNFKNK-IVFVTGH 183
Cdd:cd03247 130 DpITERQLLSLIFEVLKDKtLIWITHH 156
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-204 |
2.65e-15 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 75.29 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNL-VNLF 78
Cdd:TIGR03375 463 EIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLrRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDLPSVSLNDyyrSLCKFYPNFSEKDFKEYLLK-------------FEIDINLKFGSSSYGQRKKSIIAFSLATD 145
Cdd:TIGR03375 543 YVPQDPRLFYGTLRD---NIALGAPYADDEEILRAAELagvtefvrrhpdgLDMQIGERGRSLSGGQRQAVALARALLRD 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 146 VPILIFDEPTNGLDIASKNVFRDIISNF--KNKIVFVTgHNvRDLVDIVDHLTIIGNNNIL 204
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKDRLKRWlaGKTLVLVT-HR-TSLLDLVDRIIVMDNGRIV 678
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-201 |
2.71e-15 |
|
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: 70.94 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPrnplnlvnlffvpe 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 efdlpsvslndYYRSLckfypnfsekdfkeyllkfeidinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIAS 162
Cdd:cd03221 67 -----------YFEQL------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500096509 163 KNVFRDIISNFKNKIVFVTgHNvRDLVD-IVDHLTIIGNN 201
Cdd:cd03221 106 IEALEEALKEYPGTVILVS-HD-RYFLDqVATKIIELEDG 143
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-212 |
5.16e-15 |
|
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: 72.15 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPEeFD--LPSVSLNDYYRS 97
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQ-FDalFDELTVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 98 LCKFY-----PNFSEKDFKEYLLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISN 172
Cdd:cd03263 99 YARLKglpksEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 173 FK-NKIVFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYI 212
Cdd:cd03263 179 VRkGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-193 |
1.01e-14 |
|
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: 70.98 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYR----KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-----SLK-------- 65
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisKLSekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 66 ------VFPRnpLNLVNLFFVPEEFDLPSVslndyyrsLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSI 137
Cdd:cd03255 81 rrhigfVFQS--FNLLPDLTALENVELPLL--------LAGVPKKERRERAEELLERVGLGdrLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 138 IAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK----IVFVTgHNvRDLVDIVD 193
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEagttIVVVT-HD-PELAEYAD 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-204 |
1.07e-14 |
|
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: 71.01 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRnPLNLVNLFFVPE 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDLpsvslndyyrslckfYPNFS-------------------EKDFKEYLLKFEIDINLKF--GSSSYGQRKKSIIAFS 141
Cdd:cd03259 80 DYAL---------------FPHLTvaeniafglklrgvpkaeiRARVRELLELVGLEGLLNRypHELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 142 LATDVPILIFDEPTNGLDIASKNV----FRDIISNFKNKIVFVTgHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREElreeLKELQRELGITTIYVT-HDQEEALALADRIAVMNEGRIV 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-183 |
1.25e-14 |
|
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: 73.25 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPLnLVNLFF 79
Cdd:COG4988 337 IELEDVSFSYPGGRPALdGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEFDLPSVSLNDyyrSLCKFYPNFSEKDFKE-----YLLKF------EIDINLKFGSS--SYGQRKKSIIAFSLATDV 146
Cdd:COG4988 416 VPQNPYLFAGTIRE---NLRLGRPDASDEELEAaleaaGLDEFvaalpdGLDTPLGEGGRglSGGQAQRLALARALLRDA 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 500096509 147 PILIFDEPTNGLDIASKNVFRDIISN-FKNKIVFVTGH 183
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRlAKGRTVILITH 530
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-198 |
2.07e-14 |
|
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: 68.99 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNL--FFV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgiAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 peefdlpsvslndyyrslckfypnfsekdfkeYLLkfeidinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDI 160
Cdd:cd03216 81 --------------------------------YQL-------------SVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 161 ASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLTII 198
Cdd:cd03216 116 AEVERLFKVIRRLRAQgvaVIFIS-HRLDEVFEIADRVTVL 155
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-184 |
2.26e-14 |
|
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: 70.29 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLN-----PLKGEVLFNSLKVF--PRNPLNL- 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 75 --VNLFF-VPEEFDLpSVSLNDYY------RSLCKFYPNFSEKDFKEYLLKFEIDINLKFGSSSYGQRKKSIIAFSLATD 145
Cdd:cd03260 81 rrVGMVFqKPNPFPG-SIYDNVAYglrlhgIKLKEELDERVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 146 VPILIFDEPTNGLDIASKNVFRDIISNFKNK--IVFVTgHN 184
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEytIVIVT-HN 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-208 |
2.41e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.35 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVY-----LDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKV--------- 66
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPYehqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 67 ------------FPRNPLNLVN----LFFVPEEFDLPSVSLNDY-YRSLCKfypnfsekdfkeylLKFEIDI-NLKFGSS 128
Cdd:PRK13646 81 rpvrkrigmvfqFPESQLFEDTvereIIFGPKNFKMNLDEVKNYaHRLLMD--------------LGFSRDVmSQSPFQM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 129 SYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFK---NKIVFVTGHNVRDLVDIVDHLTIIGNNNILF 205
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdeNKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
...
gi 500096509 206 SNS 208
Cdd:PRK13646 227 QTS 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-205 |
3.56e-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: 69.12 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKI--KVYLDL--NLAFS-KPQTYL-ILGKNGMGKTTLLKLISGLLNP--LKGEVLFNSLKVFPRNPL 72
Cdd:cd03213 2 VTLSFRNLTVTVKSSpsKSGKQLlkNVSGKaKPGELTaIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 73 NLVNlfFVPEEfdlpsvslnDYyrslckFYPNFSekdFKEYLlkfeiDINLKFGSSSYGQRKKSIIAFSLATDVPILIFD 152
Cdd:cd03213 82 KIIG--YVPQD---------DI------LHPTLT---VRETL-----MFAAKLRGLSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500096509 153 EPTNGLDIASKnvfRDIISNFK-----NKIVFVTGHNVR-DLVDIVDHLTIIGNNNILF 205
Cdd:cd03213 137 EPTSGLDSSSA---LQVMSLLRrladtGRTIICSIHQPSsEIFELFDKLLLLSQGRVIY 192
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-198 |
6.38e-14 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 70.11 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 12 YRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFpRNPLNL-VNLFFVPEEF----DL 86
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV-REPRKVrRSIGIVPQYAsvdeDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 87 PSVS-------LNDYYRSLckfypnfSEKDFKEYLLKFEI--DINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNG 157
Cdd:TIGR01188 82 TGREnlemmgrLYGLPKDE-------AEERAEELLELFELgeAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500096509 158 LDIASKNVFRDIISNFK--NKIVFVTGHNVR------DLVDIVDHLTII 198
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKeeGVTILLTTHYMEeadklcDRIAIIDHGRII 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-203 |
6.88e-14 |
|
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: 69.25 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLV-NLFFV 80
Cdd:cd03295 1 IEFENVTKRYGGGKKAVnNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDL-P--SVSLN-DYYRSLCKFYPNFSEKDFKEyLLKfeiDINL---KFGSS-----SYGQRKKSIIAFSLATDVPI 148
Cdd:cd03295 81 IQQIGLfPhmTVEENiALVPKLLKWPKEKIRERADE-LLA---LVGLdpaEFADRyphelSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500096509 149 LIFDEPTNGLD-IASKNV---FRDIISNFKNKIVFVTgHNVRDLVDIVDHLTIIGNNNI 203
Cdd:cd03295 157 LLMDEPFGALDpITRDQLqeeFKRLQQELGKTIVFVT-HDIDEAFRLADRIAIMKNGEI 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-216 |
7.18e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVpeeF--------DLPsvsLNDYYRSLCKFYpN 104
Cdd:COG4586 53 FIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVV---FgqrsqlwwDLP---AIDSFRLLKAIY-R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 105 FSEKDFKEYLLKF-EI-DI---------NLkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNF 173
Cdd:COG4586 126 IPDAEYKKRLDELvELlDLgelldtpvrQL-----SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500096509 174 ---KNKIVFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINNSY 216
Cdd:COG4586 201 nreRGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-203 |
1.66e-13 |
|
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: 67.52 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKvyLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVF----PRNPLNLV--- 75
Cdd:cd03298 1 VRLDKIRFSYGEQP--MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaappADRPVSMLfqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 -NLF---FVPEEFDL---PSVSLNDYYRslckfypnfseKDFKEYLLKFEIDINLKF--GSSSYGQRKKSIIAFSLATDV 146
Cdd:cd03298 79 nNLFahlTVEQNVGLglsPGLKLTAEDR-----------QAIEVALARVGLAGLEKRlpGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 147 PILIFDEPTNGLDIASKNVFRDIISNF----KNKIVFVTgHNVRDLVDIVDHLTIIGNNNI 203
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLhaetKMTVLMVT-HQPEDAKRLAQRVVFLDNGRI 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-160 |
2.79e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPLNLvNLF 78
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkPISMLSSRQLAR-RLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDLP---SV-SLNDYYRS-LCKFYPNFSEKD---FKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPI 148
Cdd:PRK11231 80 LLPQHHLTPegiTVrELVAYGRSpWLSLWGRLSAEDnarVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170
....*....|..
gi 500096509 149 LIFDEPTNGLDI 160
Cdd:PRK11231 160 VLLDEPTTYLDI 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-206 |
3.85e-13 |
|
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: 66.55 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYL-ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVF-PRNPLNL------VNLFFvpEEFDL-PSVS 90
Cdd:cd03297 14 TLKIDFDLNEEVTgIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdSRKKINLppqqrkIGLVF--QQYALfPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 91 LndyYRSLC---KFYPNFSEKDFKEYLLK-FEIDINLKFGSS--SYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKN 164
Cdd:cd03297 92 V---RENLAfglKRKRNREDRISVDELLDlLGLDHLLNRYPAqlSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500096509 165 V----FRDIISNFKNKIVFVTgHNVRDLVDIVDHLTIIGNNNILFS 206
Cdd:cd03297 169 QllpeLKQIKKNLNIPVIFVT-HDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-176 |
3.87e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.71 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL--DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN---- 76
Cdd:PRK13632 8 IKVENVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 LFFVPEEFDLPSVSLNDYYRSL--CKFYPNFSEKDFKEYLLKFEIDINLKFGSS--SYGQRKKSIIAFSLATDVPILIFD 152
Cdd:PRK13632 88 IFQNPDNQFIGATVEDDIAFGLenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQnlSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180
....*....|....*....|....
