|
Name |
Accession |
Description |
Interval |
E-value |
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-273 |
4.51e-173 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 477.63 E-value: 4.51e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 11 TPQRLKRGIPLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEARED 90
Cdd:PRK11247 3 NTARLNQGTPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 TRLMFQDSRLLPWKRVIDNVGLGLRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:PRK11247 83 TRLMFQDARLLPWKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVELPRPRSRGSARLAALEAEVLNRV 250
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPRPRRRGSARLAELEAEVLQRV 242
|
250 260
....*....|....*....|...
gi 15598638 251 LAQPelppqpepvSPLPTQLRWA 273
Cdd:PRK11247 243 MSRG---------ESEPTRLRWA 256
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
21-250 |
6.72e-110 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 317.80 E-value: 6.72e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF----GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQ 96
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:COG1116 88 EPALLPWLTVLDNVALGLelrgvpKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIED--GEIGLDLPVELPRPRS---RGSARLAALEAE 245
Cdd:COG1116 168 ALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEEIDVDLPRPRDrelRTSPEFAALRAE 247
|
....*
gi 15598638 246 VLNRV 250
Cdd:COG1116 248 ILDLL 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
21-228 |
7.76e-95 |
|
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: 278.20 E-value: 7.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG----EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQ 96
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:cd03293 81 QDALLPWLTVLDNVALGLelqgvpKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIE--DGEIGLDLPVEL 228
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSarPGRIVAEVEVDL 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-220 |
6.25e-80 |
|
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: 240.11 E-value: 6.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMFQD 97
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:cd03259 81 YALFPHLTVAENIAFGLKlrgvpkAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
21-220 |
2.20e-73 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 228.06 E-value: 2.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG---SAALAEAReDTRLMFQ 96
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRiLLDGrdvTGLPPEKR-NVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:COG3842 85 DYALFPHLTVAENVAFGLRmrgvpkAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG3842 165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
21-220 |
2.19e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 213.75 E-value: 2.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG----EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR---- 92
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 -----LMFQDSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPR 161
Cdd:COG1136 85 rrhigFVFQFFNLLPELTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 162 LLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDvSEAVAVADRVILIEDGEI 220
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
21-220 |
2.85e-67 |
|
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: 208.11 E-value: 2.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG----EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAR 88
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvdgtdiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 89 EDT-RLMFQDSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPR 161
Cdd:cd03255 81 RRHiGFVFQSFNLLPDLTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 162 LLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVsEAVAVADRVILIEDGEI 220
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-219 |
2.15e-65 |
|
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: 202.03 E-value: 2.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALA-------EAREDTRL 93
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdledelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPWKRVIDNVGLGlrgdwrakalqalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG----------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 174 ALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
21-220 |
7.21e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 203.77 E-value: 7.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMFQD 97
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvTDLPPKDRNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:COG3839 84 YALYPHMTVYENIAFPLKlrkvpkAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG3839 164 LDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
23-220 |
8.31e-64 |
|
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: 199.82 E-value: 8.31e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDTRLM 94
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdgqditgLSEKELYELRRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGLR--GDW-----RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:COG1127 88 FQGGALFDSLTVFENVAFPLRehTDLseaeiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 168 PLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
23-220 |
2.00e-62 |
|
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: 196.18 E-value: 2.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDTRLM 94
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisgLSEAELYRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGLR-------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLRehtrlseEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 168 PLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-214 |
4.07e-62 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 196.62 E-value: 4.07e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG----EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQ 96
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:COG4525 84 KDALLPWLNVLDNVAFGLRlrgvpkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVIL 214
Cdd:COG4525 164 ALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVV 207
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-220 |
6.26e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 195.21 E-value: 6.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-------LLAGSAALAEAREDTRL 93
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTitvdgedLTDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPWKRVIDNVGLGL-------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPikvkkmsKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 167 EPLGALD-ALTRiEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1126 162 EPTSALDpELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-220 |
8.82e-62 |
|
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: 194.76 E-value: 8.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMFQD 97
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdiTNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:cd03300 81 YALFPHLTVFENIAFGLRlkklpkAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
23-220 |
3.59e-61 |
|
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: 192.36 E-value: 3.59e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRG-------ELLAGSAALAEAREDTRLMF 95
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglKLTDDKKNINELRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRLLPWKRVIDNVGLGL-------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:cd03262 83 QQFNLFPHLTVLENITLAPikvkgmsKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598638 169 LGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-220 |
3.65e-61 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 196.91 E-value: 3.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAALA--EAREdtR---LM 94
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRiVLNGRDLFTnlPPRE--RrvgFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:COG1118 81 FQHYALFPHMTVAENIAFGLRvrppskAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598638 169 LGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-234 |
4.52e-61 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 192.68 E-value: 4.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQDSRLLPWKRVIDNVGLGL- 114
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 115 -------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGL 187
Cdd:TIGR01184 81 rvlpdlsKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 188 WREHGFTVLLVTHDVSEAVAVADRVILIEDG---EIGLDLPVELPRPRSR 234
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGpaaNIGQILEVPFPRPRDR 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
23-220 |
1.09e-59 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 193.63 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG---SAALAEAReDTRLMFQDS 98
Cdd:PRK09452 17 LRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRiMLDGqdiTHVPAENR-HVNTVFQSY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 99 RLLPWKRVIDNVGLGLRGDWRAKA------LQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:PRK09452 96 ALFPHMTVFENVAFGLRMQKTPAAeitprvMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 173 DALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK09452 176 DYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-220 |
5.63e-59 |
|
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: 186.69 E-value: 5.63e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMFQD 97
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdvTDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:cd03301 81 YALYPHMTVYDNIAFGLklrkvpKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
21-227 |
1.22e-58 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 187.19 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF-GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDT 91
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvdgqdvtaLRGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSRLLPWKRVIDNVGLGLRGDW--------------RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALI 157
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRLGRTstwrsllglfppedRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 158 HEPRLLLLDEPLGALD-ALTRIEMQQLIEgLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG3638 163 QEPKLILADEPVASLDpKTARQVMDLLRR-IAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-220 |
5.68e-58 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 184.88 E-value: 5.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG---SAALAEAREDTRLMFQ 96
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEvRVLGedvARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGL--GLRG----DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:COG1131 81 EPALYPDLTVRENLRFfaRLYGlprkEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1131 161 GLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
21-220 |
8.00e-58 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 184.56 E-value: 8.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGERE----VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRL--- 93
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARArlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 ------MFQDSRLLPWKRVIDNVGLGL----RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLL 163
Cdd:COG4181 89 arhvgfVFQSFQLLPTLTALENVMLPLelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAIL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 164 LLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAvAVADRVILIEDGEI 220
Cdd:COG4181 169 FADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRL 224
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
21-220 |
1.00e-57 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 187.94 E-value: 1.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMFQD 97
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGrdiTRLPPQKRDYGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLknrgmgRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
21-220 |
4.67e-57 |
|
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: 190.50 E-value: 4.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF-----GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEA 87
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDTRLMFQD--SRLLPWKRVIDNVGLGLR-------GDWRAKALQALRAVGL-AERANEWPAALSGGQKQRVALARALI 157
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRlhgllsrAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598638 158 HEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-227 |
5.50e-57 |
|
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: 182.15 E-value: 5.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVA-RRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG-----SAALAEAREDTRLM 94
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkditKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDsrllPW-----KRVIDNVG-----LGLRGDW-RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLL 163
Cdd:COG1122 81 FQN----PDdqlfaPTVEEDVAfgpenLGLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598638 164 LLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
21-227 |
2.04e-56 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 180.72 E-value: 2.04e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGERevLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR---LMFQD 97
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERpvsMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:COG3840 80 NNLFPHLTVAQNIGLGLRpglkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTA 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-230 |
2.03e-55 |
|
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: 178.84 E-value: 2.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGE----REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-----AGSAALAEAREDT 91
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTfdgrpVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSR--LLPWKRVIDNVGLGLR----GDWRAKALQALRAVGLAER-ANEWPAALSGGQKQRVALARALIHEPRLLL 164
Cdd:COG1124 82 QMVFQDPYasLHPRHTVDRILAEPLRihglPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 165 LDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVELPR 230
Cdd:COG1124 162 LDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-220 |
2.80e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 174.62 E-value: 2.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRLMF 95
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMpppewRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRLLPwKRVIDNV----GLGLRGDWRAKALQALRAVGLAERANEWPAA-LSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:COG4619 81 QEPALWG-GTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
31-219 |
3.24e-54 |
|
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: 174.58 E-value: 3.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG----SAALAEAREDTRLMFQDSRL-LPWK 104
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvLVDGkdltKLSLKELRRKVGLVFQNPDDqFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:cd03225 92 TVEEEVAFGLenlglpEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRR 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598638 179 EMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:cd03225 172 ELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-220 |
5.35e-54 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 174.47 E-value: 5.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRF-GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLM------- 94
Cdd:COG2884 4 FENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrrigv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 -FQDSRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:COG2884 84 vFQDFRLLPDRTVYENVALPLRvtgksrKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 168 PLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-220 |
6.61e-54 |
|
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: 172.20 E-value: 6.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR----LMFQ 96
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrrigYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVglglrgdwrakalqalravglaeranewpaALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 177 RIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03230 131 RREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-234 |
4.43e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 172.58 E-value: 4.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLM-------F 95
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeagmvF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRLLPWKRVIDNVGLG---LRG----DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:PRK09493 84 QQFYLFPHLTALENVMFGplrVRGaskeEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 169 LGALDALTRIE----MQQLIeglwrEHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLD-LPVEL----PRPRSR 234
Cdd:PRK09493 164 TSALDPELRHEvlkvMQDLA-----EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDgDPQVLiknpPSQRLQ 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-234 |
6.10e-53 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 175.68 E-value: 6.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA---REDTRLMFQD 97
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiqQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLRGDWRAKA------LQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEerkqrvKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI-GLDLPVELPR-PRSR 234
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKImQIGSPQELYRqPASR 231
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
26-220 |
2.36e-52 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 170.75 E-value: 2.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 26 VARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTRL--MFQDSRLLP 102
Cdd:TIGR00968 6 ISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIrLNGQDATRVHARDRKIgfVFQHYALFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 103 WKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:TIGR00968 86 HLTVRDNIAFGLeirkhpKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 177 RIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-220 |
3.98e-52 |
|
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: 170.61 E-value: 3.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE--AREDTR---LMF 95
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARriaYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRLLPWKRVIDNVGLG----------LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLL 165
Cdd:COG1120 82 QEPPAPFGLTVRELVALGryphlglfgrPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 166 DEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
21-225 |
4.21e-52 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 170.06 E-value: 4.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGE-REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDT 91
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinkLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSRLLPWKRVIDNVGLGLRGDW--------------RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALI 157
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 158 HEPRLLLLDEPLGALD-ALTRIEMqQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLP 225
Cdd:cd03256 161 QQPKLILADEPVASLDpASSRQVM-DLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-220 |
4.87e-52 |
|
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: 169.83 E-value: 4.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 24 RGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS--AALAEARE-DTRLMFQDSRL 100
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedATDVPVQErNVGFVFQHYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVGLGLR----------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:cd03296 86 FRHMTVFDNVAFGLRvkprserppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03296 166 ALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-220 |
6.20e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.88 E-value: 6.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQdSRL 100
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQ-RAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWK---RVIDNVGLGLRGDW----------RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:COG1121 86 VDWDfpiTVRDVVLMGRYGRRglfrrpsradREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 168 PLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1121 166 PFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-234 |
6.62e-52 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 172.96 E-value: 6.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 25 GVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGS-AALAEARE-DTRLMFQDSRLL 101
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrFHGTdVSRLHARDrKVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 PWKRVIDNVGLGLR----------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:PRK10851 87 RHMTVFDNIAFGLTvlprrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI-GLDLPVELPR-PRSR 234
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIeQAGTPDQVWRePATR 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
21-218 |
9.67e-52 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 169.50 E-value: 9.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQDSRL 100
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:PRK11248 82 LPWRNVQDNVAFGLqlagveKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 175 LTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
28-220 |
1.35e-51 |
|
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: 168.45 E-value: 1.35e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 28 RRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-------LLAGSAALAEARE-DTRLMFQD-- 97
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgkdLLKLSRRLRKIRRkEIQMVFQDpm 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLR------GDWRAK--ALQALRAVGLAE-RANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:cd03257 93 SSLNPRMTIGEQIAEPLRihgklsKKEARKeaVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598638 169 LGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03257 173 TSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
23-220 |
1.27e-50 |
|
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: 166.22 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGER----EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA--------GSAALAEARED 90
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdgtdltllSGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 TRLMFQDSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLL 164
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLeiagvpKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 165 LDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
36-220 |
5.81e-50 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 168.74 E-value: 5.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDTRLM-FQDSRLLPWKRV 106
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLidgeditkLSKKELRELRRKKMSMvFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEM 180
Cdd:COG4175 123 LENVAFGLeiqgvpKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREM 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598638 181 Q-QLIEgLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4175 203 QdELLE-LQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRI 242
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-220 |
2.06e-49 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 163.97 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 26 VARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS--------AALAEAREDTRLM-FQ 96
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrKELRELRRKKISMvFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:cd03294 110 SFALLPHRTVLENVAFGLevqgvpRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
23-220 |
4.11e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 165.25 E-value: 4.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRF----GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEARED 90
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltaLSERELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 TRLMFQDSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLL 164
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENVALPLeiagvpKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 165 LDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-220 |
3.77e-48 |
|
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: 160.16 E-value: 3.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGERE-VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRLM 94
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGL--GLRGdW-----RAKALQALRAVGL--AERANEWPAALSGGQKQRVALARALIHEPRLLLL 165
Cdd:cd03295 81 IQQIGLFPHMTVEENIALvpKLLK-WpkekiRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 166 DEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-220 |
8.22e-48 |
|
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: 158.04 E-value: 8.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 29 RFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMFQDSRLLPWKR 105
Cdd:cd03298 7 RFSYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdvTAAPPADRPVSMLFQENNLFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGLRGDWRAKALQ------ALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:cd03298 87 VEQNVGLGLSPGLKLTAEDrqaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598638 180 MQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
51-220 |
1.25e-47 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 161.12 E-value: 1.25e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 51 IVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR---LMFQDSRLLPWKRVIDNVGLGLRGD------WRAK 121
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhinMVFQSYALFPHMTVEENVAFGLKMRkvpraeIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 122 ALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHD 201
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*....
gi 15598638 202 VSEAVAVADRVILIEDGEI 220
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGKI 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
21-227 |
1.82e-47 |
|
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: 165.08 E-value: 1.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF--GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPS---RGELLAGSAALAEAREDTR--- 92
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 --LMFQD--SRLLPWkRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:COG1123 85 igMVFQDpmTQLNPV-TVGDQIAEALenlglsRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
21-220 |
1.92e-46 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 154.79 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGE----REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAR 88
Cdd:TIGR02982 2 ISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKvlgqelhgASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 89 EDTRLMFQDSRLLPWKRVIDNVGLGL-------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPR 161
Cdd:TIGR02982 82 RRIGYIFQAHNLLGFLTARQNVQMALelqpnlsYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 162 LLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDvSEAVAVADRVILIEDGEI 220
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
31-219 |
2.09e-46 |
|
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: 152.92 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE-AREDTR----LMFQDSRLLPwKR 105
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRkniaYVPQDPFLFS-GT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVglglrgdwrakalqalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIE 185
Cdd:cd03228 92 IRENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|....
gi 15598638 186 GLwrEHGFTVLLVTHDVSeAVAVADRVILIEDGE 219
Cdd:cd03228 141 AL--AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-220 |
2.46e-46 |
|
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: 154.65 E-value: 2.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGL-----DQPSRGE-LLAGSAALAEAREDTRL- 93
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEvLLDGKDIYDLDVDVLELr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 -----MFQDSRLLPwKRVIDNVGLGLR--GDWRAKAL-----QALRAVGLAERANE--WPAALSGGQKQRVALARALIHE 159
Cdd:cd03260 81 rrvgmVFQKPNPFP-GSIYDNVAYGLRlhGIKLKEELderveEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 160 PRLLLLDEPLGALDALTRIEMQQLIEGLWREHgfTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-220 |
4.12e-46 |
|
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: 152.59 E-value: 4.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 22 ALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE--AREDTRLMfqdsr 99
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlsPKELARKI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 llpwkrvidnvglglrgdwrAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:cd03214 76 --------------------AYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598638 180 MQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
29-215 |
4.19e-46 |
|
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: 153.84 E-value: 4.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 29 RFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQdSRLLPWK---R 105
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQ-RRSIDRDfpiS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGLRG----------DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:cd03235 87 VRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598638 176 TRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILI 215
Cdd:cd03235 167 TQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
23-215 |
4.91e-46 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 153.54 E-value: 4.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL---------LAGSAALAEAREDTRL 93
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVylngqetppLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLkykklsKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 168 PLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDvSEAVAVADRVILI 215
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
23-220 |
5.27e-46 |
|
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: 154.63 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR----LMFQDS 98
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqigVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 99 RLLPWKRVIDNVGL-----GLRGDWRAKALQAL-RAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:COG4555 84 GLYDRLTVRENIRYfaelyGLFDEELKKRIEELiELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 173 DALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4555 164 DVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
31-219 |
6.53e-46 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 153.17 E-value: 6.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSA-------ALAEAREDTRLMFQDSRLLP 102
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQvRIAGEDvnrlrgrQLPLLRRRIGVVFQDFRLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 103 WKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:TIGR02673 93 DRTVYENVALPLEvrgkkeREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598638 177 RIEMQQLIEGLWReHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:TIGR02673 173 SERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-220 |
7.47e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 157.50 E-value: 7.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR---LMFQDSR 99
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERgvgMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 LLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK11000 86 LYPHLSVAENMSFGLKlagakkEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 174 ALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11000 166 AALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
38-220 |
1.36e-45 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 156.80 E-value: 1.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 38 DIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRL---------MFQDSRLLPWKRVID 108
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLpphrrrigyVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLRGDWRAKALQALRAV----GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLI 184
Cdd:COG4148 97 NLLYGRKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598638 185 EGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4148 177 ERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRV 212
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-220 |
1.40e-45 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 155.25 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGE-REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGsaalaearEDTRLM------ 94
Cdd:COG1125 4 FENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRiLIDG--------EDIRDLdpvelr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 ------FQDSRLLPWKRVIDNVGL--GLRGdW-----RAKALQALRAVGL--AERANEWPAALSGGQKQRVALARALIHE 159
Cdd:COG1125 76 rrigyvIQQIGLFPHMTVAENIATvpRLLG-WdkeriRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 160 PRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRI 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
38-220 |
2.86e-45 |
|
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: 151.68 E-value: 2.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 38 DIDLLVPaGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAR-------EDTR--LMFQDSRLLPWKRVID 108
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinlppQQRKigLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLRGDWRAKALQALRAV----GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLI 184
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELldllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598638 185 EGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03297 175 KQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
23-219 |
4.57e-45 |
|
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: 149.32 E-value: 4.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaearedtRLMFQDSRLLP 102
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI--------------LIDGKDIAKLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 103 WKRVIDNVGLglrgdwrakALQalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQ 182
Cdd:cd00267 68 LEELRRRIGY---------VPQ-----------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLE 121
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598638 183 LIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:cd00267 122 LLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
21-223 |
5.94e-45 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 151.68 E-value: 5.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGE-REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDT 91
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlegtditkLRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSRLLPWKRVIDNV---GLGLRGDWR-----------AKALQALRAVGLAERANEWPAALSGGQKQRVALARALI 157
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVlhgRLGYKPTWRsllgrfseedkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 158 HEPRLLLLDEPLGALD-ALTRIEMQQLIEgLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLD 223
Cdd:TIGR02315 162 QQPDLILADEPIASLDpKTSKQVMDYLKR-INKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-220 |
8.08e-45 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 154.19 E-value: 8.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRF----GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA--------GSAALAEARED 90
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltalSEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 TRLMFQDSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLL 164
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLelagtpKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 165 LDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
31-220 |
5.98e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 149.89 E-value: 5.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL------AGSAALAEAREDTRLMFQ--DSRLLP 102
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldtLDEENLWEIRKKVGMVFQnpDNQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 103 wKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:TIGR04520 93 -ATVEDDVAFGLenlgvpREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 177 RIEMQQLIEGLWREHGFTVLLVTHDVSEAVaVADRVILIEDGEI 220
Cdd:TIGR04520 172 RKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKI 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-220 |
1.72e-43 |
|
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: 156.92 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGERE--VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRL 93
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIdpaslRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPwKRVIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRL 162
Cdd:COG2274 554 VLQDVFLFS-GTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLwrEHGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLS-TIRLADRIIVLDKGRI 687
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-220 |
1.98e-43 |
|
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: 154.92 E-value: 1.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 9 GGTPQRLKRGIPLALRGVA-RRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA 87
Cdd:COG4988 325 GTAPLPAAGPPSIELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDTR-----LMFQDSRLLPWkRVIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVA 151
Cdd:COG4988 405 DPASWrrqiaWVPQNPYLFAG-TIRENLRLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 152 LARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHgfTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-220 |
2.86e-43 |
|
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: 147.10 E-value: 2.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREvLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGS--AALAEAREDTRLMFQD 97
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKiLLNGKdiTNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLRGDWRAKA------LQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKeierkvLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-237 |
3.75e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 150.76 E-value: 3.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR---LMFQD 97
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpinMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLRGDWRAKALQALRA------VGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVnemlglVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGE-IGLDLPVEL-PRPRSRGSA 237
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKfVQIGEPEEIyEHPTTRYSA 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
36-220 |
5.48e-43 |
|
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: 145.63 E-value: 5.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-AGSA-------ALAEAREDTRLMFQDSRLLPWKRVI 107
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvNGQDvsdlrgrAIPYLRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQ 181
Cdd:cd03292 97 ENVAFALEvtgvppREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIM 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598638 182 QLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03292 177 NLLKKI-NKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-223 |
5.63e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 147.60 E-value: 5.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSA--------ALAEAREDTRLMFQdsrlLPW 103
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditakkkkKLKDLRKKVGLVFQ----FPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 104 KR-----VIDNVGLGLR------GDWRAKALQALRAVGL----AERAnewPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:TIGR04521 93 HQlfeetVYKDIAFGPKnlglseEEAEERVKEALELVGLdeeyLERS---PFELSGGQMRRVAIAGVLAMEPEVLILDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 169 LGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLD 223
Cdd:TIGR04521 170 TAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-220 |
1.14e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 145.93 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGS----------AALAEAREDT 91
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLnIAGHqfdfsqkpseKAIRLLRQKV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSRLLPWKRVIDNVG------LGL-RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLL 164
Cdd:COG4161 85 GMVFQQYNLWPHLTVMENLIeapckvLGLsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 165 LDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4161 165 FDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
40-220 |
2.93e-42 |
|
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: 143.85 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 40 DLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMFQDSRLLPWKRVIDNVGLGLRG 116
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDqshTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 117 DWRAKALQ------ALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWRE 190
Cdd:TIGR01277 98 GLKLNAEQqekvvdAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|
gi 15598638 191 HGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
34-220 |
3.26e-42 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 144.03 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDTR-LMFQDSRLLPWK 104
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLfngqslskLSSNERAKLRNKKLgFIYQFHHLLPDF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:TIGR02211 99 TALENVAMPLligkksVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLWREHGFTVLLVTHDVsEAVAVADRVILIEDGEI 220
Cdd:TIGR02211 179 IIFDLMLELNRELNTSFLVVTHDL-ELAKKLDRVLEMKDGQL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
40-225 |
6.58e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 143.57 E-value: 6.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 40 DLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGS--AALAEAREDTRLMFQDSRLLPWKRVIDNVGLG--- 113
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLtLNGQdhTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGlnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 114 ---LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWRE 190
Cdd:PRK10771 99 glkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178
|
170 180 190
....*....|....*....|....*....|....*
gi 15598638 191 HGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLP 225
Cdd:PRK10771 179 RQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
36-220 |
3.06e-41 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 145.22 E-value: 3.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR---LMFQDSRLLPWKRVIDNVGL 112
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRgiaYVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 113 GL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEG 186
Cdd:NF040840 96 GLklrkvpKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175
|
170 180 190
....*....|....*....|....*....|....