gi 500096509 153 EPTNGLDIASKNVFRDIISNFKNK 176
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKT 191
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-195 |
6.31e-13 |
|
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: 66.75 E-value: 6.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY----RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS-------LKVFPRNp 71
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrrRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 72 lnlVNLFFvpeefdlpsvslNDYYRSLckfYPNFS-----------------EKDFKEYLLKFEIDINLKF---GSSSYG 131
Cdd:COG1124 81 ---VQMVF------------QDPYASL---HPRHTvdrilaeplrihglpdrEERIAELLEQVGLPPSFLDrypHQLSGG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 132 QRKKSIIAFSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIVFVTgHnvrDLvDIVDHL 195
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQaeilNLLKDLREERGLTYLFVS-H---DL-AVVAHL 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
14-208 |
2.33e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.03 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 14 KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPEE---------- 83
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKiknfkelrrr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 84 ----FDLPSVSL-NDYYRSLCKFYP-------NFSEKDFKEYLLKFEIDINL----KFGSSSyGQRKKSIIAFSLATDVP 147
Cdd:PRK13631 118 vsmvFQFPEYQLfKDTIEKDIMFGPvalgvkkSEAKKLAKFYLNKMGLDDSYlersPFGLSG-GQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500096509 148 ILIFDEPTNGLDIASKNVFRDIISNFK--NKIVFVTGHNVRDLVDIVDHLTIIGNNNILFSNS 208
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKanNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-185 |
3.36e-12 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 63.60 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 16 KVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN------------------------------SLK 65
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgepldysrkgllerrqrvglvfqdpddqlfAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 66 VFPRNPLNLVNLFFVPEEFD------LPSVSLNDYYRSLCKFYpnfsekdfkeyllkfeidinlkfgssSYGQRKKSIIA 139
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVErrvreaLTAVGASGLRERPTHCL--------------------------SGGEKKRVAIA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500096509 140 FSLATDVPILIFDEPTNGLDIASKNVFRDIISNFK---NKIVFVTgHNV 185
Cdd:TIGR01166 140 GAVAMRPDVLLLDEPTAGLDPAGREQMLAILRRLRaegMTVVIST-HDV 187
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-183 |
3.65e-12 |
|
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: 65.77 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYR-KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN-LFFV 80
Cdd:TIGR02857 322 LEFSGVSVAYPgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDqIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDLPSVSLNDYYRSLCkfyPNFSEKDFKEYLLKFEID---------INLKFGSS----SYGQRKKSIIAFSLATDVP 147
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRLAR---PDASDAEIREALERAGLDefvaalpqgLDTPIGEGgaglSGGQAQRLALARAFLRDAP 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 500096509 148 ILIFDEPTNGLDIASKNVFRDIISNF-KNKIVFVTGH 183
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALaQGRTVLLVTH 515
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-184 |
4.10e-12 |
|
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: 65.84 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLD-LNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKV--FPRNPLNLVNLFF 79
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDgVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVssLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 vPEEFDLPSVSLNDYYRSLCkfyPNFSEKDFKEYL--LKFEIDI-NLKFGSS----------SYGQRKKSIIAFSLATDV 146
Cdd:TIGR02868 415 -AQDAHLFDTTVRENLRLAR---PDATDEELWAALerVGLADWLrALPDGLDtvlgeggarlSGGERQRLALARALLADA 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 500096509 147 PILIFDEPTNGLDI-ASKNVFRDIISNFKNKIVFVTGHN 184
Cdd:TIGR02868 491 PILLLDEPTEHLDAeTADELLEDLLAALSGRTVVLITHH 529
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-194 |
1.16e-11 |
|
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: 64.40 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPL-NLVNl 77
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGgvDLRDLDEDDLrRRIA- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 78 fFVPEEFDLPSVSLNDYYRsLCKfyPNFSEKDFKEYL-----------LKFEIDINLkfGSS----SYGQRKKSIIAFSL 142
Cdd:COG4987 413 -VVPQRPHLFDTTLRENLR-LAR--PDATDEELWAALervglgdwlaaLPDGLDTWL--GEGgrrlSGGERRRLALARAL 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500096509 143 ATDVPILIFDEPTNGLDIAS-KNVFRDIISNFKNK-IVFVTgHNVRDLvDIVDH 194
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATeQALLADLLEALAGRtVLLIT-HRLAGL-ERMDR 538
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-160 |
1.21e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.50 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKV-YLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVlFNSLKVfprnPLNLVNLFFVp 81
Cdd:PLN03073 509 ISFSDASFGYPGGPLlFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKV----RMAVFSQHHV- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 82 EEFDLPSVSLndYYRSLCkfYPNFSEKDFKEYLLKFEIDINLKFGSS---SYGQrkKSIIAFSLAT-DVP-ILIFDEPTN 156
Cdd:PLN03073 583 DGLDLSSNPL--LYMMRC--FPGVPEQKLRAHLGSFGVTGNLALQPMytlSGGQ--KSRVAFAKITfKKPhILLLDEPSN 656
|
....
gi 500096509 157 GLDI 160
Cdd:PLN03073 657 HLDL 660
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-183 |
1.95e-11 |
|
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: 62.24 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLF-F 79
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLkDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIgV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEFDLPSVSLNDYYRSlckFYPNFSEKDFKE--------YLLKFEID-----INLKFGSSSYGQRKKSIIAFSLATDV 146
Cdd:cd03254 82 VLQDTFLFSGTIMENIRL---GRPNATDEEVIEaakeagahDFIMKLPNgydtvLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 500096509 147 PILIFDEPTNGLD-IASKNVFRDIISNFKNKIVFVTGH 183
Cdd:cd03254 159 KILILDEATSNIDtETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-185 |
2.91e-11 |
|
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: 61.82 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNP---------- 71
Cdd:cd03256 1 IEVENLSKTYPNGKKALkDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 72 ------LNLVNLFFVPEEFDLPSVSLNDYYRSLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLA 143
Cdd:cd03256 81 gmifqqFNLIERLSVLENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLdkAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500096509 144 TDVPILIFDEPTNGLD-IASKNVFRDI--ISNFKNKIVFVTGHNV 185
Cdd:cd03256 161 QQPKLILADEPVASLDpASSRQVMDLLkrINREEGITVIVSLHQV 205
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-214 |
2.98e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.06 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLD-LNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPL---NLVNLF 78
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKgLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvrSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FV-PEEFDLPSVSLNDyyrslCKFYPNFSEKDFKEYLLKFEIDINL----KFGSS-----SYGQRKKSIIAFSLATDVPI 148
Cdd:PRK13647 85 FQdPDDQVFSSTVWDD-----VAFGPVNMGLDKDEVERRVEEALKAvrmwDFRDKppyhlSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 149 LIFDEPTNGLDIASKNVFRDIISNFKN--KIVFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINN 214
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-198 |
3.25e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.11 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNP--------------LNLV-------NLFfvpeefdlpsvsL 91
Cdd:COG1129 35 LLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdaqaagiaiihqeLNLVpnlsvaeNIF------------L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 92 NDYYRSlcKFYPNFSE--KDFKEYLLKFEIDINL--KFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIA-SKNVF 166
Cdd:COG1129 103 GREPRR--GGLIDWRAmrRRARELLARLGLDIDPdtPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLF 180
|
170 180 190
....*....|....*....|....*....|....*
gi 500096509 167 RdIISNFKNK---IVFVTgHNVRDLVDIVDHLTII 198
Cdd:COG1129 181 R-IIRRLKAQgvaIIYIS-HRLDEVFEIADRVTVL 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-216 |
3.44e-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: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 21 LNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfprnplnLVNLFFVPEEFDL-PSVSLNDYYRSLC 99
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-------ETNLDAVRQSLGMcPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 100 K---FYPNFSEKDFKEYLLKFEIDI---------NLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFR 167
Cdd:TIGR01257 1022 EhilFYAQLKGRSWEEAQLEMEAMLedtglhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500096509 168 DIISNFKN-KIVFVTGHNVrDLVDIV-DHLTIIGNNNILFSNSVSYINNSY 216
Cdd:TIGR01257 1102 DLLLKYRSgRTIIMSTHHM-DEADLLgDRIAIISQGRLYCSGTPLFLKNCF 1151
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-196 |
3.77e-11 |
|
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: 61.30 E-value: 3.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-----SLKVFPRNPLNLVNLFFVPEEFDLPSV----- 89
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditGLPPHEIARLGIGRTFQIPRLFPELTVlenvm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 90 --SLNDYYRSLCKFYPNFSEKDFKEY---LLKF-EID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIA 161
Cdd:cd03219 98 vaAQARTGSGLLLARARREEREARERaeeLLERvGLAdlADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPE 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 500096509 162 SKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLT 196
Cdd:cd03219 178 ETEELAELIRELRERgitVLLVE-HDMDVVMSLADRVT 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-185 |
4.97e-11 |
|
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: 60.95 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL----DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPlnlvNLF 78
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVtaleDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDL-P--SVSLNdyyrslCKFYPNFSEKDFKE-------YLLKFEIDinlKFGSS-----SYGQRKKSIIAFSLA 143
Cdd:cd03293 77 YVFQQDALlPwlTVLDN------VALGLELQGVPKAEareraeeLLELVGLS---GFENAyphqlSGGMRQRVALARALA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500096509 144 TDVPILIFDEPTNGLDIASKNVFRD----IISNFKNKIVFVTgHNV 185
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEelldIWRETGKTVLLVT-HDI 192
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
7-204 |
5.03e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.56 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPLNLVNLffVPEEF 84
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkPLDYSKRGLLALRQQ--VATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 85 DLPSVSLndyyrslckFYPN------FSEKDF--KEYLLKFEIDINLKFGSS-----------SYGQRKKSIIAFSLATD 145
Cdd:PRK13638 84 QDPEQQI---------FYTDidsdiaFSLRNLgvPEAEITRRVDEALTLVDAqhfrhqpiqclSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 146 VPILIFDEPTNGLDIASKNVFRDIISNF--KNKIVFVTGHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-190 |
5.90e-11 |
|
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: 60.71 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDlNLAFSKP--QTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-------SLKVFPRnpln 73
Cdd:cd03253 1 IEFENVTFAYDPGRPVLK-DVSFTIPagKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdirevTLDSLRR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 74 lvNLFFVPEEfdlpSVSLND--YYrSLCKFYPNFSEKDFKEYLLKFEID---INLKFGSS----------SYGQRKKSII 138
Cdd:cd03253 76 --AIGVVPQD----TVLFNDtiGY-NIRYGRPDATDEEVIEAAKAAQIHdkiMRFPDGYDtivgerglklSGGEKQRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500096509 139 AFSLATDVPILIFDEPTNGLDIAS-KNVFRDIISNFKNKIVFVTGHNVRDLVD 190
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTeREIQAALRDVSKGRTTIVIAHRLSTIVN 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-162 |
7.62e-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: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 21 LNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPEefdLPSVSLNDYYRSLCK 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH---APGIKTTLSVLENLR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 101 FYPNFSEKDFKEYLLKfEIDIN----LKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIAS 162
Cdd:cd03231 96 FWHADHSDEQVEEALA-RVGLNgfedRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-200 |
7.64e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPE 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDL-PSVSLNDYYRSLCKFYpNFSEKDFKEY---LLKF---EIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPT 155
Cdd:PRK13537 88 FDNLdPDFTVRENLLVFGRYF-GLSAAAARALvppLLEFaklENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500096509 156 NGLDIASKNV----FRDIISnfKNKIVFVTGHNVRDLVDIVDHLTIIGN 200
Cdd:PRK13537 167 TGLDPQARHLmwerLRSLLA--RGKTILLTTHFMEEAERLCDRLCVIEE 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-183 |
8.34e-11 |
|
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: 60.58 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL--DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSL------KVFPRNPLNL 74
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIldNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 75 V---NLFFVPEEFDlpSVSLNDYYRSLCKFYPNFSEKDFKEYLLKFEIDINLKFGSS----SYGQRKKSIIAFSLATDVP 147
Cdd:cd03252 81 VlqeNVLFNRSIRD--NIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQgaglSGGQRQRIAIARALIHNPR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 500096509 148 ILIFDEPTNGLDIASKnvfRDIISNFK----NKIVFVTGH 183
Cdd:cd03252 159 ILIFDEATSALDYESE---HAIMRNMHdicaGRTVIIIAH 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-209 |
8.61e-11 |
|
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: 61.84 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL--DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNP---LKGEVLFN-------SLK----- 65
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDgrdllelSEAlrgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 66 ---VF--PRNPLNLVN----LFFVPEEFDLPS-------------VSLNDYYRSlckfYPnfsekdfkeyllkFEIdinl 123
Cdd:COG1123 85 igmVFqdPMTQLNPVTvgdqIAEALENLGLSRaeararvlelleaVGLERRLDR----YP-------------HQL---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 124 kfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKN----VFRDIISNFKNKIVFVTgHNVRDLVDIVDHLTIIG 199
Cdd:COG1123 144 -----SGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAeildLLRELQRERGTTVLLIT-HDLGVVAEIADRVVVMD 217
|
250
....*....|
gi 500096509 200 NNNILFSNSV 209
Cdd:COG1123 218 DGRIVEDGPP 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-170 |
8.98e-11 |
|
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: 59.37 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN--LFFVPEEfdlpsvslndyyRslckfypnfsekdf 110
Cdd:cd03215 31 IAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRagIAYVPED------------R-------------- 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500096509 111 KEY--LLKFEIDINLKFGSS-SYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDII 170
Cdd:cd03215 85 KREglVLDLSVAENIALSSLlSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI 147
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-204 |
1.42e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.16 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfPRnpLNLVNLFFVPE 82
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-PA--MSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDL--PSVSLndyYRSLCKF----YPNFSEKDFKEYLLKFEIDI-----------NLKFGSSSYGQRKKSIIAFSLATD 145
Cdd:PRK11831 85 RMSMlfQSGAL---FTDMNVFdnvaYPLREHTQLPAPLLHSTVMMkleavglrgaaKLMPSELSGGMARRAALARAIALE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 146 VPILIFDEPTNGLDIASKNVFRDIISNFKNKI---VFVTGHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-183 |
1.46e-10 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 61.30 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRK--IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLV-NLFF 79
Cdd:TIGR01846 456 ITFENIRFRYAPdsPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRrQMGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEFDLPSVSLNDYYRsLCKfyPNFSEK------------DFKEYLLK-FEIDINLKFGSSSYGQRKKSIIAFSLATDV 146
Cdd:TIGR01846 536 VLQENVLFSRSIRDNIA-LCN--PGAPFEhvihaaklagahDFISELPQgYNTEVGEKGANLSGGQRQRIAIARALVGNP 612
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 147 PILIFDEPTNGLDIASKNVfrdIISNF----KNKIVFVTGH 183
Cdd:TIGR01846 613 RILIFDEATSALDYESEAL---IMRNMreicRGRTVIIIAH 650
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-198 |
1.59e-10 |
|
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: 59.08 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLN--PLKGEVLF-----NSLKVFPRNPLNLVNLFFVPEEFdlPSVSLN 92
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFkgediTDLPPEERARLGIFLAFQYPPEI--PGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 93 DYYRSLckfypnfsekdfkeyllkfeidiNLKFgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISN 172
Cdd:cd03217 96 DFLRYV-----------------------NEGF---SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINK 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 500096509 173 FKNK---IVFVTgHNVR-------DLVDIVDHLTII 198
Cdd:cd03217 150 LREEgksVLIIT-HYQRlldyikpDRVHVLYDGRIV 184
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-213 |
1.73e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPL--NLVNLFFV 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkaHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEE---FDLPSVSLNDYYRsLCKfyPNFSEKDFKEYL--LKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPT 155
Cdd:PRK15439 92 PQEpllFPNLSVKENILFG-LPK--RQASMQKMKQLLaaLGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 156 NGLD-IASKNVFRDIISnFKNK---IVFVTgHNVRDLVDIVDHLTIIGNNNILFSNSVSYIN 213
Cdd:PRK15439 169 ASLTpAETERLFSRIRE-LLAQgvgIVFIS-HKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-194 |
1.84e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 60.85 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVlfnslkVFPRNplnlVNLFFVPEEFDL 86
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------SIPKG----LRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 87 -PSVSLNDY-------YRSLCKFY------PNFSEKDFKEYL------------------------LKF-EIDINLKFGS 127
Cdd:COG0488 73 dDDLTVLDTvldgdaeLRALEAELeeleakLAEPDEDLERLAelqeefealggweaearaeeilsgLGFpEEDLDRPVSE 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 128 SSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNKIVFVTgHNvRDLVD-IVDH 194
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVS-HD-RYFLDrVATR 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-221 |
2.01e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.52 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 11 SYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS--LKVFPRNPLNLVNLFFVPEEFDL-P 87
Cdd:PRK10895 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedISLLPLHARARRGIGYLPQEASIfR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 88 SVSLNDYYRSLCKFYPNFSEKDFK----EYLLKFEID-INLKFGSS-SYGQRKKSIIAFSLATDVPILIFDEPTNGLDIA 161
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLSAEQREdranELMEEFHIEhLRDSMGQSlSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 162 SKNVFRDIISNFKNK--IVFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINNSYKVKIV 221
Cdd:PRK10895 172 SVIDIKRIIEHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-195 |
2.09e-10 |
|
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: 60.69 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY-----RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNL 77
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 78 F----FVpeeFDLPSVSLNDY---YRSLC---KFYPNFSEKDFKE---YLLKfEIDINLKFGSS-----SYGQRKKSIIA 139
Cdd:COG1123 341 RrrvqMV---FQDPYSSLNPRmtvGDIIAeplRLHGLLSRAERRErvaELLE-RVGLPPDLADRyphelSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 140 FSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIVFVTgHnvrDLvDIVDHL 195
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQaqilNLLRDLQRELGLTYLFIS-H---DL-AVVRYI 471
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
7-203 |
3.11e-10 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 58.33 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDLNLAfsKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFP----RNPLNLV----NLF 78
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGlapyQRPVSMLfqenNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 ---FVPEEFDL---PSVSLNDYYRSlcKFYPNFSEKDFKEYLLKFEidinlkfGSSSYGQRKKSIIAFSLATDVPILIFD 152
Cdd:TIGR01277 83 ahlTVRQNIGLglhPGLKLNAEQQE--KVVDAAQQVGIADYLDRLP-------EQLSGGQRQRVALARCLVRPNPILLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500096509 153 EPTNGLDIASKNVFRDIISNF---KNKIVFVTGHNVRDLVDIVDHLTIIGNNNI 203
Cdd:TIGR01277 154 EPFSALDPLLREEMLALVKQLcseRQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-195 |
3.67e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.26 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYR------KIKVYlDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFP-RNPLN 73
Cdd:PRK13634 1 MDITFQKVEHRYQyktpfeRRALY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 74 LVNL-------FFVPEEFDLPSVSLNDyyrsLCkFYP-NF--SEKDFKE---YLLK-------------FEIdinlkfgs 127
Cdd:PRK13634 80 LKPLrkkvgivFQFPEHQLFEETVEKD----IC-FGPmNFgvSEEDAKQkarEMIElvglpeellarspFEL-------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 128 sSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK----IVFVTgHNVRDLVDIVDHL 195
Cdd:PRK13634 147 -SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkgltTVLVT-HSMEDAARYADQI 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-206 |
4.26e-10 |
|
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: 58.21 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-----SLKVFPRNPLNLVnlfFVP 81
Cdd:cd03224 5 NLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditGLPPHERARAGIG---YVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 82 EE---FDLPSVSLN----DYYRSLCKFypnfsEKDFKEYLLKFEIdinLK------FGSSSYGQRKKSIIAFSLATDVPI 148
Cdd:cd03224 82 EGrriFPELTVEENlllgAYARRRAKR-----KARLERVYELFPR---LKerrkqlAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 149 LIFDEPTNGLD-IASKNVFrDIISNFKNK---IVFVTgHNVRDLVDIVDHLTIIGNNNILFS 206
Cdd:cd03224 154 LLLDEPSEGLApKIVEEIF-EAIRELRDEgvtILLVE-QNARFALEIADRAYVLERGRVVLE 213
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-191 |
7.39e-10 |
|
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: 57.73 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEfiDVSFSYRKIKVYlDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLvNLFFV 80
Cdd:cd03299 1 LKVE--NLSKDWKEFKLK-NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR-DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PeefdlpsvslNDYYrslckFYPNFSEKDFKEYLL------KFEID---------------INLKFGSSSYGQRKKSIIA 139
Cdd:cd03299 77 P----------QNYA-----LFPHMTVYKNIAYGLkkrkvdKKEIErkvleiaemlgidhlLNRKPETLSGGEQQRVAIA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500096509 140 FSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNKIVFVTGHNVRDLVDI 191
Cdd:cd03299 142 RALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEA 193
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-159 |
8.79e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.94 E-value: 8.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS--LKVFPRNPLNL---VNLFFVPEEFDLPSVSLND- 93
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLresVGMVFQDPDNQLFSASVYQd 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 94 -YYRSLCKFYPNFSEKDFKEYLLKFEIDINLKFGSS---SYGQRKKSIIAFSLATDVPILIFDEPTNGLD 159
Cdd:PRK13636 104 vSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPThclSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
33-170 |
1.11e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 56.60 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFVPEEFDLP---SVSLN-DYYRSLCKFYPNFSEK 108
Cdd:TIGR01189 31 VTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKpelSALENlHFWAAIHGGAQRTIED 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500096509 109 DFKEY-LLKFEidiNLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDII 170
Cdd:TIGR01189 111 ALAAVgLTGFE---DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-208 |
1.11e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 57.83 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYR-----KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKV--------- 66
Cdd:PRK13649 1 MGINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 67 -FPRNPLNLVnlFFVPEEFDLPSVSLNDyyrslCKFYP-NF------SEKDFKEYLLKFEIDINLkFGSS----SYGQRK 134
Cdd:PRK13649 81 kQIRKKVGLV--FQFPESQLFEETVLKD-----VAFGPqNFgvsqeeAEALAREKLALVGISESL-FEKNpfelSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 135 KSIIAFSLATDVPILIFDEPTNGLDIASKnvfRDIISNFKN------KIVFVTgHNVRDLVDIVDHLTIIGNNNILFSNS 208
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGR---KELMTLFKKlhqsgmTIVLVT-HLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-162 |
1.42e-09 |
|
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: 56.78 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY---RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLF- 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDLPSVSLNDYYRsLCKFYPnfSEKDFKEYLLKFEID---INL--KF-------GSS-SYGQRKKSIIAFSLATD 145
Cdd:cd03249 81 LVSQEPVLFDGTIAENIR-YGKPDA--TDEEVEEAAKKANIHdfiMSLpdGYdtlvgerGSQlSGGQKQRIAIARALLRN 157
|
170
....*....|....*..
gi 500096509 146 VPILIFDEPTNGLDIAS 162
Cdd:cd03249 158 PKILLLDEATSALDAES 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-203 |
1.48e-09 |
|
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: 56.96 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLvNLFFV 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDLpsvslndyYRSLCKF--------------YPNFSEKDFK-EYLLKFeidINLKFGSSSY------GQRKKSIIA 139
Cdd:cd03296 80 FQHYAL--------FRHMTVFdnvafglrvkprseRPPEAEIRAKvHELLKL---VQLDWLADRYpaqlsgGQRQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 140 FSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNKI----VFVTgHNVRDLVDIVDHLTIIGNNNI 203
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVT-HDQEEALEVADRVVVMNKGRI 215
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-229 |
1.69e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.87 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSlKVFPR---------------NPLNLVNLFFVPEEF 84
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-INYNKldhklaaqlgigiiyQELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 85 ---DLPS-----VSLNDYyrslckfypNFSEKDFKEYLLK--FEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEP 154
Cdd:PRK09700 102 yigRHLTkkvcgVNIIDW---------REMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 155 TNGLDIASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLTIIGNNNILFSNSVSYINNSykvKIVDKLEGEEL 229
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEgtaIVYIS-HKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND---DIVRLMVGREL 246
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-203 |
1.71e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPLNlVNLF 78
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNgqPIADYSEAALR-QAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDLPSVSLNDYYRSLCkfyPNFSEKDFK--------EYLLKFEIDINLKFGSS----SYGQRKKSIIAFSLATDV 146
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAA---PNASDEALIevlqqvglEKLLEDDKGLNAWLGEGgrqlSGGEQRRLGIARALLHDA 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 147 PILIFDEPTNGLDiasKNVFRDIISN----FKNK-IVFVTgHNVRDLvDIVDHLTIIGNNNI 203
Cdd:PRK11160 495 PLLLLDEPTEGLD---AETERQILELlaehAQNKtVLMIT-HRLTGL-EQFDRICVMDNGQI 551
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-183 |
1.86e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.87 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRK-IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNplNLVNLF- 78
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvDIRDLTLE--SLRRQIg 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 FVPEEFDLPSVSLND---YYRslckfyPNFSEKD---------FKEYLLKFE--ID-------INLkfgssSYGQRKKSI 137
Cdd:COG1132 418 VVPQDTFLFSGTIREnirYGR------PDATDEEveeaakaaqAHEFIEALPdgYDtvvgergVNL-----SGGQRQRIA 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 500096509 138 IAFSLATDVPILIFDEPTNGLDIAS-KNVFRDIISNFKNKIVFVTGH 183
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETeALIQEALERLMKGRTTIVIAH 533
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-198 |
1.96e-09 |
|
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: 56.22 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFpRNPLNL-VNLFFVPEEfdlpsVSLNDY---Y 95
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV-REPREVrRRIGIVFQD-----LSVDDEltgW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 96 RSLCKF-----YPNFSEKDFKEYLLKFeIDI----NLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVF 166
Cdd:cd03265 92 ENLYIHarlygVPGAERRERIDELLDF-VGLleaaDRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 167 RDIISNFK---NKIVFVTGHNVR------DLVDIVDHLTII 198
Cdd:cd03265 171 WEYIEKLKeefGMTILLTTHYMEeaeqlcDRVAIIDHGRII 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
7-204 |
2.29e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.94 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRK-----IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfprnPLNL------- 74
Cdd:PRK13645 11 NVSYTYAKktpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI----PANLkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 75 -----VNLFFVPEEFDLpsvsLNDYYRSLCKFYPNFSEKDFKEYLLKFEIDINLKFGSSSY----------GQRKKSIIA 139
Cdd:PRK13645 87 rlrkeIGLVFQFPEYQL----FQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYvkrspfelsgGQKRRVALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500096509 140 FSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIVFVTgHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEedfiNLFERLNKEYKKRIIMVT-HNMDQVLRIADEVIVMHEGKVI 230
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
34-219 |
2.46e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 56.19 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 34 LGKNGMGKTTLLKLISGLLNPLKGEVLFN-----SLKVFPRNPLNLVNLffvPEEfdlPSVslndyYRSLC--------- 99
Cdd:COG1137 35 LGPNGAGKTTTFYMIVGLVKPDSGRIFLDgeditHLPMHKRARLGIGYL---PQE---ASI-----FRKLTvednilavl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 100 -KFYPNFSEKDFK-EYLLKfEIDI----NLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLD-IASKNVfRDIISN 172
Cdd:COG1137 104 eLRKLSKKEREERlEELLE-EFGIthlrKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVADI-QKIIRH 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500096509 173 FKNK-I-VFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINNSYKVK 219
Cdd:COG1137 182 LKERgIgVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-198 |
2.93e-09 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 56.01 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPrnplNLVNLFFVPE--EF--DLP----SVSLND------YYRSL 98
Cdd:TIGR03771 11 LLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK----GWRHIGYVPQrhEFawDFPisvaHTVMSGrtghigWLRRP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 99 CKfyPNFSEKDFKEYLLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDI---ISNFKN 175
Cdd:TIGR03771 87 CV--ADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELfieLAGAGT 164
|
170 180
....*....|....*....|...