gi 15598638 187 LWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRL 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-220 |
4.06e-41 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 144.99 E-value: 4.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF-GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSA---ALAEAREDTRLMFQ 96
Cdd:PRK11650 4 LKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRvvnELEPADRDIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:PRK11650 84 NYALYPHMSVRENMAYGLkirgmpKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-227 |
2.60e-40 |
|
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: 139.83 E-value: 2.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA------GSAALAEARE----- 89
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDVWELRKriglv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 90 DTRLMFQDSRLLPWKRVI-----DNVGLGLRGDW--RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:COG1119 84 SPALQLRFPRDETVLDVVlsgffDSIGLYREPTDeqRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKE 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-220 |
5.11e-40 |
|
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: 138.27 E-value: 5.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 25 GVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTR---LMFQDSRL 100
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAtVAGHDVVREPREVRRrigIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVGL-----GLRGD-WRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:cd03265 85 DDELTGWENLYIharlyGVPGAeRRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 175 LTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
21-217 |
5.59e-40 |
|
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: 137.61 E-value: 5.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR----LMFQ 96
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGL-----GLRGDwRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:COG4133 83 ADGLKPELTVRENLRFwaalyGLRAD-REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 172 LDALTRIEMQQLIEGlWREHGFTVLLVTHDvsEAVAVADRVILIED 217
Cdd:COG4133 162 LDAAGVALLAELIAA-HLARGGAVLLTTHQ--PLELAAARVLDLGD 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
21-213 |
7.96e-40 |
|
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: 140.57 E-value: 7.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF----GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQP---SRGELL--------AGSAALA 85
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgedllkLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 86 EAR-EDTRLMFQD--SRLLPWKRVIDNVGLGLR-------GDWRAKALQALRAVGL---AERANEWPAALSGGQKQRVAL 152
Cdd:COG0444 82 KIRgREIQMIFQDpmTSLNPVMTVGDQIAEPLRihgglskAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 153 ARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVI 213
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-220 |
8.41e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.61 E-value: 8.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSA----------ALAEAREDT 91
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGNHfdfsktpsdkAIRELRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSRLLPWKRVIDNV------GLGL-RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLL 164
Cdd:PRK11124 85 GMVFQQYNLWPHLTVQQNLieapcrVLGLsKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 165 LDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11124 165 FDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-250 |
1.33e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 145.64 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF--GER--EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAG-------SAALAE-A 87
Cdd:PRK10535 5 LELKDIRRSYpsGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYrVAGqdvatldADALAQlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDTRLMFQDSRLLPWKRVIDNV-------GLGlRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEP 160
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVevpavyaGLE-RKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 161 RLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAvAVADRVILIEDGEIGLDlpvelprPRSRGSARLA 240
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVRN-------PPAQEKVNVA 234
|
250
....*....|
gi 15598638 241 ALEAEVLNRV 250
Cdd:PRK10535 235 GGTEPVVNTA 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-220 |
1.84e-39 |
|
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: 137.86 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGS--AALAeAREDTRL---- 93
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRiLFDGRdiTGLP-PHRIARLgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPWKRVIDNVGLGLRG---------------------DWRAKALQALRAVGLAERANEWPAALSGGQKQRVAL 152
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHArlgrgllaallrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 153 ARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-217 |
2.02e-39 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 136.46 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAG-LDQP--SRGELLAGSAAL----AEAREdTRL 93
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLtalpAEQRR-IGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPWKRVIDNVGLGL-----RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALpptigRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 169 LGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAvADRVILIED 217
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
19-220 |
2.18e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 137.62 E-value: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 19 IPLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL------------AE 86
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 87 AREDTRL------MFQDSRLLPWKRVIDNVG------LGL-RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALA 153
Cdd:COG4598 87 RRQLQRIrtrlgmVFQSFNLWSHMTVLENVIeapvhvLGRpKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 154 RALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-220 |
6.88e-39 |
|
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: 135.64 E-value: 6.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALA--EAREDTRL----M 94
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglPPHEIARLgigrT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGL----RGDW------------RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIH 158
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAqartGSGLllararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598638 159 EPRLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
34-205 |
7.40e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 135.71 E-value: 7.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAR-EDTRLMFQDSRLLPWK 104
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpmskLSSAAKAELRnQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK11629 103 TALENVAMPLligkkkPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|....*..
gi 15598638 179 EMQQLIEGLWREHGFTVLLVTHDVSEA 205
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
31-220 |
1.34e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 142.23 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG-----SAALAEAREDTRLMFQDSRLLPwKR 105
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdirDLTLESLRRQIGVVPQDTFLFS-GT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:COG1132 430 IRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDT 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 175 LTRIEMQQLIEGLWREHgfTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:COG1132 510 ETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRI 552
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-226 |
3.73e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 134.81 E-value: 3.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 25 GVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL---------LAGSAALAeAREDTRLMF 95
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplakLNRAQRKA-FRRDIQMVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDS--RLLPWKRVIDNVGLGLR-------GDWRAKALQALRAVGLA-ERANEWPAALSGGQKQRVALARALIHEPRLLLL 165
Cdd:PRK10419 96 QDSisAVNPRKTVREIIREPLRhllsldkAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 166 DEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPV 226
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-213 |
1.45e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 134.86 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 24 RGVARRfgEREVLK---DIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDTR 92
Cdd:COG4608 21 GGLFGR--TVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILfdgqditgLSGRELRPLRRRMQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQD--SRLLPWKRVIDNVGLGL-------RGDWRAKALQALRAVGL-AERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:COG4608 99 MVFQDpyASLNPRMTVGDIIAEPLrihglasKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 163 LLLDEPLGALDAltRIEMQ--QLIEGLWREHGFTVLLVTHDVSEAVAVADRVI 213
Cdd:COG4608 179 IVCDEPVSALDV--SIQAQvlNLLEDLQDELGLTYLFISHDLSVVRHISDRVA 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
31-221 |
2.38e-37 |
|
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: 130.84 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG--SAALAEAREDTRLMFQDS-RLLPWKRVI 107
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNgkPIKAKERRKSIGYVMQDVdYQLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNVGLGLR--GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDaltRIEMQQ--- 182
Cdd:cd03226 91 EELLLGLKelDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YKNMERvge 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598638 183 LIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEIG 221
Cdd:cd03226 168 LIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-220 |
2.58e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 132.18 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS-------------AALAEARE 89
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqkGLIRQLRQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 90 DTRLMFQDSRLLPWKRVIDNVGLG-------LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:PRK11264 86 HVGFVFQNFNLFPHRTVLENIIEGpvivkgePKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLWREHGfTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-225 |
2.99e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.83 E-value: 2.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRLMFQ--DSRLLPwK 104
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdvRRQVGMVFQnpDNQFVG-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK13635 98 TVQDDVAFGLenigvpREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 179 EMQQLIEGLWREHGFTVLLVTHDVSEAvAVADRVILIEDGE-------------------IGLDLP 225
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEileegtpeeifksghmlqeIGLDVP 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-220 |
4.02e-37 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 137.51 E-value: 4.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 28 RRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLdQPSRGELL--------AGSAALAEAREDTRLMFQD-- 97
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRfdgqdldgLSRRALRPLRRRMQVVFQDpf 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLR--------GDWRAKALQALRAVGL-AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:COG4172 373 GSLSPRMTVGQIIAEGLRvhgpglsaAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598638 169 LGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
8-220 |
1.78e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 133.62 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 8 LGGTPQRLKRGIP--LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALA 85
Cdd:PRK10070 14 FGEHPQRAFKYIEqgLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 86 -----EAREDTR----LMFQDSRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRV 150
Cdd:PRK10070 94 kisdaELREVRRkkiaMVFQSFALMPHMTVLDNTAFGMElaginaEERREKALDALRQVGLENYAHSYPDELSGGMRQRV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 151 ALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10070 174 GLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-220 |
1.81e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 130.66 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDTRLM 94
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipaMSRSRLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGLRGD-------WRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:PRK11831 90 FQSGALFTDMNVFDNVAYPLREHtqlpaplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 168 PLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11831 170 PFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-220 |
7.21e-36 |
|
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: 127.33 E-value: 7.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAALAEAREDTRL--MFQD 97
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEiTFDGKSYQKNIEALRRIgaLIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLG--LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:cd03268 81 PGFYPNLTARENLRLLarLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03268 161 GIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
38-220 |
9.79e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 130.62 E-value: 9.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 38 DIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRL---------MFQDSRLLPWKRVID 108
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppekrrigyVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGL---RGDWRAKALQALRAV-GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLI 184
Cdd:TIGR02142 95 NLRYGMkraRPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 15598638 185 EGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-168 |
1.17e-35 |
|
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: 124.68 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAALAEAREDTR----LMFQDSRLLPWKRVIDNV 110
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTiLLDGQDLTDDERKSLRkeigYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 111 GLGLR---------GDWRAKALQALRAVGLAER-ANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:pfam00005 81 RLGLLlkglskrekDARAEEALEKLGLGDLADRpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-220 |
2.21e-35 |
|
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: 125.86 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA-GSAALAEAREDTRLMFQDSR 99
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 LLPWKRVIDN-VGLG-LRG----DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:cd03269 81 LYPKMKVIDQlVYLAqLKGlkkeEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 174 ALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03269 161 PVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-220 |
2.42e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.20 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE--AREDTRL---MF 95
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAELARRravLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRL-LPWkRVIDNVGLGL----RGDWRAKAL--QALRAVGLAERANEWPAALSGGQKQRVALARALI------HEPRL 162
Cdd:PRK13548 83 QHSSLsFPF-TVEEVVAMGRaphgLSRAEDDALvaAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-220 |
2.74e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.15 E-value: 2.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG-------SAALAEAREdtr 92
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEvRLNGrplaawsPWELARRRA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQDSRL-LPWkRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARAL--IHE---- 159
Cdd:COG4559 79 VLPQHSSLaFPF-TVEEVVALGRaphgssAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEpvdg 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 160 -PRLLLLDEPLGALDaltrIEMQQLIEGLWRE---HGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4559 158 gPRWLFLDEPTSALD----LAHQHAVLRLARQlarRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-220 |
5.07e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 126.30 E-value: 5.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLR------------------LLAGLDqpsrgeLLAGSA 82
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndlipgarvegeiLLDGED------IYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 83 ALAEARedTRLM--FQDSRLLPwKRVIDNVGLGLR--GdWRAKAL------QALRAVGL----AERANEWPAALSGGQKQ 148
Cdd:COG1117 86 DVVELR--RRVGmvFQKPNPFP-KSIYDNVAYGLRlhG-IKSKSEldeiveESLRKAALwdevKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598638 149 RVALARALIHEPRLLLLDEPLGALD--ALTRIEmqQLIEGLwREHgFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDpiSTAKIE--ELILEL-KKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-225 |
5.79e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 127.06 E-value: 5.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRL---------MFQ--DSRL 100
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLkplrkkvgiVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVID------NVGLGlRGDWRAKALQALRAVGLAERANEW-PAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK13634 99 FEETVEKDicfgpmNFGVS-EEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 174 ALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDG-------------------EIGLDLP 225
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGtvflqgtpreifadpdeleAIGLDLP 248
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-220 |
1.17e-34 |
|
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: 131.04 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 10 GTPQRLKRGIPLALRGVARRF--GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA 87
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDTR-----LMFQDSRLLPwKRVIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVA 151
Cdd:COG4987 403 DEDDLrrriaVVPQRPHLFD-TTLRENLRLARPDATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 152 LARALIHEPRLLLLDEPLGALDALTRiemQQLIEGLWRE-HGFTVLLVTHDvSEAVAVADRVILIEDGEI 220
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATE---QALLADLLEAlAGRTVLLITHR-LAGLERMDRILVLEDGRI 547
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-220 |
2.76e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 124.70 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEARED---------- 90
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 ------TRL--MFQDSRLLPWKRVIDNVG------LGL-RGDWRAKALQALRAVGLAERAN-EWPAALSGGQKQRVALAR 154
Cdd:PRK10619 86 qlrllrTRLtmVFQHFNLWSHMTVLENVMeapiqvLGLsKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 155 ALIHEPRLLLLDEPLGALDA-----LTRIeMQQLIeglwrEHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPelvgeVLRI-MQQLA-----EEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-220 |
3.90e-34 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 124.53 E-value: 3.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 25 GVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA--------REDTRLMFQ 96
Cdd:TIGR02769 16 GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkqrrafRRDVQLVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 D--SRLLPWKRVIDNVGLGLR-------GDWRAKALQALRAVGL-AERANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:TIGR02769 96 DspSAVNPRMTVRQIIGEPLRhltsldeSEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 167 EPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
21-220 |
4.82e-34 |
|
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: 122.69 E-value: 4.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFvAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR----LMFQ 96
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRrrigYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGL--GLRG----DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:cd03264 80 EFGVYPNFTVREFLDYiaWLKGipskEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLWREHgfTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
35-219 |
5.63e-34 |
|
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: 122.19 E-value: 5.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAeAREdtrlmfqdsrllPWKR---VIDNV 110
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVsVPGSIAYV-SQE------------PWIQngtIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 111 GLGLRGDwRAKALQALRAVGLAERANEWPA-----------ALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT--R 177
Cdd:cd03250 87 LFGKPFD-EERYEKVIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVgrH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 178 IeMQQLIEGLWREHGfTVLLVTHDVsEAVAVADRVILIEDGE 219
Cdd:cd03250 166 I-FENCILGLLLNNK-TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
21-220 |
6.91e-34 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 122.79 E-value: 6.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTRLM---FQ 96
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQIsVAGHDLRRAPRAALARLgvvFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNV-------GLGlRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPL 169
Cdd:TIGR03864 82 QPTLDLDLSVRQNLryhaalhGLS-RAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598638 170 GALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEaVAVADRVILIEDGEI 220
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALARDQGLSVLWATHLVDE-IEASDRLVVLHRGRV 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-220 |
7.09e-34 |
|
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: 122.54 E-value: 7.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR------LM 94
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERaragigYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGLRGDWRAKALQALRAV-----GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPL 169
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598638 170 GALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03224 161 EGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-223 |
1.19e-33 |
|
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: 121.93 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF--GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL-----AEAREDTRL 93
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIrqldpADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLpWKRVIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRL 162
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598638 163 LLLDEPLGALDalTRIEMqQLIEGL--WREHGfTVLLVTHDVSeAVAVADRVILIEDGEIGLD 223
Cdd:cd03245 162 LLLDEPTSAMD--MNSEE-RLKERLrqLLGDK-TLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
31-220 |
1.73e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 122.64 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDT-----RLMFQD--SRLLPW 103
Cdd:COG4167 24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYrckhiRMIFQDpnTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 104 KRV--IDNVGLGLRGDWRAKA-----LQALRAVGL-AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:COG4167 104 LNIgqILEEPLRLNTDLTAEEreeriFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4167 184 VRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
36-225 |
1.91e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.55 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAA-----LAEAREDTRLMFQDsrllPWKRVID-- 108
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnFEKLRKHIGIVFQN----PDNQFVGsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 ---NVGLGLRG------DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:PRK13648 101 vkyDVAFGLENhavpydEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 180 MQQLIEGLWREHGFTVLLVTHDVSEAVAvADRVILIEDG-------------------EIGLDLP 225
Cdd:PRK13648 181 LLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGtvykegtpteifdhaeeltRIGLDLP 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-213 |
3.68e-33 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 120.59 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRLMF 95
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLkpeiyRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 Q----------DSRLLPWKrvidnvglgLRGDW--RAKALQALRAVGLAERANEWP-AALSGGQKQRVALARALIHEPRL 162
Cdd:PRK10247 88 QtptlfgdtvyDNLIFPWQ---------IRNQQpdPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEaVAVADRVI 213
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVI 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-220 |
4.70e-33 |
|
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: 118.86 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG--EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR------ 92
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELgdhvgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMfQDSRLLPwKRVIDNVglglrgdwrakalqalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:cd03246 81 LP-QDDELFS-GSIAENI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 173 DALTRIEMQQLIEGLwREHGFTVLLVTHDvSEAVAVADRVILIEDGEI 220
Cdd:cd03246 128 DVEGERALNQAIAAL-KAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-220 |
5.06e-33 |
|
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: 118.30 E-value: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLagsaalaearedtrlmfqdsrl 100
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 lpwkrvIDNVGLGLRGDWRAKAL------QalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:cd03216 59 ------VDGKEVSFASPRDARRAgiamvyQ-----------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 175 LTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-220 |
5.27e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 120.27 E-value: 5.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GERE--VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR---------LMFQDSR 99
Cdd:PRK10584 19 GEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhvgFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 LLPWKRVIDNVGLG--LRG----DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK10584 99 LIPTLNALENVELPalLRGessrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 174 ALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAvAVADRVILIEDGEI 220
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-220 |
7.73e-33 |
|
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: 120.28 E-value: 7.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG--EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA-----GSAALAEAREDTRL 93
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdghdlALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPwKRVIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRL 162
Cdd:cd03252 81 VLQENVLFN-RSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLWRehGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRI 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
23-220 |
1.46e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 124.79 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaEAREDTRLMF--QDSRL 100
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLRIGYlpQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVGLGLRG--------------------------------------DWRAKALQALRAVGLAERANEWP-AA 141
Cdd:COG0488 73 DDDLTVLDTVLDGDAElraleaeleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPvSE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 142 LSGGQKQRVALARALIHEPRLLLLDEPLGALDaltrIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-220 |
1.73e-32 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 121.91 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 38 DIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRL---------MFQDSRLLPWKRVID 108
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekrrigyVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLW 188
Cdd:PRK11144 96 NLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190
....*....|....*....|....*....|..
gi 15598638 189 REHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
32-220 |
1.87e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.22 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRLMFQ--DSRLLPwK 104
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdiRHKIGMVFQnpDNQFVG-A 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK13650 98 TVEDDVAFGLenkgipHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLWREHGFTVLLVTHDVSEaVAVADRVILIEDGEI 220
Cdd:PRK13650 178 ELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-228 |
2.28e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.29 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQP-----SRGELLA---GSAALAEAREDTRLMFQ--DSRLL 101
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnSKITVDGitlTAKTVWDIREKVGIVFQnpDNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 PwKRVIDNVGLGL--RGDWRAKAL----QALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:PRK13640 99 G-ATVGDDVAFGLenRAVPRPEMIkivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 176 TRIEMQQLIEGLWREHGFTVLLVTHDVSEAvAVADRVILIEDGEI-GLDLPVEL 228
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLlAQGSPVEI 230
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
32-225 |
3.13e-32 |
|
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: 124.98 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL-----AEAREDTRLMFQDSRLLpWKRV 106
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIrqidpADLRRNIGYVPQDPRLF-YGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:TIGR03375 556 RDNIALGAPYADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNR 635
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598638 176 TRiemQQLIEGLWRE-HGFTVLLVTHDVSeAVAVADRVILIEDGEIGLDLP 225
Cdd:TIGR03375 636 SE---ERFKDRLKRWlAGKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGP 682
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-220 |
4.91e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.25 E-value: 4.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 12 PQRLKRgIPLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS----AALAEA 87
Cdd:COG0488 308 PERLGK-KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvkiGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDtrlmfqdsrLLPWKRVIDNVGLGLRGDWRAKALQALRAVGLA-ERANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:COG0488 387 QEE---------LDPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 167 EPLGALDaltrIEMQQLIEGLWREHGFTVLLVTHD---VSeavAVADRVILIEDGEI 220
Cdd:COG0488 458 EPTNHLD----IETLEALEEALDDFPGTVLLVSHDryfLD---RVATRILEFEDGGV 507
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
32-220 |
7.92e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.78 E-value: 7.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAG--------SAALAEAREDTRLMFQ--DSRL 100
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGyhitpetgNKNLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPwKRVIDNVGLGLRG------DWRAKALQALRAVGLAER-ANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK13641 99 FE-NTVLKDVEFGPKNfgfsedEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 174 ALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
31-220 |
1.09e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 122.49 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKS----TLLRLLAGLDQPSRGELLAGSAALAEAREDTR---------LMFQD 97
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrrirgnriaMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 --SRLLPWKRVIDNVG------LGLRG-DWRAKALQALRAVGLAE---RANEWPAALSGGQKQRVALARALIHEPRLLLL 165
Cdd:COG4172 101 pmTSLNPLHTIGKQIAevlrlhRGLSGaAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 166 DEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHD---VSEavaVADRVILIEDGEI 220
Cdd:COG4172 181 DEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVMRQGEI 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
45-213 |
1.11e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 119.30 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 45 AGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAREDTRLMFQD--SRLLPWKRVID------ 108
Cdd:PRK11308 40 RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdllkADPEAQKLLRQKIQIVFQNpyGSLNPRKKVGQileepl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 --NVGLGlRGDWRAKALQALRAVGL-AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIE 185
Cdd:PRK11308 120 liNTSLS-AAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMM 198
|
170 180
....*....|....*....|....*...
gi 15598638 186 GLWREHGFTVLLVTHDVSEAVAVADRVI 213
Cdd:PRK11308 199 DLQQELGLSYVFISHDLSVVEHIADEVM 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-220 |
1.34e-31 |
|
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: 116.95 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSaalaearEDTRLMFQDSrllpWKRVI---- 107
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG-------QDIREVTLDS----LRRAIgvvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 -------DNVGLGLR-GDWRAKALQ---ALRAVGLAERANEWPAA-----------LSGGQKQRVALARALIHEPRLLLL 165
Cdd:cd03253 82 qdtvlfnDTIGYNIRyGRPDATDEEvieAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 166 DEPLGALDALTRIEMQQLIEGLWRehGFTVLLVTHDVSEaVAVADRVILIEDGEI 220
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRI 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
32-223 |
2.26e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.46 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG-------SAALAEAREDTRLMFQDSRLLPWK 104
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdkKVKLSDIRKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVID--------NVGLGlRGDWRAKALQALRAVGLA--ERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:PRK13637 99 ETIEkdiafgpiNLGLS-EEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 175 LTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLD 223
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-227 |
2.91e-31 |
|
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: 115.85 E-value: 2.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR------LM 94
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgigYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDN--VGLGLRGDwRAKALQALRAVG-----LAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:COG0410 84 PEGRRIFPSLTVEENllLGAYARRD-RAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 168 PLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAA 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-227 |
3.50e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSA-ALAEAREDTRL----M 94
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEiLLDGEPvRFRSPRDAQAAgiaiI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLG---LRG---DWRA---KALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLL 165
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGrepRRGgliDWRAmrrRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 166 DEPlgaLDALTRIEMQQL---IEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG1129 165 DEP---TASLTEREVERLfriIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVA 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-215 |
3.62e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 114.25 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 29 RFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-AGSAALAEAREDTRLmfqdSRLLPwKRVI 107
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRrAGGARVAYVPQRSEV----PDSLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNVGLGL---RGDWR-------AKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTR 177
Cdd:NF040873 76 DLVAMGRwarRGLWRrltrddrAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598638 178 IEMQQLIeGLWREHGFTVLLVTHDVsEAVAVADRVILI 215
Cdd:NF040873 156 ERIIALL-AEEHARGATVVVVTHDL-ELVRRADPCVLL 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
32-223 |
6.95e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 116.34 E-value: 6.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL------AGSAALAEAREDTRLMFQ--DSRLLPw 103
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYvdgldtSDEENLWDIRNKAGMVFQnpDNQIVA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 104 KRVIDNVGLG------LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTR 177
Cdd:PRK13633 101 TIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 178 IEMQQLIEGLWREHGFTVLLVTHDVSEAVAvADRVILIEDGEIGLD 223
Cdd:PRK13633 181 REVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
31-220 |
1.08e-30 |
|
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: 114.24 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG-----SAALAEAREDTRLMFQDSRLLPwKR 105
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgidirDISRKSLRSMIGVVLQDTFLFS-GT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGLRGDWRAKALQALRAV-----------GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:cd03254 93 IMENIRLGRPNATDEEVIEAAKEAgahdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 175 ltriEMQQLI-EGLWR-EHGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:cd03254 173 ----ETEKLIqEALEKlMKGRTSIIIAHRLS-TIKNADKILVLDDGKI 215
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-215 |
1.35e-30 |
|
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: 119.31 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 9 GGTPQRLKRGIPLALRGVARRF-GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA 87
Cdd:TIGR02857 310 GKAPVTAAPASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDTRL-----------MFQDSrllpwkrVIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGG 145
Cdd:TIGR02857 390 DADSWRdqiawvpqhpfLFAGT-------IAENIRLARPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 146 QKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHgfTVLLVTHDVsEAVAVADRVILI 215
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRL-ALAALADRIVVL 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-220 |
1.54e-30 |
|
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: 119.14 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG--EREVLKDID---LLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL--LAGS--AALAEAREDT 91
Cdd:TIGR03269 280 IKVRNVSKRYIsvDRGVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 R--------LMFQDSRLLPWKRVIDN----VGLGLRGDW-RAKALQALRAVGLAERA-----NEWPAALSGGQKQRVALA 153
Cdd:TIGR03269 360 RgrakryigILHQEYDLYPHRTVLDNlteaIGLELPDELaRMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVALA 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 154 RALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR03269 440 QVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-220 |
1.54e-30 |
|
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: 113.86 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSA-----ALAEAREDTRLMFQDSRLLPwKRV 106
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdyTLASLRRQIGLVSQDVFLFN-DTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:cd03251 93 AENIAYGRPGATREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLWRehGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:cd03251 173 SERLVQAALERLMK--NRTTFVIAHRLS-TIENADRIVVLEDGKI 214
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-223 |
2.35e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 114.34 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 26 VARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGL-----DQPSRGELL------AGSAA--LAEAREDTR 92
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGSHIELLgrtvqrEGRLArdIRKSRANTG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQDSRLLPWKRVIDNVGLGLRGD---WRA-----------KALQALRAVGLAERANEWPAALSGGQKQRVALARALIH 158
Cdd:PRK09984 90 YIFQQFNLVNRLSVLENVLIGALGStpfWRTcfswftreqkqRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 159 EPRLLLLDEPLGALDALT-RIEMQQLiEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLD 223
Cdd:PRK09984 170 QAKVILADEPIASLDPESaRIVMDTL-RDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-220 |
4.55e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.48 E-value: 4.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS--------AALAEArEDTR 92
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlYALSEA-ERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQDsrllpWKRVIDNVGLGLR---------------------GDWRAKALQALRAVGL-AERANEWPAALSGGQKQRV 150
Cdd:PRK11701 86 LLRTE-----WGFVHQHPRDGLRmqvsaggnigerlmavgarhyGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 151 ALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-220 |
5.79e-30 |
|
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: 112.25 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALaearedTRL-MFQDSR 99
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI------TKLpMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 L----LP-----WKR--VIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:cd03218 75 LgigyLPqeasiFRKltVEENILAVLeirglsKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-218 |
6.60e-30 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 112.14 E-value: 6.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF-----GERE--VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSA------ALAEA 87
Cdd:COG4778 5 LEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDTRL-------MFQDSRLLPwkRV--IDNVGLGL------RGDWRAKALQALRAVGLAERAneW---PAALSGGQKQR 149
Cdd:COG4778 85 REILALrrrtigyVSQFLRVIP--RVsaLDVVAEPLlergvdREEARARARELLARLNLPERL--WdlpPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 150 VALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-223 |
8.88e-30 |
|
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: 112.04 E-value: 8.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 18 GIPLALRGVARR-FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTR--- 92
Cdd:cd03267 18 GLIGSLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRKKFLRrig 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 -LMFQDSRL---LPwkrVIDNVGLgLRGDWRAKALQALRAV-GLAERAN-----EWPA-ALSGGQKQRVALARALIHEPR 161
Cdd:cd03267 98 vVFGQKTQLwwdLP---VIDSFYL-LAAIYDLPPARFKKRLdELSELLDleellDTPVrQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598638 162 LLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLD 223
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-220 |
1.51e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 111.86 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRL---LAGLDQPSR--GEL-LAGSAALA------EAREDTRLMFQD 97
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEARveGEVrLFGRNIYSpdvdpiEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLRGDWRAKALQ--------ALRAVGLAE----RANEWPAALSGGQKQRVALARALIHEPRLLLL 165
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLVKSKKeldervewALKKAALWDevkdRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 166 DEPLGALDALTRIEMQQLIEGLWREhgFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-220 |
1.56e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 112.90 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEReVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA---------REDTRLMFQ--DS 98
Cdd:PRK13643 17 FASR-ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeikpvRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 99 RLLPwKRVIDNVGLGLRGDWRAK------ALQALRAVGLA-ERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:PRK13643 96 QLFE-ETVLKDVAFGPQNFGIPKekaekiAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13643 175 LDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
23-220 |
2.14e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 111.33 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG-------SAALAEA----RED 90