gi 500096509 176 KIVFVTgHNVRDLVDIVDHLTII 198
Cdd:TIGR03771 165 AILMTT-HDLAQAMATCDRVVLL 186
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-198 |
3.40e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFV 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PeEFDlpSVSLNDYYR-SLCKF--YPNFSEKDFKEY---LLKF---EIDINLKFGSSSYGQRKKSIIAFSLATDVPILIF 151
Cdd:PRK13536 120 P-QFD--NLDLEFTVReNLLVFgrYFGMSTREIEAVipsLLEFarlESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 500096509 152 DEPTNGLDIASKNV----FRDIISnfKNKIVFVTGHNVRDLVDIVDHLTII 198
Cdd:PRK13536 197 DEPTTGLDPHARHLiwerLRSLLA--RGKTILLTTHFMEEAERLCDRLCVL 245
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-162 |
4.56e-09 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 56.65 E-value: 4.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-------SLKVFpRNPL 72
Cdd:TIGR02203 330 DVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdladyTLASL-RRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 73 NLVN----LF--FVPEEF---DLPSVSLNDYYRSLCKFYPnfseKDFKEYL---LKFEIDINlkfGSS-SYGQRKKSIIA 139
Cdd:TIGR02203 409 ALVSqdvvLFndTIANNIaygRTEQADRAEIERALAAAYA----QDFVDKLplgLDTPIGEN---GVLlSGGQRQRLAIA 481
|
170 180
....*....|....*....|...
gi 500096509 140 FSLATDVPILIFDEPTNGLDIAS 162
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNES 504
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-183 |
4.66e-09 |
|
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: 55.31 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRK--IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLF-F 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIgL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEFDLPSVSLND---YYRslckfyPNFSEKDFKE-----YLLKFEIDINLKFGSS--------SYGQRKKSIIAFSLA 143
Cdd:cd03251 81 VSQDVFLFNDTVAEniaYGR------PGATREEVEEaaraaNAHEFIMELPEGYDTVigergvklSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 144 TDVPILIFDEPTNGLDIASKNVFRDIISNF-KNKIVFVTGH 183
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLmKNRTTFVIAH 195
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
3-186 |
5.40e-09 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 56.50 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIK----VYLD-LNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNL 77
Cdd:TIGR01194 338 IELKDVHMNPKAPEgsegFALGpIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDYRDL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 78 F-FVPEEFDLpsvsLNDYYRSLCKFYPnfSEKDFKEYLLKFEID-----INLKFGSS---SYGQRKKSIIAFSLATDVPI 148
Cdd:TIGR01194 418 FsAIFADFHL----FDDLIGPDEGEHA--SLDNAQQYLQRLEIAdkvkiEDGGFSTTtalSTGQQKRLALICAWLEDRPI 491
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 149 LIFDEPTNGLDIASKNVF-RDIISNFK--NKIVFVTGHNVR 186
Cdd:TIGR01194 492 LLFDEWAADQDPAFKRFFyEELLPDLKrqGKTIIIISHDDQ 532
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-183 |
6.45e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKiKVYLDlNLAFSKPQTYLI--LGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFFV 80
Cdd:PRK13540 2 LDVIELDFDYHD-QPLLQ-QISFHLPAGGLLhlKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDL-PSVSLndyyRSLCKFYPNFS----EKDFKEYLLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPT 155
Cdd:PRK13540 80 GHRSGInPYLTL----RENCLYDIHFSpgavGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|
gi 500096509 156 NGLDIASKNVFRDIISNFKNK--IVFVTGH 183
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKggAVLLTSH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
3-190 |
7.35e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 55.09 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYR-------KIKVYL---------------DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVL 60
Cdd:COG1134 5 IEVENVSKSYRlyhepsrSLKELLlrrrrtrreefwalkDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 61 FNSlKVFPrnPLNLvNLFFVPE----EfdlpsvslNDYYRslCKFYpNFSEKDFKEYL---LKF-EID--INLKFGSSSY 130
Cdd:COG1134 85 VNG-RVSA--LLEL-GAGFHPEltgrE--------NIYLN--GRLL-GLSRKEIDEKFdeiVEFaELGdfIDQPVKTYSS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500096509 131 GQRKKsiIAFSLATDVP--ILIFDEPTNGLDIA----SKNVFRDIISNFKNkIVFVTgHN---VRDLVD 190
Cdd:COG1134 150 GMRAR--LAFAVATAVDpdILLVDEVLAVGDAAfqkkCLARIRELRESGRT-VIFVS-HSmgaVRRLCD 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-190 |
7.35e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.95 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLAfskPQTYL-ILGKNGMGKTTLLKLISGLLNPLKGEV-LFNSLKV--FPRNPLNlvn 76
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLV---PGSRIgLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyFAQHQLE--- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 lFFVPEEFDLpsvslndyyRSLCKFYPNFSEKDFKEYLLKFEI------DINLKFgssSYGQRKKSIIAFSLATDVPILI 150
Cdd:PRK10636 387 -FLRADESPL---------QHLARLAPQELEQKLRDYLGGFGFqgdkvtEETRRF---SGGEKARLVLALIVWQRPNLLL 453
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500096509 151 FDEPTNGLDIASKNVFRDIISNFKNKIVFVTG--HNVRDLVD 190
Cdd:PRK10636 454 LDEPTNHLDLDMRQALTEALIDFEGALVVVSHdrHLLRSTTD 495
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-170 |
1.32e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 53.39 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLfnslkvfpRNPLnlVNLFFVPEEFDLP---------SVS 90
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------RAGG--ARVAYVPQRSEVPdslpltvrdLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 91 LNDY-YRSLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFR 167
Cdd:NF040873 80 MGRWaRRGLWRRLTRDDRAAVDDALERVGLAdlAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
...
gi 500096509 168 DII 170
Cdd:NF040873 160 ALL 162
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
33-62 |
1.43e-08 |
|
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: 53.83 E-value: 1.43e-08
10 20 30
....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:COG0410 34 LLGRNGAGKTTLLKAISGLLPPRSGSIRFD 63
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-229 |
1.46e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.35 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYR-----KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN- 76
Cdd:PRK13643 2 IKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 -------LFFVPEEFDLPSVSLNDyyrslCKFYP-NF---SEKDFKEYLLKFE-IDINLKFGSSSY-----GQRKKSIIA 139
Cdd:PRK13643 82 vrkkvgvVFQFPESQLFEETVLKD-----VAFGPqNFgipKEKAEKIAAEKLEmVGLADEFWEKSPfelsgGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 140 FSLATDVPILIFDEPTNGLD----IASKNVFRDiISNFKNKIVFVTgHNVRDLVDIVDHLTIIGNNNILFSNSVSYInns 215
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDpkarIEMMQLFES-IHQSGQTVVLVT-HLMDDVADYADYVYLLEKGHIISCGTPSDV--- 231
|
250
....*....|....
gi 500096509 216 ykVKIVDKLEGEEL 229
Cdd:PRK13643 232 --FQEVDFLKAHEL 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-198 |
1.49e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 6 IDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNP-------------- 71
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkealengismvhqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 72 LNLVNLFFVPEEFDLPSVSLNDYYRSLCKFYpNFSEKDFKEylLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIF 151
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMFVDQDKMY-RDTKAIFDE--LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 500096509 152 DEPTNGLDIASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIVDHLTII 198
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERgcgIVYIS-HKMEEIFQLCDEITIL 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-159 |
1.59e-08 |
|
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: 53.69 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVF-PRNPLNLV--NLFF 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEFDLpsvslndyyrslckfYPNFS--------------------EKDFKEYLLKFEID--INLKFGSSSYGQRKKSI 137
Cdd:cd03262 81 VFQQFNL---------------FPHLTvlenitlapikvkgmskaeaEERALELLEKVGLAdkADAYPAQLSGGQQQRVA 145
|
170 180
....*....|....*....|..
gi 500096509 138 IAFSLATDVPILIFDEPTNGLD 159
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALD 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-183 |
1.68e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSY---RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN---------------S 63
Cdd:PTZ00265 382 KIQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrsK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 64 LKVFPRNPLNLVNLFFVPEEFDLPSV----SLNDYY-----------------RSLC--------------------KFY 102
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNIKYSLYSLkdleALSNYYnedgndsqenknkrnscRAKCagdlndmsnttdsneliemrKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 103 PNFSEKDF----KEYLL---------KFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDI 169
Cdd:PTZ00265 542 QTIKDSEVvdvsKKVLIhdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
250
....*....|....*..
gi 500096509 170 ISNFK---NKIVFVTGH 183
Cdd:PTZ00265 622 INNLKgneNRITIIIAH 638
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-174 |
1.72e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.99 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKP--QTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN---- 76
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPkgQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKhigi 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 LFFVPEefdlpsvslNDYYRSLCKFYPNF-------SEKDFKEYLLKFEIDINL------KFGSSSYGQRKKSIIAFSLA 143
Cdd:PRK13648 88 VFQNPD---------NQFVGSIVKYDVAFglenhavPYDEMHRRVSEALKQVDMleradyEPNALSGGQKQRVAIAGVLA 158
|
170 180 190
....*....|....*....|....*....|.
gi 500096509 144 TDVPILIFDEPTNGLDIASKNVFRDIISNFK 174
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVK 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-198 |
1.93e-08 |
|
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: 53.74 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY----RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN-- 76
Cdd:cd03258 2 IELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 ----LFFvpEEFDL---PSVSLNDYYRSLCKFYPNfSEKDFK-EYLLKFeidINLKFGSSSY------GQRKKSIIAFSL 142
Cdd:cd03258 82 rrigMIF--QHFNLlssRTVFENVALPLEIAGVPK-AEIEERvLELLEL---VGLEDKADAYpaqlsgGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 143 ATDVPILIFDEPTNGLDIASKN----VFRDIISNFKNKIVFVTgHNVRDLVDIVDHLTII 198
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQsilaLLRDINRELGLTIVLIT-HEMEVVKRICDRVAVM 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-194 |
2.16e-08 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 53.51 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYR----KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN--SLKVFPRNPLNLV- 75
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 --NLFFVPEEFDL-PS------VSLNDYYRslcKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLAT 144
Cdd:COG1136 85 rrHIGFVFQFFNLlPEltalenVALPLLLA---GVSRKERRERARELLERVGLGdrLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 145 DVPILIFDEPTNGLDiaSKN------VFRDIISNFKNKIVFVTgHNvRDLVDIVDH 194
Cdd:COG1136 162 RPKLILADEPTGNLD--SKTgeevleLLRELNRELGTTIVMVT-HD-PELAARADR 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-181 |
2.25e-08 |
|
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: 52.60 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLkvfprnplnlvnlffv 80
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 peefDLPSVSLNDYyrslckfypnfseKDFKEYLLKfeiDINLkFGSS------SYGQRKKSIIAFSLATDVPILIFDEP 154
Cdd:cd03246 65 ----DISQWDPNEL-------------GDHVGYLPQ---DDEL-FSGSiaenilSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190
....*....|....*....|....*....|
gi 500096509 155 TNGLDIASKNVFRDIISNFKNK---IVFVT 181
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAgatRIVIA 153
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-205 |
2.42e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSY---RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLkvfprnPLNLVNLF 78
Cdd:TIGR00958 478 LIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV------PLVQYDHH 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 F-------VPEEFDLPSVSLNDYYRSLCKFYP-----NFSEKDF-KEYLLKFEIDINLKFGSS----SYGQRKKSIIAFS 141
Cdd:TIGR00958 552 YlhrqvalVGQEPVLFSGSVRENIAYGLTDTPdeeimAAAKAANaHDFIMEFPNGYDTEVGEKgsqlSGGQKQRIAIARA 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500096509 142 LATDVPILIFDEPTNGLDIASKNVFRDIISnFKNKIVFVTGHnvrdlvdivdHLTIIGN-NNILF 205
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQLLQESRS-RASRTVLLIAH----------RLSTVERaDQILV 685
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-195 |
3.04e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 11 SYRKIK--VYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLL--NPLKGEVLFNSLKvFPRNpLNLVNLFFVPEEFD- 85
Cdd:COG2401 37 ELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ-FGRE-ASLIDAIGRKGDFKd 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 86 ----LPSVSLNDYYRSLCKfypnfsekdFKEYllkfeidinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLD-- 159
Cdd:COG2401 115 avelLNAVGLSDAVLWLRR---------FKEL---------------STGQKFRFRLALLLAERPKLLVIDEFCSHLDrq 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 500096509 160 ---IASKNvFRDIISNFKNKIVFVTGHNvrdlvDIVDHL 195
Cdd:COG2401 171 takRVARN-LQKLARRAGITLVVATHHY-----DVIDDL 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-223 |
3.19e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLN------PLKGEVLFNSLKVFPRNPLNLVN----LFFVPEEFdlPSV 89
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKevgmVFQQPNPF--PHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 90 SLNDYYRSLCKFYPNFSEKDFKEYL--------LKFEIDINLKFGSS--SYGQRKKSIIAFSLATDVPILIFDEPTNGLD 159
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVeeclrkvgLWKEVYDRLNSPASqlSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500096509 160 IASKNVFRDIISNFKNKIVFV-TGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINNSYKVKIVDK 223
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIViVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-160 |
3.72e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.69 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLFF- 79
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAs 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEfdlPSVSLNDYYRS---------LCKFYPNFSEKD--FKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDV 146
Cdd:PRK09536 82 VPQD---TSLSFEFDVRQvvemgrtphRSRFDTWTETDRaaVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQAT 158
|
170
....*....|....
gi 500096509 147 PILIFDEPTNGLDI 160
Cdd:PRK09536 159 PVLLLDEPTASLDI 172
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-62 |
3.87e-08 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 52.36 E-value: 3.87e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 3 IEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:COG2884 2 IRFENVSKRYPGGREALsDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN 62
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-185 |
3.99e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 52.80 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 25 FSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVlfnslkvfprnplnlvnlffvpeEFDLPSVSlndyyrslckFYPN 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-----------------------EIELDTVS----------YKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 105 FSEKDFKEYLLKFEIDINLKFGSSSY------------------------GQRKKSIIAFSLATDVPILIFDEPTNGLD- 159
Cdd:cd03237 69 YIKADYEGTVRDLLSSITKDFYTHPYfkteiakplqieqildrevpelsgGELQRVAIAACLSKDADIYLLDEPSAYLDv 148
|
170 180 190
....*....|....*....|....*....|
gi 500096509 160 ----IASKnVFRDIISNfKNKIVFVTGHNV 185
Cdd:cd03237 149 eqrlMASK-VIRRFAEN-NEKTAFVVEHDI 176
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-190 |
6.25e-08 |
|
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: 50.83 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 27 KPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNplnlvnlffvpeefdlpsvslndyyrslckfypnfs 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEE------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 107 ekdfkEYLLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISN--------FKNKIV 178
Cdd:smart00382 45 -----VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllksEKNLTV 119
|
170
....*....|..
gi 500096509 179 FVTGHNVRDLVD 190
Cdd:smart00382 120 ILTTNDEKDLGP 131
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-62 |
9.53e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 51.63 E-value: 9.53e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 1 MKIEFIDVSFSYRK----IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:COG1116 6 PALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD 71
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
33-225 |
1.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.97 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNpLNL------VNLFF-VPE------------EFDLPSVSLND 93
Cdd:PRK13637 38 LIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKK-VKLsdirkkVGLVFqYPEyqlfeetiekdiAFGPINLGLSE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 94 ------YYRSLckfypNFSEKDFKEYLLK--FEIdinlkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK-- 163
Cdd:PRK13637 117 eeienrVKRAM-----NIVGLDYEDYKDKspFEL---------SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRde 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500096509 164 --NVFRDIISNFKNKIVFVTgHNVRDLVDIVDHLTIIGNNNILFSNSVSYInnsykVKIVDKLE 225
Cdd:PRK13637 183 ilNKIKELHKEYNMTIILVS-HSMEDVAKLADRIIVMNKGKCELQGTPREV-----FKEVETLE 240
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-197 |
1.07e-07 |
|
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: 51.25 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKV--FPRNPLNLV--NL 77
Cdd:cd03292 1 IEFINVTKTYPNGTAALdGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdLRGRAIPYLrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 78 FFVPEEFDLPSvSLNDYYRslCKFYPNFSEKDFKEY---------LLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPI 148
Cdd:cd03292 81 GVVFQDFRLLP-DRNVYEN--VAFALEVTGVPPREIrkrvpaaleLVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 500096509 149 LIFDEPTNGLDIASK----NVFRDIisNFKNKIVFVTGHNvRDLVDIVDHLTI 197
Cdd:cd03292 158 LIADEPTGNLDPDTTweimNLLKKI--NKAGTTVVVATHA-KELVDTTRHRVI 207
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-159 |
1.34e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.51 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS------------LKVFPR 69
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 70 NPLNLVN--LFFVPEEFDLPS--VSLNDYYRSLCKFYpNFSEKDFKE----YLLKFEID--INLKFGSS-SYGQRKKSII 138
Cdd:PRK10619 85 NQLRLLRtrLTMVFQHFNLWShmTVLENVMEAPIQVL-GLSKQEAREravkYLAKVGIDerAQGKYPVHlSGGQQQRVSI 163
|
170 180
....*....|....*....|.
gi 500096509 139 AFSLATDVPILIFDEPTNGLD 159
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALD 184
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-193 |
1.54e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 51.37 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYR-----KIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFP------- 68
Cdd:PRK13641 1 MSIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPetgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 69 ---RNPLNLVnlFFVPEEFDLPSVSLNDyyrslCKFYP---NFSEKDFKEYLLKFEIDINLK--------FGSSSyGQRK 134
Cdd:PRK13641 81 kklRKKVSLV--FQFPEAQLFENTVLKD-----VEFGPknfGFSEDEAKEKALKWLKKVGLSedliskspFELSG-GQMR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 135 KSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFK---NKIVFVTgHNVRDLVDIVD 193
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVT-HNMDDVAEYAD 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-201 |
1.58e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 51.19 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISgLLNPLKGEV-------LFNSlKVFPRNpLNLV 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVrvegrveFFNQ-NIYERR-VNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 NL-------FFVPEEFDLPSVSLNDYYRSLCKFYPNFSEKDFKEYLLK---FEIDINLKFGSS----SYGQRKKSIIAFS 141
Cdd:PRK14258 85 RLrrqvsmvHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKdadLWDEIKHKIHKSaldlSGGQQQRLCIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500096509 142 LATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK----IVFVTgHNVRDLVDIVDHLTIIGNN 201
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRseltMVIVS-HNLHQVSRLSDFTAFFKGN 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-181 |
1.72e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 51.24 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYR-----KIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLK----------- 65
Cdd:PRK13633 5 IKCKNVSYKYEsneesTEKLALdDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 66 -----VFpRNPLNLV-------NLFFVPEEFDLPSVSLNDYYRSLCKFYPNFSEKDFKEYLLkfeidinlkfgssSYGQR 133
Cdd:PRK13633 85 nkagmVF-QNPDNQIvativeeDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLL-------------SGGQK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 500096509 134 KKSIIAFSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIVFVT 181
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRrevvNTIKELNKKYGITIILIT 202
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-211 |
2.29e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.56 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY--RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfprNPLNLVNLffv 80
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASL--- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDLPS--VSL-ND-------YYRSlcKFYPNFS-EKDFK-----EYLLKFEIDINLKFG----SSSYGQRKKSIIAF 140
Cdd:PRK11176 416 RNQVALVSqnVHLfNDtianniaYART--EQYSREQiEEAARmayamDFINKMDNGLDTVIGengvLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 141 SLATDVPILIFDEPTNGLDIASKnvfRDIISNF----KNKIVFVTGHNVR-----DLVDIVDHLTII--GNNNILFSNSV 209
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESE---RAIQAALdelqKNRTSLVIAHRLStiekaDEILVVEDGEIVerGTHAELLAQNG 570
|
..
gi 500096509 210 SY 211
Cdd:PRK11176 571 VY 572
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-159 |
2.40e-07 |
|
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: 49.95 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfprNPLNlvnlffvPE 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV---TDLP-------PK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDLPSVsLNDYyrslcKFYPNFSEKDFKEYLLKF------EID---------------INLKFGSSSYGQRKKSIIAFS 141
Cdd:cd03301 71 DRDIAMV-FQNY-----ALYPHMTVYDNIAFGLKLrkvpkdEIDervrevaellqiehlLDRKPKQLSGGQRQRVALGRA 144
|
170
....*....|....*...
gi 500096509 142 LATDVPILIFDEPTNGLD 159
Cdd:cd03301 145 IVREPKVFLMDEPLSNLD 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-163 |
2.79e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.32 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVyldlnLAFSkpqtylilGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN--LFFVPEEf 84
Cdd:PRK09700 281 DISFSVCRGEI-----LGFA--------GLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKkgMAYITES- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 85 dlpsvslndyyRSLCKFYPNFS------------------------EKDFKEYLLKFEIDINLKFGSS-------SYGQR 133
Cdd:PRK09700 347 -----------RRDNGFFPNFSiaqnmaisrslkdggykgamglfhEVDEQRTAENQRELLALKCHSVnqnitelSGGNQ 415
|
170 180 190
....*....|....*....|....*....|
gi 500096509 134 KKSIIAFSLATDVPILIFDEPTNGLDIASK 163
Cdd:PRK09700 416 QKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-62 |
3.04e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 50.87 E-value: 3.04e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLD 65
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-197 |
3.84e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLdlnlafskpqtylILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN---------L 77
Cdd:PRK11288 22 DISFDCRAGQVHA-------------LMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAagvaiiyqeL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 78 FFVPEEfdlpSVSLNDYYRSLckfyPN----FSEKDFK----EYL--LKFEIDINLKFGSSSYGQRKKSIIAFSLATDVP 147
Cdd:PRK11288 89 HLVPEM----TVAENLYLGQL----PHkggiVNRRLLNyearEQLehLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 500096509 148 ILIFDEPTNGLDI-ASKNVFRdIISNFKNK---IVFVTgHNVRDLVDIVDHLTI 197
Cdd:PRK11288 161 VIAFDEPTSSLSArEIEQLFR-VIRELRAEgrvILYVS-HRMEEIFALCDAITV 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-190 |
4.44e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.99 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVL--------FNSLK-------- 65
Cdd:PRK13644 2 IRLENVSYSYPDGTPALeNINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgidtgdFSKLQgirklvgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 66 VFPRNPLNLV------NLFFVPEEFDLPSVSLNDYY-RSLCKF----YPNFSEKdfkeyllkfeidinlkfgSSSYGQRK 134
Cdd:PRK13644 82 VFQNPETQFVgrtveeDLAFGPENLCLPPIEIRKRVdRALAEIglekYRHRSPK------------------TLSGGQGQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 135 KSIIAFSLATDVPILIFDEPTNGLDIAS-KNVFRDIIS-NFKNKIVFVTGHNVRDLVD 190
Cdd:PRK13644 144 CVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKlHEKGKTIVYITHNLEELHD 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-198 |
4.63e-07 |
|
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: 49.39 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRK---IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSlkvfprNPLNLVN-- 76
Cdd:cd03248 11 IVKFQNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG------KPISQYEhk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 -----LFFVPEEFDLPSVSLND---YYRSLCKF------YPNFSEKDF-KEYLLKFEIDINLKFGSSSYGQRKKSIIAFS 141
Cdd:cd03248 85 ylhskVSLVGQEPVLFARSLQDniaYGLQSCSFecvkeaAQKAHAHSFiSELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 142 LATDVPILIFDEPTNGLDIASKNVFRDIISNF-KNKIVFVTGHNVRdLVDIVDHLTII 198
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWpERRTVLVIAHRLS-TVERADQILVL 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-159 |
6.82e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 49.14 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGL--LNP---LKGEVLFNSLKVFPRNPLNL-- 74
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKMDVIELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 75 -VNLFF-----VPEEFDLPSVSLNDYYRSLCKFYPNFSEKdFKEYLLKFEI------DINLKFGSSSYGQRKKSIIAFSL 142
Cdd:PRK14247 83 rVQMVFqipnpIPNLSIFENVALGLKLNRLVKSKKELQER-VRWALEKAQLwdevkdRLDAPAGKLSGGQQQRLCIARAL 161
|
170
....*....|....*..