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvLVDGldvattpSRELAKRlailRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 TRLMfqdSRLlpwkRVIDNVGLG--------LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:COG4604 84 NHIN---SRL----TVRELVAFGrfpyskgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRV 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
32-220 |
2.18e-29 |
|
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: 111.09 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG----SAALAEAREDTRLMFQDSRLLPwKRV 106
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEiLLDGvdirDLNLRWLRSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLWRehGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:cd03249 174 SEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-220 |
2.95e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.35 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA--------REDTRLMFQDSRLL 101
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevpflRRQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 PWKRVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:PRK10908 92 MDRTVYDNVAIPLiiagasGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10908 172 LSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
34-220 |
3.27e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSA------ALAEAREDTRLMFQ--DSRLLPwK 104
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEvLIKGEPikydkkSLLEVRKTVGIVFQnpDDQLFA-P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVG-----LGLRGDWRAKAL-QALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK13639 95 TVEEDVAfgplnLGLSKEEVEKRVkEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13639 175 QIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-220 |
9.20e-29 |
|
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: 109.13 E-value: 9.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGERE--VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRLM---- 94
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSlgyc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGL--GLRG----DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:cd03263 81 PQFDALFDELTVREHLRFyaRLKGlpksEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598638 169 LGALDALTRIEMQQLIEGLWREHgfTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-220 |
1.13e-28 |
|
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: 114.43 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFG--EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE-----AREDTRL 93
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADytlasLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPwKRVIDNVGLGLRGDW-RAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPR 161
Cdd:TIGR02203 411 VSQDVVLFN-DTIANNIAYGRTEQAdRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 162 LLLLDEPLGALDALTRIEMQQLIEGLWRehGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-218 |
2.02e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.92 E-value: 2.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPS------RGELLAGSAALAEAREDTRLM 94
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTggtillRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNV--------------GLGLRGDWR-------AKALQALRAVGLAERANEWPAALSGGQKQRVALA 153
Cdd:PRK11300 86 FQHVRLFREMTVIENLlvaqhqqlktglfsGLLKTPAFRraesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 154 RALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-220 |
4.24e-28 |
|
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: 107.07 E-value: 4.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRF----GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAALAEAREDTR--- 92
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFaTVDGFDVVKEPAEARRrlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQDSRLLPWKRVIDNVGL--GLRGDWRAKALQALRAV----GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYfaGLYGLKGDELTARLEELadrlGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 167 EPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-227 |
5.14e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 109.04 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAALAEAREDTRLMFQDSR 99
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEvLWDGEPLDPEDRRRIGYLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 LLPWKRVIDNVG-LG-LRGDWRAKALQALRA----VGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:COG4152 82 LYPKMKVGEQLVyLArLKGLSKAEAKRRADEwlerLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 174 ALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG4152 162 PVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
21-219 |
5.65e-28 |
|
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: 104.45 E-value: 5.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaearedtrlmfqdsrl 100
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 lpwkRVIDNVGLGLRgdwrakalqalravglaeranewpAALSGGQKQRVALARALIHEPRLLLLDEPLGALDaltrIEM 180
Cdd:cd03221 58 ----TWGSTVKIGYF------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----LES 105
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598638 181 QQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:cd03221 106 IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
32-220 |
8.75e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.77 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-----LAGSAALAEAREDTRLMFQ--DSRLLPwK 104
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgiTISKENLKEIRKKIGIIFQnpDNQFIG-A 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK13632 100 TVEDDIAFGLenkkvpPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLWREHGFTVLLVTHDVSEAVaVADRVILIEDGEI 220
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-220 |
9.20e-28 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 107.57 E-value: 9.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRLMFQD--SRLLPWKRV 106
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysyrSQRIRMIFQDpsTSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVGLGLR------GDWRAKAL-QALRAVGL-AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK15112 107 SQILDFPLRlntdlePEQREKQIiETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK15112 187 QLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-223 |
1.09e-27 |
|
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: 105.09 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGERE--VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS---AALAEAREDTRLMF 95
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRLLPWKRVIDNVGlglrgdwrakalqalravglaeranewpAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:cd03247 81 NQRPYLFDTTLRNNLG----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 176 TRIEMQQLIEGLWREHgfTVLLVTHDVSeAVAVADRVILIEDGEIGLD 223
Cdd:cd03247 133 TERQLLSLIFEVLKDK--TLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
31-220 |
1.13e-27 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 111.38 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAeAREDTRL------MFQDSRLLPwK 104
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS-QWDREELgrhigyLPQDVELFD-G 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGlGLRGDWRAKALQALRAVGLAE-----------RANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:COG4618 421 TIAENIA-RFGDADPEKVVAAAKLAGVHEmilrlpdgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 174 ALTRIEMQQLIEGLwREHGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:COG4618 500 DEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRV 544
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
34-220 |
2.98e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS-------AALAEAREDTRLMFQD-SRLLPWKR 105
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrKGLMKLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:PRK13636 100 VYQDVSFGAvnlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598638 180 MQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-220 |
3.50e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.11 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGsaalaearED-TRL-MFQD 97
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRiFLDG--------EDiTHLpMHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRL----LP------WK-RVIDNVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEP 160
Cdd:COG1137 76 ARLgigyLPqeasifRKlTVEDNILAVLelrklsKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 161 RLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
21-222 |
3.59e-27 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 104.79 E-value: 3.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-----------------LAGSAA 83
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIifdghpwtrkdlhkigsLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 84 LAE---ARED-----TRLMFQDSRLLPwkrVIDNVGLGLRGDWRAKALqalravglaeranewpaalSGGQKQRVALARA 155
Cdd:TIGR03740 81 LYEnltARENlkvhtTLLGLPDSRIDE---VLNIVDLTNTGKKKAKQF-------------------SLGMKQRLGIAIA 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 156 LIHEPRLLLLDEPLGALDALTRIEMQQLIEgLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGL 222
Cdd:TIGR03740 139 LLNHPKLLILDEPTNGLDPIGIQELRELIR-SFPEQGITVILSSHILSEVQQLADHIGIISEGVLGY 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-220 |
4.42e-27 |
|
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: 104.54 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 8 LGGTPQRLKRGipLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE---------LL 78
Cdd:cd03220 12 TYKGGSSSLKK--LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTvtvrgrvssLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 79 AGSAAL---AEAREDTRLMfqdSRLLPWKR-----VIDNV----GLGLRGDWRAKalqalravglaeranewpaALSGGQ 146
Cdd:cd03220 90 GLGGGFnpeLTGRENIYLN---GRLLGLSRkeideKIDEIiefsELGDFIDLPVK-------------------TYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598638 147 KQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-230 |
4.74e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.51 E-value: 4.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVA-RRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaEAREDTRLMFqdsr 99
Cdd:COG4178 363 LALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGARVLF---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 lLPWK-RVIdnvgLG-LR---------GDW-RAKALQALRAVGL---AERANE---WPAALSGGQKQRVALARALIHEPR 161
Cdd:COG4178 431 -LPQRpYLP----LGtLReallypataEAFsDAELREALEAVGLghlAERLDEeadWDQVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 162 LLLLDEPLGALDALTRIEMQQLIEGlwREHGFTVLLVTHDvSEAVAVADRVILIEDGEIGLDLPVELPR 230
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGDGSWQLLPAEAPA 571
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-220 |
6.72e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.60 E-value: 6.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALA---------EAREDTRLMFQ--DSRL 100
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikQIRKKVGLVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPwKRVIDNVGLGLRG------DWRAKALQALRAVGLAERA-NEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK13649 99 FE-ETVLKDVAFGPQNfgvsqeEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 174 ALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13649 178 PKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
18-201 |
7.64e-27 |
|
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: 108.99 E-value: 7.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 18 GIPLALRGV-ARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDT----- 91
Cdd:TIGR02868 332 KPTLELRDLsAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrrv 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSRLLPwKRVIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEP 160
Cdd:TIGR02868 412 SVCAQDAHLFD-TTVRENLRLARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 161 RLLLLDEPLGALDALTRIEMqqlIEGLWR-EHGFTVLLVTHD 201
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADEL---LEDLLAaLSGRTVVLITHH 529
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-224 |
8.44e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.78 E-value: 8.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL--------------------------LAGSA--- 82
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklpeykrakyigrvfqdpMMGTApsm 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 83 ------ALAEAREDTRlmfqdsrllpwkrvidNVGLGLRGDWRA--KALQALRAVGLAERANEWPAALSGGQKQRVALAR 154
Cdd:COG1101 98 tieenlALAYRRGKRR----------------GLRRGLTKKRRElfRELLATLGLGLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 155 ALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDL 224
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDV 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
30-210 |
2.15e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.71 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRL---LAGLDQPSRGE---------LLAGSAALAEAREDTRLMFQD 97
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEgkvtfhgknLYAPDVDPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPwKRVIDNVGLGLR-----GDWRAKALQALRAVGL----AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEP 168
Cdd:PRK14243 100 PNPFP-KSIYDNIAYGARingykGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 169 LGALDALTRIEMQQLIEGLWREhgFTVLLVTHDVSEAVAVAD 210
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
34-218 |
2.55e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.05 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTR----LMFQDS-----RLLPW 103
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRskvgLVFQDPddqvfSSTVW 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 104 KRV-IDNVGLGLRGD-WRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQ 181
Cdd:PRK13647 99 DDVaFGPVNMGLDKDeVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598638 182 QLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK13647 179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
30-220 |
2.60e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.53 E-value: 2.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE--AREDTR---LMFQDSRLLPWK 104
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyaSKEVARrigLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGLG------LRGDWRAK----ALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:PRK10253 97 TVQELVARGryphqpLFTRWRKEdeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 175 LTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-220 |
2.98e-26 |
|
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: 102.55 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE-----AREDTRLMFQDSRLLPwKRV 106
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkyLHSKVSLVGQEPVLFA-RSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVGLGLRG--DWRAKALQ---------ALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:cd03248 105 QDNIAYGLQScsFECVKEAAqkahahsfiSELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLWREHgfTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:cd03248 185 SEQQVQQALYDWPERR--TVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-220 |
4.15e-26 |
|
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: 106.81 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQ--PSRGELL-------------------- 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 79 -----AGSAALAEA-------------REDTRLMFQDS-RLLPWKRVIDNV-----GLGLRGDWRA-KALQALRAVGLAE 133
Cdd:TIGR03269 81 pcpvcGGTLEPEEVdfwnlsdklrrriRKRIAIMLQRTfALYGDDTVLDNVlealeEIGYEGKEAVgRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 134 RANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVI 213
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
....*..