gi 500096509 143 ATDVPILIFDEPTNGLD 159
Cdd:PRK14247 162 AFQPEVLLADEPTANLD 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-62 |
8.49e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 49.30 E-value: 8.49e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG 63
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-210 |
8.57e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.87 E-value: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 15 IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISG--LLNPLKGEVLFNSLKVFPRNPLNLVNL-----FFVPEEfdLP 87
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLgiflaFQYPIE--IP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 88 SVSLNDY----YRSLCKFYpNFSEKD---FKEYLL-KFEI----------DINLKFgssSYGQRKKS-IIAFSLaTDVPI 148
Cdd:CHL00131 98 GVSNADFlrlaYNSKRKFQ-GLPELDpleFLEIINeKLKLvgmdpsflsrNVNEGF---SGGEKKRNeILQMAL-LDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 149 LIFDEPTNGLDIASKNVFRDIISNFKNK---IVFVTgHNVRDLVDIV-DHLTIIGNNNILFSNSVS 210
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSensIILIT-HYQRLLDYIKpDYVHVMQNGKIIKTGDAE 237
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-203 |
9.75e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 49.31 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfPRNPLNLVNLFFV 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDLpsvslndyYRSLCKF--------------YPNFSEKDFKEYLLkFEIdINL-----KFGSS-SYGQRKKSIIAF 140
Cdd:PRK10851 80 FQHYAL--------FRHMTVFdniafgltvlprreRPNAAAIKAKVTQL-LEM-VQLahladRYPAQlSGGQKQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 141 SLATDVPILIFDEPTNGLDIASKNVFRDIISN----FKNKIVFVTgHNVRDLVDIVDHLTIIGNNNI 203
Cdd:PRK10851 150 ALAVEPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVT-HDQEEAMEVADRVVVMSQGNI 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-212 |
1.03e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.03 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDlNLAFSKP--QTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNlfFV 80
Cdd:PRK13652 4 IETRDLCYSYSGSKEALN-NINFIAPrnSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK--FV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFDLPSVSLndyyrslckFYPNFsEKD---------FKEYLLKFEIDINLK-FGSSSY----------GQRKKSIIAF 140
Cdd:PRK13652 81 GLVFQNPDDQI---------FSPTV-EQDiafgpinlgLDEETVAHRVSSALHmLGLEELrdrvphhlsgGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 141 SLATDVPILIFDEPTNGLD-IASKNVF---RDIISNFKNKIVFVTgHNVRDLVDIVDHLTIIGNNNILFSNSVSYI 212
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDpQGVKELIdflNDLPETYGMTVIFST-HQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
33-205 |
1.29e-06 |
|
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: 47.91 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSlKVFPrnPLNLvNLFFVPEEfdlpSVSLNDYYRslCKFYpNFSEKDFKE 112
Cdd:cd03220 53 LIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSS--LLGL-GGGFNPEL----TGRENIYLN--GRLL-GLSRKEIDE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 113 YL---LKF-EI--DINLKFGSSSYGQrkKSIIAFSLATDVP--ILIFDEPTNGLDIA----SKNVFRDIISNFKnKIVFV 180
Cdd:cd03220 122 KIdeiIEFsELgdFIDLPVKTYSSGM--KARLAFAIATALEpdILLIDEVLAVGDAAfqekCQRRLRELLKQGK-TVILV 198
|
170 180
....*....|....*....|....*
gi 500096509 181 TgHNVRDLVDIVDHLTIIGNNNILF 205
Cdd:cd03220 199 S-HDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-180 |
1.38e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISG--LLNplKGEVLFNS-LKVF------PRNPLNLVnlF-FVPEEFDLPSVSLNDYYRSLCKFY 102
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGevLLD--DGRIIYEQdLIVArlqqdpPRNVEGTV--YdFVAEGIEEQAEYLKRYHDISHLVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 103 PNFSEKDF----------------------KEYLLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDI 160
Cdd:PRK11147 110 TDPSEKNLnelaklqeqldhhnlwqlenriNEVLAQLGLDPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
170 180
....*....|....*....|
gi 500096509 161 ASKNVFRDIISNFKNKIVFV 180
Cdd:PRK11147 190 ETIEWLEGFLKTFQGSIIFI 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
33-198 |
1.40e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPL--------------NLVNLFFVPEefdlpSVSLndYYRSL 98
Cdd:COG3845 36 LLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaialgigmvhqhfMLVPNLTVAE-----NIVL--GLEPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 99 CKFYPNFSE--KDFKEYLLKFEIDINL--KFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGL-DIASKNVFRdIISNF 173
Cdd:COG3845 109 KGGRLDRKAarARIRELSERYGLDVDPdaKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILRRL 187
|
170 180
....*....|....*....|....*...
gi 500096509 174 KNK---IVFVTgHNVRDLVDIVDHLTII 198
Cdd:COG3845 188 AAEgksIIFIT-HKLREVMAIADRVTVL 214
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-198 |
1.41e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.19 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY--RKIKVYldlNLAFS-KP-QTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfprNPLNLV--- 75
Cdd:PRK13657 335 VEFDDVSFSYdnSRQGVE---DVSFEaKPgQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI---RTVTRAslr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 -NLFFVPEEFDLPSVSLNDYYRsLCKfyPNFSEKDFKEYL-------------LKFEIDINLKFGSSSYGQRKKSIIAFS 141
Cdd:PRK13657 409 rNIAVVFQDAGLFNRSIEDNIR-VGR--PDATDEEMRAAAeraqahdfierkpDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500096509 142 LATDVPILIFDEPTNGLDIASKNVFRDIISNF-KNKIVFVTGH---NVR--DLVDIVDHLTII 198
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELmKGRTTFIIAHrlsTVRnaDRILVFDNGRVV 548
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-164 |
1.63e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.04 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAfsKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS---LKVFP-RNPLNLV--- 75
Cdd:PRK10771 2 LKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdhTTTPPsRRPVSMLfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 -NLF---FVPEEFDL---PSVSLNDYYR-SLCKFYPNFSEKDFKEYLLkfeidinlkfGSSSYGQRKKSIIAFSLATDVP 147
Cdd:PRK10771 80 nNLFshlTVAQNIGLglnPGLKLNAAQReKLHAIARQMGIEDLLARLP----------GQLSGGQRQRVALARCLVREQP 149
|
170
....*....|....*..
gi 500096509 148 ILIFDEPTNGLDIASKN 164
Cdd:PRK10771 150 ILLLDEPFSALDPALRQ 166
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-200 |
2.22e-06 |
|
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: 47.08 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSY-----RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-SLKVFPRNPLnLVN 76
Cdd:cd03250 1 ISVEDASFTWdsgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPgSIAYVSQEPW-IQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 -------LFFvpEEFDlpsvslNDYYRS---LCKFypnfsEKDFKeyLLKF----EI---DINLkfgssSYGQRKKSIIA 139
Cdd:cd03250 80 gtireniLFG--KPFD------EERYEKvikACAL-----EPDLE--ILPDgdltEIgekGINL-----SGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500096509 140 FSLATDVPILIFDEPTNGLDIA-SKNVFRDIISNF--KNKIVFVTGHNVrDLVDIVDHLTIIGN 200
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLllNNKTRILVTHQL-QLLPHADQIVVLDN 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
7-161 |
2.28e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.86 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN-------SLKVFPRNplnlvnLFF 79
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDaqpleswSSKAFARK------VAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEfdLPS---------VSLNDY--YRSLCKFYPNFSEKDFKEYLLkfeidINLK------FGSSSYGQRKKSIIAFSL 142
Cdd:PRK10575 90 LPQQ--LPAaegmtvrelVAIGRYpwHGALGRFGAADREKVEEAISL-----VGLKplahrlVDSLSGGERQRAWIAMLV 162
|
170
....*....|....*....
gi 500096509 143 ATDVPILIFDEPTNGLDIA 161
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIA 181
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-153 |
2.31e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRKIKVYLD-LNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNLF-- 78
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFsa 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 79 -FV----------PEEFDlPSVSLNDYYRSLCKFYPNFSEKDFKEYLLKFeidinlkfgssSYGQRKKSIIAFSLATDVP 147
Cdd:PRK10522 402 vFTdfhlfdqllgPEGKP-ANPALVEKWLERLKMAHKLELEDGRISNLKL-----------SKGQKKRLALLLALAEERD 469
|
....*.
gi 500096509 148 ILIFDE 153
Cdd:PRK10522 470 ILLLDE 475
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-204 |
3.46e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLD-LNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLF--NSLKVFPRNPLNL---VN 76
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKgINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkgEPIKYDKKSLLEVrktVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 77 LFFVPEEFDL--PSVSLNDYYRSL-CKFYPNFSEKDFKEYLLK-----FEidiNLKFGSSSYGQRKKSIIAFSLATDVPI 148
Cdd:PRK13639 82 IVFQNPDDQLfaPTVEEDVAFGPLnLGLSKEEVEKRVKEALKAvgmegFE---NKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 149 LIFDEPTNGLDI--ASK--NVFRDIisNFKNKIVFVTGHNVrDLVDI-VDHLTIIGNNNIL 204
Cdd:PRK13639 159 IVLDEPTSGLDPmgASQimKLLYDL--NKEGITIIISTHDV-DLVPVyADKVYVMSDGKII 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
7-181 |
3.57e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 47.08 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLIS--GLLNP---LKGEVLFNSLKVF-PRNplNLVNL--- 77
Cdd:PRK14239 10 DLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNIYsPRT--DTVDLrke 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 78 ----FFVPEEFDLpSVSLNDYYRSLCKfypnfSEKDfkEYLLKFEIDINLKfGSS----------------SYGQRKKSI 137
Cdd:PRK14239 88 igmvFQQPNPFPM-SIYENVVYGLRLK-----GIKD--KQVLDEAVEKSLK-GASiwdevkdrlhdsalglSGGQQQRVC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 500096509 138 IAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK--IVFVT 181
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDytMLLVT 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-198 |
4.31e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 35 GKNGMGKTTLLKLISGLLnP---LKGEVLFNSLKVFPRN--------------PLNLV-------NLFFVPEEfdLPSVS 90
Cdd:PRK13549 38 GENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNirdteragiaiihqELALVkelsvleNIFLGNEI--TPGGI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 91 LND---YYRSlckfypnfsEKDFKEylLKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFR 167
Cdd:PRK13549 115 MDYdamYLRA---------QKLLAQ--LKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLL 183
|
170 180 190
....*....|....*....|....*....|....
gi 500096509 168 DIISNFKNK---IVFVTgHNVRDLVDIVDHLTII 198
Cdd:PRK13549 184 DIIRDLKAHgiaCIYIS-HKLNEVKAISDTICVI 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-62 |
4.42e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.34 E-value: 4.42e-06
10 20 30
....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDAGEVLWQ 61
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-159 |
4.57e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 46.62 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVF-PRNPLNLV------ 75
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdPKVDERLIrqeagm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 -----NLFfvPEEFDLPSVSlndyyrslckFYPNFSEKDFKEYLLKFEIDINLKFGSS----------SYGQRKKSIIAF 140
Cdd:PRK09493 82 vfqqfYLF--PHLTALENVM----------FGPLRVRGASKEEAEKQARELLAKVGLAerahhypselSGGQQQRVAIAR 149
|
170
....*....|....*....
gi 500096509 141 SLATDVPILIFDEPTNGLD 159
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALD 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-185 |
5.00e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFN---SLKvfprnPLNLVNLFFVPEEFDLPSVS--LNDYYrslckFYPNFSE 107
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkiSYK-----PQYIKPDYDGTVEDLLRSITddLGSSY-----YKSEIIK 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 108 KDFKEYLLKFEIDiNLkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDI-----ASKnVFRDIISNfKNKIVFVTG 182
Cdd:PRK13409 440 PLQLERLLDKNVK-DL-----SGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlaVAK-AIRRIAEE-REATALVVD 511
|
...
gi 500096509 183 HNV 185
Cdd:PRK13409 512 HDI 514
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-159 |
5.48e-06 |
|
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: 46.46 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFP----RNPLNLV--- 75
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphKRPVNTVfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 -NLFfvpeefdlPSVSLND---YYRSLCKFYPNFSEKDFKEYL--LKFEIDINLKFGSSSYGQRKKSIIAFSLATDVPIL 149
Cdd:cd03300 81 yALF--------PHLTVFEniaFGLRLKKLPKAEIKERVAEALdlVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170
....*....|
gi 500096509 150 IFDEPTNGLD 159
Cdd:cd03300 153 LLDEPLGALD 162
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-190 |
5.48e-06 |
|
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: 46.25 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRKikvylDL-----NLAFS-KPQTYL-ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVfPRNPLNL 74
Cdd:cd03369 6 EIEVENLSVRYAP-----DLppvlkNVSFKvKAGEKIgIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI-STIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 75 V--NLFFVPEEFDLPSVSLndyyRSLCKFYPNFSEKDFKEYLLKFEIDINLkfgssSYGQRKKSIIAFSLATDVPILIFD 152
Cdd:cd03369 80 LrsSLTIIPQDPTLFSGTI----RSNLDPFDEYSDEEIYGALRVSEGGLNL-----SQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 500096509 153 EPTNGLDIASKNVFRDII-SNFKNKIVFVTGHNVRDLVD 190
Cdd:cd03369 151 EATASIDYATDALIQKTIrEEFTNSTILTIAHRLRTIID 189
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-185 |
6.40e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.26 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTylILGKNGMGKTTLLKLISGLLNPLKGEVLfnslkvfpRNPlnLVNLFFVPE 82
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILT--LLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RNG--KLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFDL-PSVSLNdyYRSLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLD 159
Cdd:PRK09544 75 KLYLdTTLPLT--VNRFLRLRPGTKKEDILPALKRVQAGhlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180
....*....|....*....|....*....