gi 15598638 214 LIEDGEI 220
Cdd:TIGR03269 241 WLENGEI 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-220 |
6.19e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.40 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE--AREDTRLMfqdsRLLPWK--- 104
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlsSRQLARRL----ALLPQHhlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 ----RVIDNVGLG----------LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:PRK11231 88 pegiTVRELVAYGrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 171 ALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11231 168 YLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-220 |
1.15e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.53 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGL-----DQPSRGE-LLAGSAA----LAEARED 90
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEvYLDGQDIfkmdVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 TRLMFQDSRLLPWKRVIDNVGLGLRGDWRAKALQAL--RAVGLAERANEW---------PAA-LSGGQKQRVALARALIH 158
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELqeRVRWALEKAQLWdevkdrldaPAGkLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598638 159 EPRLLLLDEPLGALDALTRIEMQQLIEGLWREhgFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-213 |
1.26e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 103.25 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 12 PQRLKrgiplALRGVARRFGEREVLkdidllvpagqfvAIVGRSGCGKSTLLRLLAGLDQPSRGE-------LLAGSAA- 83
Cdd:PRK15079 31 PKTLK-----AVDGVTLRLYEGETL-------------GVVGESGCGKSTFARAIIGLVKATDGEvawlgkdLLGMKDDe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 84 LAEAREDTRLMFQD--SRLLPWKRVIDNVGLGLR--------GDWRAKALQALRAVGLAERA-NEWPAALSGGQKQRVAL 152
Cdd:PRK15079 93 WRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLRtyhpklsrQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 153 ARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVI 213
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
21-220 |
1.45e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 100.68 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL------LAGSAALAEAREDTRLM 94
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIrldgedITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDN--VGLGLRGDWRAKALQ-------ALRAVgLAERANEwpaaLSGGQKQRVALARALIHEPRLLLL 165
Cdd:TIGR03410 81 PQGREIFPRLTVEENllTGLAALPRRSRKIPDeiyelfpVLKEM-LGRRGGD----LSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 166 DEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRV 210
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
21-220 |
1.49e-25 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 101.45 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEaREDTRLMFQDSRL 100
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAE-LELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 L---PWKRVIDNVGLGLR---------------------GDWRAKALQALRAVGL-AERANEWPAALSGGQKQRVALARA 155
Cdd:TIGR02323 83 LmrtEWGFVHQNPRDGLRmrvsaganigerlmaigarhyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 156 LIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR02323 163 LVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
31-220 |
2.18e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.42 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA-----GSAALAEAREDTRLMFQDSRLLPWKR 105
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepiTKENIREVRKFVGLVFQNPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDN------VGLGLRGDWRA-KALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK13652 95 TVEQdiafgpINLGLDEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13652 175 ELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
31-220 |
3.33e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.52 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDT-RLMFQdsrLLPwKRVI-- 107
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQAIS---VVS-QRVHlf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 -----DNVGLGLRGDWRAKALQALRAVGLA------ERANEWPA----ALSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:PRK11160 427 satlrDNLLLAAPNASDEALIEVLQQVGLEklleddKGLNAWLGeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15598638 173 DALTRIEMQQLIeglwREH--GFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:PRK11160 507 DAETERQILELL----AEHaqNKTVLMITHRLT-GLEQFDRICVMDNGQI 551
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
31-200 |
5.33e-25 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 98.72 E-value: 5.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR--LMFQ------DSRLLP 102
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHqdLLYLghqpgiKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 103 WKRVIDNVGLGLRGDwRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA-----LTR 177
Cdd:PRK13538 92 LENLRFYQRLHGPGD-DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKqgvarLEA 170
|
170 180
....*....|....*....|...
gi 15598638 178 IEMQQLieglwrEHGFTVLLVTH 200
Cdd:PRK13538 171 LLAQHA------EQGGMVILTTH 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-246 |
5.38e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 100.56 E-value: 5.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALA-----------EAREDTRLMFQDS 98
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGgrsifnyrdvlEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 99 RLLPWKrVIDNVGLGLRG-------DWRAKALQALRAVGL----AERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:PRK14271 111 NPFPMS-IMDNVLAGVRAhklvprkEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 168 PLGALDALTRIEMQQLIEGLWREhgFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE--LPRPRSRGSAR-LAALEA 244
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEqlFSSPKHAETARyVAGLSG 267
|
..
gi 15598638 245 EV 246
Cdd:PRK14271 268 DV 269
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-200 |
2.10e-24 |
|
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: 97.04 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEARED-TRLMFQDSR 99
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 LLPWK---RVIDNVGL--GLRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:TIGR01189 81 LPGLKpelSALENLHFwaAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*....
gi 15598638 175 ltriEMQQLIEGLWREH---GFTVLLVTH 200
Cdd:TIGR01189 161 ----AGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-231 |
4.94e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.55 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 22 ALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE------AREDTRLMF 95
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskafARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QdsrlLPWKR---VIDNVGLGlRGDW-----------RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPR 161
Cdd:PRK10575 93 Q----LPAAEgmtVRELVAIG-RYPWhgalgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 162 LLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGE-IGLDLPVELPRP 231
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEmIAQGTPAELMRG 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-220 |
5.52e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.43 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL-----------AEAREDTRLMFQDSRL 100
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifqidaIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVGL-----GLRGDWRAKAL--QALRAVGL----AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPL 169
Cdd:PRK14246 102 FPHLSIYDNIAYplkshGIKEKREIKKIveECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598638 170 GALDALTRIEMQQLIEGLWREhgFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-220 |
5.55e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 101.05 E-value: 5.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 20 PLALRGVARRF--------GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGS--------- 81
Cdd:COG5265 350 PLVVGGGEVRFenvsfgydPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRiLIDGQdirdvtqas 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 82 --AALAEAREDTrLMFQDSrllpwkrVIDNVGLGLRGDWRAKALQALRAV-----------GLAERANEWPAALSGGQKQ 148
Cdd:COG5265 430 lrAAIGIVPQDT-VLFNDT-------IAYNIAYGRPDASEEEVEAAARAAqihdfieslpdGYDTRVGERGLKLSGGEKQ 501
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598638 149 RVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHgfTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:COG5265 502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLS-TIVDADEILVLEAGRI 570
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
38-220 |
7.00e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 96.28 E-value: 7.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 38 DIDLLVPAGQFVAIVGRSGCGKST----LLRLLAGLDQPSRGELLAGSAALAEAR---EDTRLMFQDSR--LLPWKRVID 108
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSirgRHIATIMQNPRtaFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLR------GDWRAKALQALRAVGLAERA---NEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:TIGR02770 84 HAIETLRslgklsKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598638 180 MQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-227 |
9.88e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.85 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 18 GIPLALRG-VARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-AG------SAALAeaRE 89
Cdd:COG4586 19 GLKGALKGlFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGyvpfkrRKEFA--RR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 90 DTRLMFQDSRL---LPwkrVIDNVGL-----GLRGDWRAKALQALRAV-GLAE------RAnewpaaLSGGQKQRVALAR 154
Cdd:COG4586 97 IGVVFGQRSQLwwdLP---AIDSFRLlkaiyRIPDAEYKKRLDELVELlDLGElldtpvRQ------LSLGQRMRCELAA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598638 155 ALIHEPRLLLLDEP-LGaLDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:COG4586 168 ALLHRPKILFLDEPtIG-LDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLE 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-220 |
1.01e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 13 QRLKRGIPLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKST----LLRLLAgldqpSRGEL--------LAG 80
Cdd:PRK15134 279 EQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIwfdgqplhNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 81 SAALAEAREDTRLMFQD--SRLLPWKRVIDNVGLGLR--------GDWRAKALQALRAVGL-AERANEWPAALSGGQKQR 149
Cdd:PRK15134 354 RRQLLPVRHRIQVVFQDpnSSLNPRLNVLQIIEEGLRvhqptlsaAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQR 433
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 150 VALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-220 |
1.50e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.92 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 13 QRLKRgipLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA-GS-AALAE---- 86
Cdd:COG1134 22 RSLKE---LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVnGRvSALLElgag 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 87 ------AREDTRLMfqdSRLlpwkrvidnvgLGLRgdwRAKALQALRAV----GLAERANEwPA-ALSGGQKQRVALARA 155
Cdd:COG1134 99 fhpeltGRENIYLN---GRL-----------LGLS---RKEIDEKFDEIvefaELGDFIDQ-PVkTYSSGMRARLAFAVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 156 LIHEPRLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
21-213 |
5.31e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.41 E-value: 5.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAgSAALAEAREDTRLMFQDSRL 100
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR-NGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVidnvgLGLR-GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:PRK09544 84 LTVNRF-----LRLRpGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190
....*....|....*....|....*....|....
gi 15598638 180 MQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVI 213
Cdd:PRK09544 159 LYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
33-220 |
9.03e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.50 E-value: 9.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 33 REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAreDTRLMFQDSRLLPWKRVI----- 107
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI--DRHTLRQFINYLPQEPYIfsgsi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 -DNVGLGLRGD------WRAKALQALRA------VGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:TIGR01193 565 lENLLLGAKENvsqdeiWAACEIAEIKDdienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 175 LTRiemQQLIEGLWREHGFTVLLVTHDVSEAVAVaDRVILIEDGEI 220
Cdd:TIGR01193 645 ITE---KKIVNNLLNLQDKTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-220 |
1.40e-22 |
|
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: 91.72 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL----------------AGSAALAEARedtrlmfQDS 98
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgkpvtrrsprdairAGIAYVPEDR-------KRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 99 RLLPWKRVIDNVGLGLRgdwrakalqalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:cd03215 88 GLVLDLSVAENIALSSL--------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:cd03215 142 EIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
31-220 |
1.54e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 96.65 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDT-----RLMFQDSRLLPwKR 105
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgkhiGYLPQDVELFP-GT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGLRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:TIGR01842 408 VAENIARFGENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 175 LTRIEMQQLIEGLwREHGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:TIGR01842 488 EGEQALANAIKAL-KARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-200 |
2.72e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.94 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 25 GVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGldqpsrgellagsaALAEAREDTRLMFQDSRLLPWK 104
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCVDVPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVglGLRGDWRAkALQALRAVGLAERANeW---PAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQ 181
Cdd:COG2401 101 SLIDAI--GRKGDFKD-AVELLNAVGLSDAVL-WlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170
....*....|....*....
gi 15598638 182 QLIEGLWREHGFTVLLVTH 200
Cdd:COG2401 177 RNLQKLARRAGITLVVATH 195
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
30-220 |
2.78e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQ--PS---RGELLAGSAALAEAREDT-------RLMFQD 97
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdlrkeiGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKrVIDNVGLGLR-GDWRAKAL------QALRAVGL----AERANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:PRK14239 95 PNPFPMS-IYENVVYGLRlKGIKDKQVldeaveKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 167 EPLGALDALTRIEMQQLIEGLwrEHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-232 |
3.62e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.92 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAA---------LAEAREDTRLMFQ--DSRL 100
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkdkyIRPVRKRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LP--WKRVI----DNVGLGLRgDWRAKALQALRAVGLAERANEW-PAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK13646 99 FEdtVEREIifgpKNFKMNLD-EVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 174 ALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIgldlpVELPRPR 232
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI-----VSQTSPK 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
39-220 |
4.05e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.30 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 39 IDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLdQPSRGELLAG-----SAALAEAREDTRLMFQDSrLLPWKRVIDNVGLG 113
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINgielrELDPESWRKHLSWVGQNP-QLPHGTLRDNVLLG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 114 LRGDWRAKALQALRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRiemQQ 182
Cdd:PRK11174 447 NPDASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSE---QL 523
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598638 183 LIEGLWRE-HGFTVLLVTHDVsEAVAVADRVILIEDGEI 220
Cdd:PRK11174 524 VMQALNAAsRRQTTLMVTHQL-EDLAQWDQIWVMQDGQI 561
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
36-223 |
4.32e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS------AALAEAREDTRLMFQDSRLLPWKRVI-D 108
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVGIVFQNPETQFVGRTVeE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLRG------DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQ 182
Cdd:PRK13644 98 DLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15598638 183 LIEGLwREHGFTVLLVTHDVSEaVAVADRVILIEDGEIGLD 223
Cdd:PRK13644 178 RIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLE 216
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-218 |
5.14e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.95 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 20 PLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRG------ELLAGSAALAEAREDTRL 93
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGsislcgEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDsrLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:PRK13537 87 QFDN--LDPDFTVRENLLVFGRyfglsaAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 15598638 168 PLGALDALTRIEMQQLIEGLWrEHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-223 |
5.84e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 91.48 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE------AREDTRLM 94
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqtakiMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGLRGDWRAKALQALRAV-----GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPL 169
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVyelfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 170 GALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLD 223
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
31-220 |
6.26e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 94.78 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE-----AREDTRLMFQDSRLLPwKR 105
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshsvLRQGVAMVQQDPVVLA-DT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGlRGDWRAKALQALRAVGLAERANEWPAA-----------LSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:PRK10790 431 FLANVTLG-RDISEEQVWQALETVQLAELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15598638 175 LTRIEMQQLIeGLWREHGfTVLLVTHDVSEAVAvADRVILIEDGEI 220
Cdd:PRK10790 510 GTEQAIQQAL-AAVREHT-TLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
36-220 |
7.18e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.08 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAE----AREDTRLMFQ--DSRLLPwKRVID 108
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkIDGELLTAEnvwnLRRKIGMVFQnpDNQFVG-ATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGL------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQ 182
Cdd:PRK13642 102 DVAFGMenqgipREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598638 183 LIEGLWREHGFTVLLVTHDVSEAvAVADRVILIEDGEI 220
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-221 |
7.77e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.79 E-value: 7.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE-----AREDTRLMFQDSRLlpWKR- 105
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhyLHRQVALVGQEPVL--FSGs 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGLRGDWRAKALQALRAVGLAERANEWPAA-----------LSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:TIGR00958 571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 175 ltriEMQQLIEGLWREHGFTVLLVTHDVSeAVAVADRVILIEDGEIG 221
Cdd:TIGR00958 651 ----ECEQLLQESRSRASRTVLLIAHRLS-TVERADQILVLKKGSVV 692
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-220 |
9.84e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.37 E-value: 9.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 18 GIPLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG--SAALAEAREDTRLMF 95
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgdDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 ---QDSRLLPWKRVIDNVGLG----------LRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:PRK09536 81 svpQDTSLSFEFDVRQVVEMGrtphrsrfdtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
32-220 |
1.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-------AGSAALAEAREDTRLMFQDSRLLPWK 104
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdekNKKKTKEKEKVLEKLVIQKTRFKKIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVID---NVG-------------------------LGL-RGDWRAKALQALRAVGLAER-ANEWPAALSGGQKQRVALAR 154
Cdd:PRK13651 99 KIKEirrRVGvvfqfaeyqlfeqtiekdiifgpvsMGVsKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALAG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 155 ALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
23-205 |
1.76e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 93.65 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTRL------MFQ 96
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVcpriayMPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 --DSRLLPWKRVIDNV-------GLGlRGDWRAKALQALRAVGLAERANEwPAA-LSGGQKQRVALARALIHEPRLLLLD 166
Cdd:NF033858 84 glGKNLYPTLSVFENLdffgrlfGQD-AAERRRRIDELLRATGLAPFADR-PAGkLSGGMKQKLGLCCALIHDPDLLILD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598638 167 EPLGALDALTRIEMQQLIEGLWREH-GFTVLLVTHDVSEA 205
Cdd:NF033858 162 EPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEA 201
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-220 |
3.53e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.07 E-value: 3.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-------REDTRL 93
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkrgllalRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 MFQDSRLLPWKRVID-NVGLGLRGDWRAKALQALR---AVGL--AERANEWP-AALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:PRK13638 82 VFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITRRvdeALTLvdAQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 167 EPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-219 |
4.81e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.01 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL-----AEARedtRL-- 93
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrirspRDAI---ALgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 94 -M-FQDSRLLPWKRVIDNVGLGLRGDW-----RAKALQALRAV----GLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:COG3845 83 gMvHQHFMLVPNLTVAENIVLGLEPTKggrldRKAARARIRELseryGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598638 163 LLLDEPLGAL-----DALTRIeMQQLieglwREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:COG3845 163 LILDEPTAVLtpqeaDELFEI-LRRL-----AAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
29-220 |
5.31e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 88.32 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 29 RFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE-AREDTR----------LMFQD 97
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRsrisiipqdpVLFSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SrllpwkrVIDNVG-LGLRGDwrAKALQALRAVGLAERANEWPAAL-----------SGGQKQRVALARALIHEPRLLLL 165
Cdd:cd03244 93 T-------IRSNLDpFGEYSD--EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 166 DEPLGALDALTRIEMQQLIeglwREH--GFTVLLVTHDVsEAVAVADRVILIEDGEI 220
Cdd:cd03244 164 DEATASVDPETDALIQKTI----REAfkDCTVLTIAHRL-DTIIDSDRILVLDKGRV 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
7.38e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAA-LAEAREDTRLMFQDS 98
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIkLDGGDIdDPDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 99 RLLPWKRVIDNVGL--GLRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:PRK13539 83 AMKPALTVAENLEFwaAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
170 180
....*....|....*....|....*..
gi 15598638 177 riemQQLIEGLWREH---GFTVLLVTH 200
Cdd:PRK13539 163 ----VALFAELIRAHlaqGGIVIAATH 185
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-220 |
9.04e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 9.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL------AEAREDTRLM 94
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVG--LGLRGDWRAKAlQALRAVGLAER------ANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMavLQIRDDLSAEQ-REDRANELMEEfhiehlRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 167 EPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
36-220 |
1.26e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.23 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAG----SAALAEAREDTRLMFQDSRLLPwKRVIDNV 110
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEiLLDGhdlrDYTLASLRNQVALVSQNVHLFN-DTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 111 GLGLRGDW-RAKALQALRAV-----------GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRI 178
Cdd:PRK11176 438 AYARTEQYsREQIEEAARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 179 EMQQLIEGLWREHgfTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:PRK11176 518 AIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEI 556
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-220 |
2.62e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 2.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL----------AEAREDTRLMFQDSRLL 101
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkikevKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 PWKRVIDN------VGLGL-RGDWRAKALQALRAVGLAER-ANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK13645 103 LFQETIEKdiafgpVNLGEnKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 174 ALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-200 |
4.27e-20 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 84.51 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaEAREDTRLMF------------QDSRLLP 102
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLFlpqrpylplgtlREQLIYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 103 WKRVidnvglglrgdwrakalqalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDAltriEMQQ 182
Cdd:cd03223 88 WDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESED 128
|
170
....*....|....*...
gi 15598638 183 LIEGLWREHGFTVLLVTH 200
Cdd:cd03223 129 RLYQLLKELGITVISVGH 146
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-210 |
4.35e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.01 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQ-------PSRGELLAGS-----AALAEAREDTRLMFQD 97
Cdd:PRK14258 17 YDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevrvEGRVEFFNQNiyerrVNLNRLRRQVSMVHPK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKrVIDNVGLGLR-GDWRAK------ALQALRAVGL----AERANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:PRK14258 97 PNLFPMS-VYDNVAYGVKiVGWRPKleiddiVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 167 EPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVAD 210
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-218 |
4.55e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKS----TLLRLLagldqPS------RGELLAGSAALAEAREDT---------R 92
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQTlrgvrgnkiA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQD--SRLLPW----KRVIDNVGL--GLRGD-WRAKALQALRAVGL---AERANEWPAALSGGQKQRVALARALIHEP 160
Cdd:PRK15134 96 MIFQEpmVSLNPLhtleKQLYEVLSLhrGMRREaARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 161 RLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
31-220 |
6.17e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.86 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-----AGSAALAEAREDTRLMFQDSRLLpwKR 105
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidgtdIRTVTRASLRRNIAVVFQDAGLF--NR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VI-DNVGLGlRGDWR-------AKALQAL-----RAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:PRK13657 424 SIeDNIRVG-RPDATdeemraaAERAQAHdfierKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 173 DALTRIEMQQLIEGLwrEHGFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:PRK13657 503 DVETEAKVKAALDEL--MKGRTTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
31-220 |
6.87e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 84.91 E-value: 6.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGL--DQPSRGELLAGSAALAEAREDTRLMF--QDSRLLPWKRV 106
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKIIGYvpQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVG--LGLRGdwrakalqalravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLI 184
Cdd:cd03213 100 RETLMfaAKLRG-------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 15598638 185 EGLwREHGFTVLLVTHDVS-EAVAVADRVILIEDGEI 220
Cdd:cd03213 155 RRL-ADTGRTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-220 |
8.48e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 12 PQRLKRGIPLALRGVARRFGERE-----VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALA- 85
Cdd:PRK13631 13 PNPLSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 86 --------------------EAREDTRLMFQDSRLLPWKRVIDN------VGLGL-RGDWRAKALQALRAVGLAERANEW 138
Cdd:PRK13631 93 kknnhelitnpyskkiknfkELRRRVSMVFQFPEYQLFKDTIEKdimfgpVALGVkKSEAKKLAKFYLNKMGLDDSYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 139 -PAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIED 217
Cdd:PRK13631 173 sPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
...
gi 15598638 218 GEI 220
Cdd:PRK13631 252 GKI 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-219 |
1.49e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 87.96 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLdQPS---RGELL-AGSAALAEAREDTR---- 92
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYwSGSPLKASNIRDTEragi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 -LMFQDSRLLPWKRVIDNVGLG----LRGD--------WRAKALqaLRAVGLAERANEWPAA-LSGGQKQRVALARALIH 158
Cdd:TIGR02633 81 vIIHQELTLVPELSVAENIFLGneitLPGGrmaynamyLRAKNL--LRELQLDADNVTRPVGdYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598638 159 EPRLLLLDEPLGaldALTRIEMQQLIEGL--WREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:TIGR02633 159 QARLLILDEPSS---SLTEKETEILLDIIrdLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-228 |
1.78e-19 |
|
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: 83.73 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLD--QPSRGELLAGSAALAEAREDTR------ 92
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERarlgif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQDSRLLPWKRVIDnvglglrgdwrakalqALRAVglaeraNEwpaALSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:cd03217 81 LAFQYPPEIPGVKNAD----------------FLRYV------NE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 173 DaltrIEMQQLIEGL---WREHGFTVLLVTH--DVSEAVaVADRVILIEDGEIGLDLPVEL 228
Cdd:cd03217 136 D----IDALRLVAEVinkLREEGKSVLIITHyqRLLDYI-KPDRVHVLYDGRIVKSGDKEL 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-201 |
2.70e-19 |
|
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: 87.30 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEllagsaalAEAREDTRLMF--QDSRLLPWKRVID 108
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPGIKVGYlpQEPQLDPTKTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLRGdwRAKALQALRAVGLA----------------------------------ERA--------NEWPAA-LSGG 145
Cdd:TIGR03719 88 NVEEGVAE--IKDALDRFNEISAKyaepdadfdklaaeqaelqeiidaadawdldsqlEIAmdalrcppWDADVTkLSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 146 QKQRVALARALIHEPRLLLLDEPLGALDAltriEMQQLIEGLWREHGFTVLLVTHD 201
Cdd:TIGR03719 166 ERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
36-218 |
3.60e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 83.53 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-----LAGSAALAEAREDTRLMFQDSRLLPW---KRVI 107
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnkNESEPSFEATRSRNRYSVAYAAQKPWllnATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNVGLG-------LRGDWRAKALQA---LRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA-LT 176
Cdd:cd03290 97 ENITFGspfnkqrYKAVTDACSLQPdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIhLS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15598638 177 RIEMQQLIEGLWREHGFTVLLVTHDVsEAVAVADRVILIEDG 218
Cdd:cd03290 177 DHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-219 |
7.68e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 85.75 E-value: 7.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLdQPS---RGELL-AGSAALAEAREDTR---- 92
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIfEGEELQASNIRDTEragi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 -LMFQDSRLLPWKRVIDNVGLG---LRG---DW-----RAKALqaLRAVGLAERANEWPAALSGGQKQRVALARALIHEP 160
Cdd:PRK13549 85 aIIHQELALVKELSVLENIFLGneiTPGgimDYdamylRAQKL--LAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598638 161 RLLLLDEPLGaldALTRIEMQQL---IEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:PRK13549 163 RLLILDEPTA---SLTESETAVLldiIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-218 |
7.78e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 12 PQRLKRGIPLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL------LAGSAALA 85
Cdd:PRK13536 33 IPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 86 EARedTRLMFQDSRLLPWKRVIDN-VGLGLRGDWRAKALQA-----LRAVGLAERANEWPAALSGGQKQRVALARALIHE 159
Cdd:PRK13536 113 RAR--IGVVPQFDNLDLEFTVRENlLVFGRYFGMSTREIEAvipslLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 160 PRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
33-241 |
1.10e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 33 REVLKDIDLLVPAGQFVAIVGRSGCGKS-----TLLRLLAGLDQpSRGELLAGSAALAEAR----------EDTRLMFQD 97
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCAlrgrkiatimQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLRGDwRAKALQALRAVGLAERA---NEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:PRK10418 95 LHTMHTHARETCLALGKPAD-DATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 175 LTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE--LPRPRSRGSARLAA 241
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVEtlFNAPKHAVTRSLVS 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-222 |
1.56e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAREDTR------LM 94
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGL--RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGal 172
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGLpkRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTA-- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 173 dALTRIEMQQL---IEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGL 222
Cdd:PRK15439 170 -SLTPAETERLfsrIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-200 |
2.97e-18 |
|
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: 80.61 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAR-EDTRLMFQDSR 99
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 100 LLPWK---RVIDNVGLGLRGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:cd03231 81 APGIKttlSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*..