gi 500096509 160 IASKNVFRDIISNFKNKI---VFVTGHNV 185
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELdcaVLMVSHDL 181
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
8.25e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 46.16 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRKIKVYLDLNLafSKPQTYLILGKNGMGKTTLLKLISGLLNPLKG-----EVLFNSLKVFPR------ 69
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNI--HHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiELLGRTVQREGRlardir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 70 ----------NPLNLVNLFFVPEEFDLPSVSLNDYYRSLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSI 137
Cdd:PRK09984 83 ksrantgyifQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVhfAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 138 IAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK---IVFVTGHNVRDLVDIVDHLTIIGNNNILFSNSVSYINN 214
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDN 242
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-196 |
9.42e-06 |
|
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: 45.80 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN----------------------SLKVFPR-----N-- 70
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgrditglpphriarlgiartfqNPRLFPEltvleNvl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 71 --PLNLVNLFFVPEEFDLPSVSLndyyrslckfypnfSEKDFKE---YLLKFeidINLKF------GSSSYGQRKKSIIA 139
Cdd:COG0411 102 vaAHARLGRGLLAALLRLPRARR--------------EEREAREraeELLER---VGLADradepaGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 500096509 140 FSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK----IVFVtGHNVrDLV-DIVDHLT 196
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgitILLI-EHDM-DLVmGLADRIV 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-204 |
1.07e-05 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 46.18 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNL-----VNLFFVPEEFDL-PSVSLND 93
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrrKKIAMVFQSFALmPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 94 yYRSLCKFYPNFSEKDFKEYLLKFEIDINLKFGSSSY------GQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFR 167
Cdd:PRK10070 126 -NTAFGMELAGINAEERREKALDALRQVGLENYAHSYpdelsgGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500096509 168 DIISNFKNK----IVFVTgHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:PRK10070 205 DELVKLQAKhqrtIVFIS-HDLDEAMRIGDRIAIMQNGEVV 244
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-159 |
1.17e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.98 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSL---KVFP-RNPLNLV--------------NLFFVP 81
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlsHVPPyQRPINMMfqsyalfphmtveqNIAFGL 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500096509 82 EEFDLPSVSLNDYYRSLCKFYpnfsekdfkeYLLKFEidiNLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLD 159
Cdd:PRK11607 117 KQDKLPKAEIASRVNEMLGLV----------HMQEFA---KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
8-161 |
1.34e-05 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.36 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 8 VSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVL--------FNSLKVFPRNPLnLVNLFF 79
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWldgehiqhYASKEVARRIGL-LAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 VPEEFDLPS-VSLNDY-YRSLCKFYPNFSEKDFKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPT 155
Cdd:PRK10253 92 TPGDITVQElVARGRYpHQPLFTRWRKEDEEAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
....*.
gi 500096509 156 NGLDIA 161
Cdd:PRK10253 172 TWLDIS 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
38-163 |
1.49e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.78 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 38 GMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN--LFFVPEE-------FDLP------SVSLNDYYRSLckFY 102
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRagIAYVPEDrkgeglvLDLSirenitLASLDRLSRGG--LL 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500096509 103 PNFSEKDF-KEYLLKFEI---DINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK 163
Cdd:COG1129 366 DRRRERALaEEYIKRLRIktpSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAK 430
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-173 |
1.67e-05 |
|
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: 45.70 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKiKVYLDlNLAFSKPQTYL--ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSlkvfprnplnLVNLFFV 80
Cdd:TIGR03719 323 IEAENLTKAFGD-KLLID-DLSFKLPPGGIvgVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE----------TVKLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEEFD---------------LPSVSLNDY---YRSLC-KFypNFSEKDFKEyllkfeidinlKFGSSSYGQRKKSIIAFS 141
Cdd:TIGR03719 391 DQSRDaldpnktvweeisggLDIIKLGKReipSRAYVgRF--NFKGSDQQK-----------KVGQLSGGERNRVHLAKT 457
|
170 180 190
....*....|....*....|....*....|..
gi 500096509 142 LATDVPILIFDEPTNGLDIASKNVFRDIISNF 173
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF 489
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-62 |
1.89e-05 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 44.76 E-value: 1.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:PRK13548 7 NLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLN 62
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-196 |
2.27e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNP-----------------LKGEVLFNSLKVFPRNPLNLVnlfFVPEEFDLPSVSLNDYY 95
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPnlgdyeeepswdevlkrFRGTELQNYFKKLYNGEIKVV---HKPQYVDLIPKVFKGKV 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 96 RSLCKfypNFSEKD-FKEYLLKFEID--INLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK-NVFRDIIS 171
Cdd:PRK13409 181 RELLK---KVDERGkLDEVVERLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRlNVARLIRE 257
|
170 180
....*....|....*....|....*
gi 500096509 172 NFKNKIVFVTGHnvrDLVdIVDHLT 196
Cdd:PRK13409 258 LAEGKYVLVVEH---DLA-VLDYLA 278
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-174 |
2.36e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVyldlnLAFSkpqtylilGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLN------------- 73
Cdd:PRK10762 270 DVSFTLRKGEI-----LGVS--------GLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyisedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 74 ----LVNLFFVPEEFDLPSVslndyyRSLCKFYPNFSEKDFKEYLLKFEIDINLK-------FGSSSYGQRKKSIIAFSL 142
Cdd:PRK10762 337 krdgLVLGMSVKENMSLTAL------RYFSRAGGSLKHADEQQAVSDFIRLFNIKtpsmeqaIGLLSGGNQQKVAIARGL 410
|
170 180 190
....*....|....*....|....*....|..
gi 500096509 143 ATDVPILIFDEPTNGLDIASKNVFRDIISNFK 174
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFK 442
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-61 |
3.55e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 43.93 E-value: 3.55e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLF 61
Cdd:PRK10247 12 NVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF 66
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-62 |
4.52e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 44.17 E-value: 4.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD 74
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-170 |
6.57e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 43.55 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNlvnlffvpe 82
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 efdlpsvslndyyRSLC------KFYPNFSEKDFKEYLLKF------EIDINLK----------FGSS-----SYGQRKK 135
Cdd:PRK11432 78 -------------RDICmvfqsyALFPHMSLGENVGYGLKMlgvpkeERKQRVKealelvdlagFEDRyvdqiSGGQQQR 144
|
170 180 190
....*....|....*....|....*....|....*
gi 500096509 136 SIIAFSLATDVPILIFDEPTNGLDIASKNVFRDII 170
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-181 |
7.44e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 43.29 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGL--LNP---LKGEV-LFN----SLKVFP---R 69
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEearVEGEVrLFGrniySPDVDPievR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 70 NPLNLVnlFFVPEEFD----LPSVSLNDYYRSLCKFYPNFSEK---DFKEYLLKFEID--INLKFGSSSYGQRKKSIIAF 140
Cdd:PRK14267 85 REVGMV--FQYPNPFPhltiYDNVAIGVKLNGLVKSKKELDERvewALKKAALWDEVKdrLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 500096509 141 SLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK--IVFVT 181
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEytIVLVT 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-203 |
7.75e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISG-----LLNPL--------KGEVLF-------- 61
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgYSNDLtlfgrrrgSGETIWdikkhigy 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 62 --NSLKVFPRNPLNLVNlffvpeefdlpsVSLNDYYRSLcKFYPNFSEKDFK---EYLLKFEIDINLK---FGSSSYGQR 133
Cdd:PRK10938 341 vsSSLHLDYRVSTSVRN------------VILSGFFDSI-GIYQAVSDRQQKlaqQWLDILGIDKRTAdapFHSLSWGQQ 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500096509 134 KKSIIAFSLATDVPILIFDEPTNGLDIASKNVFR---DI-ISNFKNKIVFVTgHNVRDLVDIVDH-LTIIGNNNI 203
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRrfvDVlISEGETQLLFVS-HHAEDAPACITHrLEFVPDGDI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-59 |
7.88e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.57 E-value: 7.88e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 500096509 3 IEFIDVSFSYRKiKVYLDlNLAFSKPQTYL--ILGKNGMGKTTLLKLISGLLNPLKGEV 59
Cdd:PRK11819 325 IEAENLSKSFGD-RLLID-DLSFSLPPGGIvgIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
29-62 |
8.18e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 8.18e-05
10 20 30
....*....|....*....|....*....|....
gi 500096509 29 QTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:PRK15112 40 QTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID 73
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-204 |
8.72e-05 |
|
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: 43.64 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 29 QTYLILGKNGMGKTTLLKLISGLLNPLKGEV----------------------------LFNSLKVFPRNPLnLVNL--- 77
Cdd:TIGR03269 311 EIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdewvdmtkpgpdgrgrakryigiLHQEYDLYPHRTV-LDNLtea 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 78 --FFVPEEFD-------LPSVSlndyyrslckfypnFSEKDFKEYLLKFEIDInlkfgssSYGQRKKSIIAFSLATDVPI 148
Cdd:TIGR03269 390 igLELPDELArmkavitLKMVG--------------FDEEKAEEILDKYPDEL-------SEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 500096509 149 LIFDEPTNGLDIASKNVFRDIISNFK---NKIVFVTGHNVRDLVDIVDHLTIIGNNNIL 204
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-198 |
9.05e-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: 43.07 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFsYRKIKvylDLNLAFSKPQTYLIlGKNGMGKTTLLKLISGLLNPLKGEVL----FNSLKVFPRNPL---- 72
Cdd:COG3593 1 MKLEKIKIKN-FRSIK---DLSIELSDDLTVLV-GENNSGKSSILEALRLLLGPSSSRKFdeedFYLGDDPDLPEIeiel 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 73 -------NLVNLFFVPEEFDLPSVSLNDYYRSLCKFYPNFSEKdFKEYLLKFEIDINLKFGSSSYGQRK----------- 134
Cdd:COG3593 76 tfgsllsRLLRLLLKEEDKEELEEALEELNEELKEALKALNEL-LSEYLKELLDGLDLELELSLDELEDllkslslried 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 135 -------------KSIIAFSL---------ATDVPILIFDEPTNGLDIASKNVFRDIISNF--KNKIVFVTGHNVrDLVD 190
Cdd:COG3593 155 gkelpldrlgsgfQRLILLALlsalaelkrAPANPILLIEEPEAHLHPQAQRRLLKLLKELseKPNQVIITTHSP-HLLS 233
|
....*...
gi 500096509 191 IVDHLTII 198
Cdd:COG3593 234 EVPLENIR 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-204 |
9.34e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 9.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRK--IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS--------------LKV 66
Cdd:PLN03232 1235 IKFEDVHLRYRPglPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrrvLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 67 FPRNPLnlvnLFFVPEEFDL-PSVSLNDyyrslCKFYPNFSEKDFKEYLLK--FEIDINLKFGSSSY--GQRKKSIIAFS 141
Cdd:PLN03232 1315 IPQSPV----LFSGTVRFNIdPFSEHND-----ADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFsvGQRQLLSLARA 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500096509 142 LATDVPILIFDEPTNGLDIASKNVF-RDIISNFKNKIVFVTGHNVRDLVDiVDHLTIIGNNNIL 204
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIqRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-59 |
1.06e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEV 59
Cdd:PRK15064 324 NLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-159 |
1.35e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 42.11 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 12 YRKIKVYLDL--NLAFSKPQTYL--ILGKNGMGKTTLLKLISGLLNPLKGEVLF-----NSLKVFPRNPLNLVNLFFVpE 82
Cdd:PRK11629 15 YQEGSVQTDVlhNVSFSIGEGEMmaIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngqpmSKLSSAAKAELRNQKLGFI-Y 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFD--LPSVS-LNDYYRSLC--KFYPNFSEKDFKEYLLKFEIDINLKFGSS--SYGQRKKSIIAFSLATDVPILIFDEPT 155
Cdd:PRK11629 94 QFHhlLPDFTaLENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSelSGGERQRVAIARALVNNPRLVLADEPT 173
|
....
gi 500096509 156 NGLD 159
Cdd:PRK11629 174 GNLD 177
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-208 |
2.05e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.09 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQ---TYLIlGKNGMGKTTLLKLISGLLNP--------------LKGEVLFNSLK 65
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRgswTALI-GHNGSGKSTISKLINGLLLPddnpnskitvdgitLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 66 ----VFpRNPLNLV-------NLFFVPEEFDLPSVSLNDYYRSLckfypnFSEKDFKEYllkfeidINLKFGSSSYGQRK 134
Cdd:PRK13640 85 kvgiVF-QNPDNQFvgatvgdDVAFGLENRAVPRPEMIKIVRDV------LADVGMLDY-------IDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 135 KSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNFKNK---IVFVTGHNVrDLVDIVDHLTIIGNNNILFSNS 208
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnlTVISITHDI-DEANMADQVLVLDDGKLLAQGS 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-159 |
2.08e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.00 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 1 MKIEFIDVSFSYRK-----IKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFnslkVFPRNPLNLV 75
Cdd:PRK13651 1 MQIKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEW----IFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 76 NLFFvpeEFDLPSVSLNDYYRSLCKFYPNFSEK-----DFKEYLLkFE--IDINLKFGSSSY------------------ 130
Cdd:PRK13651 77 TKEK---EKVLEKLVIQKTRFKKIKKIKEIRRRvgvvfQFAEYQL-FEqtIEKDIIFGPVSMgvskeeakkraakyielv 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 500096509 131 ----------------GQRKKSIIAFSLATDVPILIFDEPTNGLD 159
Cdd:PRK13651 153 gldesylqrspfelsgGQKRRVALAGILAMEPDFLVFDEPTAGLD 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-172 |
2.35e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 5 FIDVSFSYRKIKVyldLNLAfskpqtylilGKNGMGKTTLLKLISGLLNPLKGEVLF-----NSLKVFPRNPLNLVNLff 79
Cdd:PRK15439 279 FRNISLEVRAGEI---LGLA----------GVVGAGRTELAETLYGLRPARGGRIMLngkeiNALSTAQRLARGLVYL-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 80 vPEE-------FDLPsVSLNDYyrSLCKFYPNFSEKDFKE--YLLKFEIDINLKF-------GSSSYGQRKKSIIAFSLA 143
Cdd:PRK15439 344 -PEDrqssglyLDAP-LAWNVC--ALTHNRRGFWIKPAREnaVLERYRRALNIKFnhaeqaaRTLSGGNQQKVLIAKCLE 419
|
170 180
....*....|....*....|....*....
gi 500096509 144 TDVPILIFDEPTNGLDIASKNVFRDIISN 172
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRS 448
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-185 |
2.44e-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: 42.08 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFN---SLKvfprnPLNLVNLFFVPEEFDLPSVSLNDYYRSlcKFYPNFSEKD 109
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkiSYK-----PQYISPDYDGTVEEFLRSANTDDFGSS--YYKTEIIKPL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 110 FKEYLLKFEIDiNLkfgssSYGQRKKSIIAFSLATDVPILIFDEPTNGLDI-----ASKnVFRDIISNfKNKIVFVTGHN 184
Cdd:COG1245 444 GLEKLLDKNVK-DL-----SGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlaVAK-AIRRFAEN-RGKTAMVVDHD 515
|
.
gi 500096509 185 V 185
Cdd:COG1245 516 I 516
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
123-163 |
2.59e-04 |
|
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: 42.12 E-value: 2.59e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 500096509 123 LKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK 163
Cdd:TIGR02633 399 LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
129-210 |
2.62e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 41.96 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 129 SYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK----NVFRDIISnfKNKIVFVTGHN-VRDLVDIVDHLTIIGNNNI 203
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAysvvQVLKGLAQ--KGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
....*..
gi 500096509 204 LFSNSVS 210
Cdd:TIGR00955 246 AYLGSPD 252
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
123-163 |
2.82e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 2.82e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 500096509 123 LKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK 163
Cdd:PRK13549 401 LAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
7-63 |
4.15e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.60 E-value: 4.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNS 63
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG 72
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-62 |
5.67e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 40.55 E-value: 5.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500096509 3 IEFIDVSFSY----RKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD 65
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-181 |
6.43e-04 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 40.01 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSlkVFPRNP----LNLVNLFFVPEEFDLPSVsLNDYY 95
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--KNESEPsfeaTRSRNRYSVAYAAQKPWL-LNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 96 RSLCKFYPNFSEKDFKEYL----LKFEIDInLKFGSS----------SYGQRKKSIIAFSLATDVPILIFDEPTNGLDI- 160
Cdd:cd03290 96 EENITFGSPFNKQRYKAVTdacsLQPDIDL-LPFGDQteigerginlSGGQRQRICVARALYQNTNIVFLDDPFSALDIh 174
|
170 180
....*....|....*....|....*
gi 500096509 161 ASKNVFRDIISNF----KNKIVFVT 181
Cdd:cd03290 175 LSDHLMQEGILKFlqddKRTLVLVT 199
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-114 |
7.00e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 40.56 E-value: 7.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKvfprnplnlvNLFFVPEEFDLPSVSLNDyyrSLC 99
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----------RVLFLPQRPYLPLGTLRE---ALL 447
|
90
....*....|....*....
gi 500096509 100 kfYPN----FSEKDFKEYL 114
Cdd:COG4178 448 --YPAtaeaFSDAELREAL 464
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-66 |
9.21e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 9.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 500096509 16 KVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKV 66
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNI 64
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-198 |
9.21e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 39.87 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 7 DVSFSYRKIKVYLDlNLAFSKPQTYL--ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVNlfFVP--E 82
Cdd:PRK15056 11 DVTVTWRNGHTALR-DASFTVPGGSIaaLVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVA--YVPqsE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 83 EFD--LPS-----VSLNDYYRSLCKFYPNFSEKDFKEYLLKfEIDI----NLKFGSSSYGQRKKSIIAFSLATDVPILIF 151
Cdd:PRK15056 88 EVDwsFPVlvedvVMMGRYGHMGWLRRAKKRDRQIVTAALA-RVDMvefrHRQIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 500096509 152 DEPTNGLDIASKNVFRDIISNFKN--KIVFVTGHNVRDLVDIVDHLTII 198
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
33-54 |
1.05e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.15 E-value: 1.05e-03
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-66 |
1.27e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 39.30 E-value: 1.27e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKV 66
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV 65
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
33-62 |
1.34e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 39.30 E-value: 1.34e-03
10 20 30
....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPPDSGSILID 66
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
33-61 |
1.80e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 38.75 E-value: 1.80e-03
10 20
....*....|....*....|....*....
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLF 61
Cdd:PRK11701 37 IVGESGSGKTTLLNALSARLAPDAGEVHY 65
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-170 |
2.26e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 39.12 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 38 GMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRNPLNLVN--LFFVPEE------FDLPSVSLN-------DYYRSLCKFY 102
Cdd:PRK11288 289 GAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRagIMLCPEDrkaegiIPVHSVADNinisarrHHLRAGCLIN 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 103 PNFSEKDFKEYLLKFEI---DINLKFGSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDII 170
Cdd:PRK11288 369 NRWEAENADRFIRSLNIktpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVI 439
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
32-205 |
2.29e-03 |
|
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: 38.40 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 32 LILGKNGMGKTTLLKLISGLLNP---LKGEVLFNSL------KVFPRNplnlvnLFFVPEEfDLpsvslndyyrslckFY 102
Cdd:cd03233 37 LVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIpykefaEKYPGE------IIYVSEE-DV--------------HF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 103 PNFSEKDFKEYLLKFEIDINLKfGSSSyGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIV 178
Cdd:cd03233 96 PTLTVRETLDFALRCKGNEFVR-GISG-GERKRVSIAEALVSRASVLCWDNSTRGLDSSTAleilKCIRTMADVLKTTTF 173
|
170 180
....*....|....*....|....*..
gi 500096509 179 FVTGHNVRDLVDIVDHLTIIGNNNILF 205
Cdd:cd03233 174 VSLYQASDEIYDLFDKVLVLYEGRQIY 200
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-173 |
2.42e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 38.38 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 29 QTYLIlGKNGMGKTTLLKLISGLLnPLKGEVLFN--SLKVFPRNPLNLVNLFFVPEEfdlPSVSLNDYYRSLCKFYPNFS 106
Cdd:PRK03695 24 ILHLV-GPNGAGKSTLLARMAGLL-PGSGSIQFAgqPLEAWSAAELARHRAYLSQQQ---TPPFAMPVFQYLTLHQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 107 EKDFKEYLLKFEID-INL--KFGSS----SYG--QRKKSIIAF-----SLATDVPILIFDEPTNGLDIASKNVFRDIISN 172
Cdd:PRK03695 99 RTEAVASALNEVAEaLGLddKLGRSvnqlSGGewQRVRLAAVVlqvwpDINPAGQLLLLDEPMNSLDVAQQAALDRLLSE 178
|
.
gi 500096509 173 F 173
Cdd:PRK03695 179 L 179
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
126-200 |
2.61e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 2.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 126 GSSSYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDIISNF--KNKIVFVTGHNVRDLVDIVDHLTIIGN 200
Cdd:PRK10982 390 GSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELakKDKGIIIISSEMPELLGITDRILVMSN 466
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-60 |
2.64e-03 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 38.93 E-value: 2.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRKIKVYL-DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVL 60
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLqNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIR 399
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
129-159 |
3.07e-03 |
|
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: 37.61 E-value: 3.07e-03
10 20 30
....*....|....*....|....*....|..
gi 500096509 129 SYGQRKKSIIAFSLATDvPILIF-DEPTNGLD 159
Cdd:cd03232 110 SVEQRKRLTIGVELAAK-PSILFlDEPTSGLD 140
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-59 |
3.15e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 38.07 E-value: 3.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 2 KIEFIDVSFSYRKIKVYLDLNLAFS--KPQTYLILGKNGMGKTTLLKLISGLLNPLKGEV 59
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSvyEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI 64
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-208 |
3.65e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 37.94 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 3 IEFIDVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKV--FPRNPLNLVNLFFV 80
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 81 PEE---FDLPSVSLNdyyRSLCKFypnFSEKdfKEYLLKFEIDINL----------KFGSSSYGQRKKSIIAFSLATDVP 147
Cdd:PRK11614 86 PEGrrvFSRMTVEEN---LAMGGF---FAER--DQFQERIKWVYELfprlherriqRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500096509 148 ILIFDEPTNGL-DIASKNVFrDIISNFKNK--IVFVTGHNVRDLVDIVDHLTIIGNNNILFSNS 208
Cdd:PRK11614 158 LLLLDEPSLGLaPIIIQQIF-DTIEQLREQgmTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-60 |
4.29e-03 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 37.73 E-value: 4.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 500096509 7 DVSFSYRKIKVYLDLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVL 60
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL 70
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
25-194 |
4.34e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 37.59 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 25 FSKPQTyLILGKNGMGKTTLLklisgllnplkgEVLFNSLkvFPRNPLNLVNLFFVPeefDLPSVSLNDYYRSLckfypN 104
Cdd:cd03240 20 FFSPLT-LIVGQNGAGKTTII------------EALKYAL--TGELPPNSKGGAHDP---KLIREGEVRAQVKL-----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500096509 105 FSEKDFKEYLLKFEIDI--NLKF--------------GSSSYGQRKKSIIAFSLA------TDVPILIFDEPTNGLDIAS 162
Cdd:cd03240 77 FENANGKKYTITRSLAIleNVIFchqgesnwplldmrGRCSGGEKVLASLIIRLAlaetfgSNCGILALDEPTTNLDEEN 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 500096509 163 -KNVFRDIISNFKNKIVF---VTGHnVRDLVDIVDH 194
Cdd:cd03240 157 iEESLAEIIEERKSQKNFqliVITH-DEELVDAADH 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
129-192 |
5.31e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 38.15 E-value: 5.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 129 SYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIVFVTgHN---VRDLVDIV 192
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLRELQQELNMGLLFIT-HNlsiVRKLADRV 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-62 |
5.36e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 37.55 E-value: 5.36e-03
10 20 30
....*....|....*....|....*....|
gi 500096509 33 ILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLN 58
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-70 |
5.68e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 37.40 E-value: 5.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500096509 3 IEFIDVSFSYRKIKVYLDLN-LAFS-KPQTYL-ILGKNGMGKTTLLKLISGLLNPLKGEVLFNSLKVFPRN 70
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNdVSFHvKQGEWLsIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN 75
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
129-190 |
6.41e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.20 E-value: 6.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500096509 129 SYGQRKKSIIAFSLATDVPILIFDEPTNGLDIASKNVFRDII-SNFKNKIVFVTGHNVRDLVD 190
Cdd:cd03288 158 SVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVmTAFADRTVVTIAHRVSTILD 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
131-190 |
6.71e-03 |
|
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: 37.34 E-value: 6.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 500096509 131 GQRKKSIIAFSLATDVPILIFDEPTNGLDIASK----NVFRDIISNFKNKIVFVTgHN---VRDLVD 190
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQaqilNLLKDLQRELGLAILFIT-HDlgvVAEIAD 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-62 |
7.59e-03 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 36.97 E-value: 7.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 500096509 20 DLNLAFSKPQTYLILGKNGMGKTTLLKLISGLLNPLKGEVLFN 62
Cdd:PRK10419 30 NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWR 72
|
|
| |