gi 15598638 177 riemQQLIEGLWREH---GFTVLLVTH 200
Cdd:cd03231 161 ----VARFAEAMAGHcarGGMVVLTTH 183
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-201 |
3.12e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.01 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEllagsAALAEAREDTRLMfQDSRLLPWKRVIDNV 110
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-----ARPAPGIKVGYLP-QEPQLDPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 111 GLGLRGdwRAKALQALRAVG------------LAER----------ANEW---------------PAA------LSGGQK 147
Cdd:PRK11819 92 EEGVAE--VKAALDRFNEIYaayaepdadfdaLAAEqgelqeiidaADAWdldsqleiamdalrcPPWdakvtkLSGGER 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 148 QRVALARALIHEPRLLLLDEPLGALDAltriEMQQLIEGLWREHGFTVLLVTHD 201
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-220 |
6.13e-18 |
|
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: 80.39 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQpsRGELLAGSAALAEaREDTRLMF--------QDSRLLPW 103
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNG-QPRKPDQFqkcvayvrQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 104 KRV------IDNVGLGLRGDWRAK----ALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:cd03234 96 LTVretltyTAILRLPRKSSDAIRkkrvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 174 ALTRIEMQQLIEGLWREhGFTVLLVTHD-VSEAVAVADRVILIEDGEI 220
Cdd:cd03234 176 SFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
38-218 |
9.01e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.31 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 38 DIDLLVPAGQFVAIVGRSGCGKS----TLLRLLAgldqpsRGELLAGSAA--------LAEAR------EDTRLMFQD-- 97
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqtafALMGLLA------ANGRIGGSATfngreilnLPEKElnklraEQISMIFQDpm 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNV--------GLGlRGDWRAKALQALRAVGLAE---RANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:PRK09473 108 TSLNPYMRVGEQLmevlmlhkGMS-KAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598638 167 EPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-220 |
1.02e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRfgerEVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL----------------AGSAAL 84
Cdd:COG1129 257 LEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsprdairAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 85 AEAREDTRLMFQDSrllpwkrVIDNVGLGLRGDWRAKALqaLRAVGLAERANEW-------------PA-ALSGGQKQRV 150
Cdd:COG1129 333 PEDRKGEGLVLDLS-------IRENITLASLDRLSRGGL--LDRRRERALAEEYikrlriktpspeqPVgNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 151 ALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-212 |
1.23e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 79.78 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEARED--TRLM---- 94
Cdd:COG4674 11 LYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHeiARLGigrk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDNVGLGLRGDWRAKAL--------------QALRAVGLAERANEWPAALSGGQKQRVALARALIHEP 160
Cdd:COG4674 91 FQKPTVFEELTVFENLELALKGDRGVFASlfarltaeerdrieEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 161 RLLLLDEPLGaldALTRIEMQQ---LIEGLWREHgfTVLLVTHDVSEAVAVADRV 212
Cdd:COG4674 171 KLLLLDEPVA---GMTDAETERtaeLLKSLAGKH--SVVVVEHDMEFVRQIARKV 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-218 |
1.43e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSA------ALAeAREDTRLMF 95
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItINNINynkldhKLA-AQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRLLPWKRVIDNVGLG------LRG----DW---RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRL 162
Cdd:PRK09700 87 QELSVIDELTVLENLYIGrhltkkVCGvniiDWremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 163 LLLDEPlgaLDALTRIEMQQL--IEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK09700 167 IIMDEP---TSSLTNKEVDYLflIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
35-219 |
3.21e-17 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 79.13 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaeaREDTRLMF--QDSRLLPwKRVIDNVGL 112
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------KHSGRISFssQFSWIMP-GTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 113 GLRGD-WRAKALqaLRAVGLAERANEWPA-----------ALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEM 180
Cdd:cd03291 121 GVSYDeYRYKSV--VKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598638 181 -QQLIEGLWREHgfTVLLVTHDVsEAVAVADRVILIEDGE 219
Cdd:cd03291 199 fESCVCKLMANK--TRILVTSKM-EHLKKADKILILHEGS 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-221 |
4.63e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 78.22 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALA------EAREDTRLmfqdSRLLpwkRVIDNvGLGLRGDWR 119
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyiKADYEGTV----RDLL---SSITK-DFYTHPYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 120 AKALQALRAVGLAER-ANEwpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLV 198
Cdd:cd03237 97 TEIAKPLQIEQILDReVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVV 172
|
170 180
....*....|....*....|...
gi 15598638 199 THDVSEAVAVADRVILIeDGEIG 221
Cdd:cd03237 173 EHDIIMIDYLADRLIVF-EGEPS 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
46-220 |
5.09e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG--------SAALAEAREDTRLMFQD--SRLLPWKRVIDNV----- 110
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridtlsPGKLQALRRDIQFIFQDpyASLDPRQTVGDSImeplr 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 111 --GLGLRGDWRAKALQALRAVGL-AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGL 187
Cdd:PRK10261 430 vhGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
170 180 190
....*....|....*....|....*....|...
gi 15598638 188 WREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
34-220 |
2.47e-16 |
|
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: 75.53 E-value: 2.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-----AGSAALAEAREDTRLMFQDSRLL------- 101
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidgidISTIPLEDLRSSLTIIPQDPTLFsgtirsn 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 --PWKRVIDnvglglrgdwrAKALQALRavgLAERANEwpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:cd03369 102 ldPFDEYSD-----------EEIYGALR---VSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598638 180 MQQLIeglwREH--GFTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:cd03369 164 IQKTI----REEftNSTILTIAHRLR-TIIDYDKILVMDAGEV 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-218 |
2.63e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEAreDTR-------- 92
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--STTaalaagva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQDSRLLPWKRVIDNVGLGL---------RGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLL 163
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLYLGQlphkggivnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 164 LLDEPLGALDALtriEMQQL---IEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK11288 163 AFDEPTSSLSAR---EIEQLfrvIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
26-220 |
2.78e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.40 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 26 VARRfgEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAG-LDQPSR-------------GELLAGSAALAEAREDT 91
Cdd:PRK13547 9 VARR--HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtgdvtlnGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 92 RLMFQDSRLLPWKrVIDNVGLGLRGDWRAKALQALRAVGLAERANEWPAA----------LSGGQKQRVALARAL----- 156
Cdd:PRK13547 87 VLPQAAQPAFAFS-AREIVLLGRYPHARRAGALTHRDGEIAWQALALAGAtalvgrdvttLSGGELARVQFARVLaqlwp 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 157 ----IHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13547 166 phdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-201 |
2.97e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 78.07 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS----AALAEAREDtrlmfqdsrLLPWKR 105
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTklevAYFDQHRAE---------LDPEKT 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLG-----LRGDWRaKALQALRAVGLA-ERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDaltrIE 179
Cdd:PRK11147 400 VMDNLAEGkqevmVNGRPR-HVLGYLQDFLFHpKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD----VE 474
|
170 180
....*....|....*....|..
gi 15598638 180 MQQLIEGLWREHGFTVLLVTHD 201
Cdd:PRK11147 475 TLELLEELLDSYQGTVLLVSHD 496
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
21-218 |
5.61e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.14 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGL--------DQPSRGELLAGSAALAEAREDTR 92
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 LMFQDSRLLPWKRVIDNVGLG----LRG--DWRA---KALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLL 163
Cdd:NF040905 82 IIHQELALIPYLSIAENIFLGneraKRGviDWNEtnrRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 164 LLDEPLGAL-----DALTriemqQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:NF040905 162 ILDEPTAALneedsAALL-----DLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
35-218 |
7.73e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 77.26 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaeaREDTRLMF--QDSRLLPwKRVIDNVGL 112
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------KHSGRISFspQTSWIMP-GTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 113 GLRGD-WRAKALqaLRAVGLAERANEWP-----------AALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEM 180
Cdd:TIGR01271 510 GLSYDeYRYTSV--IKACQLEEDIALFPekdktvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
170 180 190
....*....|....*....|....*....|....*....
gi 15598638 181 -QQLIEGLWREHgfTVLLVTHDVsEAVAVADRVILIEDG 218
Cdd:TIGR01271 588 fESCLCKLMSNK--TRILVTSKL-EHLKKADKILLLHEG 623
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-220 |
1.98e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.70 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTRLMF-QDS 98
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYAQDHAYDFeNDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 99 RLLPWKrvidnvglglrGDWRAKA--LQALRAVgL------AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLG 170
Cdd:PRK15064 400 TLFDWM-----------SQWRQEGddEQAVRGT-LgrllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 171 ALDaLTRIEMQQL----IEGlwrehgfTVLLVTHD---VSeavAVADRVILIEDGEI 220
Cdd:PRK15064 468 HMD-MESIESLNMalekYEG-------TLIFVSHDrefVS---SLATRIIEITPDGV 513
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
31-220 |
2.66e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 73.18 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLD--QPSRGE-LLAGSAALAE-----AREDTRLMFQD----- 97
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSiLLDGEDILELspderARAGIFLAFQYpveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 ----SRLLpwKRVIDNVGLGL--RGDWRAKALQALRAVGL----AERA-NEwpaALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:COG0396 91 gvsvSNFL--RTALNARRGEElsAREFLKLLKEKMKELGLdedfLDRYvNE---GFSGGEKKRNEILQMLLLEPKLAILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598638 167 EPLGALD--ALtRIemqqLIEGLWREH--GFTVLLVTHdvSEAV---AVADRVILIEDGEI 220
Cdd:COG0396 166 ETDSGLDidAL-RI----VAEGVNKLRspDRGILIITH--YQRIldyIKPDFVHVLVDGRI 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-220 |
3.65e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 33 REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG-SAAL---------AEAReDTRLMFQDSRLlp 102
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAErSIAYvpqqawimnATVR-GNILFFDEEDA-- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 103 wKRVIDNVglglrgdwRAKALQA---LRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT--R 177
Cdd:PTZ00243 750 -ARLADAV--------RVSQLEAdlaQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVgeR 820
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598638 178 IeMQQLIEGlwREHGFTVLLVTHDVsEAVAVADRVILIEDGEI 220
Cdd:PTZ00243 821 V-VEECFLG--ALAGKTRVLATHQV-HVVPRADYVVALGDGRV 859
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-220 |
5.12e-15 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 74.98 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLR-LLAGLDQPSRGELLAGSAALAEAREdtrlMFQDSRLLpwkrviDN 109
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMKGSVAYVPQQA----WIQNDSLR------EN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 110 V--GLGLRGDWRAKALQA------LRAVGLAERAN--EWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA-LTRI 178
Cdd:TIGR00957 719 IlfGKALNEKYYQQVLEAcallpdLEILPSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKH 798
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 179 EMQQLI--EGLWRehGFTVLLVTHDVSEAVAVaDRVILIEDGEI 220
Cdd:TIGR00957 799 IFEHVIgpEGVLK--NKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-216 |
5.51e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTRLMFQDSRLLPWK---RVIDNVG 111
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRQALQKNLVAYVPQSEEVDWSfpvLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 112 LGLRGD--W--------RAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQ 181
Cdd:PRK15056 103 MGRYGHmgWlrrakkrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180 190
....*....|....*....|....*....|....*
gi 15598638 182 QLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIE 216
Cdd:PRK15056 183 SLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-213 |
5.53e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 5.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAG-------------------LDQ-PSRGE-------LLAGSA 82
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevllddgriiyeqdlivarLQQdPPRNVegtvydfVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 83 ALAEARED----TRLMFQD------SRLLPWKRVIDNVGLglrgdWR--AKALQALRAVGLAerANEWPAALSGGQKQRV 150
Cdd:PRK11147 93 EQAEYLKRyhdiSHLVETDpseknlNELAKLQEQLDHHNL-----WQleNRINEVLAQLGLD--PDAALSSLSGGWLRKA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598638 151 ALARALIHEPRLLLLDEPLGALDaltrIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVI 213
Cdd:PRK11147 166 ALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-220 |
6.26e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.29 E-value: 6.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGV-ARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL--------AGSAALAEAR--- 88
Cdd:COG3845 258 LEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldgeditgLSPRERRRLGvay 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 89 --EDtRL--------------MFQDSRLLPWKR--VIDnvglglRGDWRAKALQAL-----RAVGLAERAnewpAALSGG 145
Cdd:COG3845 338 ipED-RLgrglvpdmsvaenlILGRYRRPPFSRggFLD------RKAIRAFAEELIeefdvRTPGPDTPA----RSLSGG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 146 QKQRVALARALIHEPRLLLLDEPlgaldalTR------IEM--QQLIEGlwREHGFTVLLVTHDVSEAVAVADRVILIED 217
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQP-------TRgldvgaIEFihQRLLEL--RDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
...
gi 15598638 218 GEI 220
Cdd:COG3845 478 GRI 480
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
47-220 |
7.62e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 7.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 47 QFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG----SAALAEAREDTRLMFQDSRLLPWKRVIDNVGL--GLRG-DWR 119
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGgkdiETNLDAVRQSLGMCPQHNILFHHLTVAEHILFyaQLKGrSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 120 AKALQA---LRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIegLWREHGFTVL 196
Cdd:TIGR01257 1037 EAQLEMeamLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTII 1114
|
170 180
....*....|....*....|....
gi 15598638 197 LVTHDVSEAVAVADRVILIEDGEI 220
Cdd:TIGR01257 1115 MSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-220 |
1.38e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.62 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRllAGLdqpsrGELLAGSAALAEAREDTRLMFQDSrllpW---KRVI 107
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS--AML-----GELPPRSDASVVIRGTVAYVPQVS----WifnATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNVGLGLRGDwRAKALQALRAVGLAERANEWPAA-----------LSGGQKQRVALARALIHEPRLLLLDEPLGALDA-L 175
Cdd:PLN03130 697 DNILFGSPFD-PERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLWRehGFTVLLVTHDVSEAVAVaDRVILIEDGEI 220
Cdd:PLN03130 776 GRQVFDKCIKDELR--GKTRVLVTNQLHFLSQV-DRIILVHEGMI 817
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
35-242 |
1.52e-14 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.44 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-----AGSAALAEAREDTRLMFQDSRLLPWKRVIDN 109
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIidglnIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 110 VGLGLRGD---WRAKALQALRAV------GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDaltrIEM 180
Cdd:TIGR00957 1381 DPFSQYSDeevWWALELAHLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD----LET 1456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 181 QQLIEGLWREH--GFTVLLVTHDVSeAVAVADRVILIEDGEIG-LDLPVELPRPRS--RGSARLAAL 242
Cdd:TIGR00957 1457 DNLIQSTIRTQfeDCTVLTIAHRLN-TIMDYTRVIVLDKGEVAeFGAPSNLLQQRGifYSMAKDAGL 1522
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
43-220 |
2.66e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.70 E-value: 2.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 43 VPAGQFVAIVGRSGCGKS-TLLRLLAGLDQPSR----------GELLAGSAAlaEARE----DTRLMFQD--SRLLPWKR 105
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRvmaeklefngQDLQRISEK--ERRNlvgaEVAMIFQDpmTSLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 V-------IDNVGLGLRGDWRAKALQALRAVGL---AERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:PRK11022 108 VgfqimeaIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15598638 176 TRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK11022 188 IQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-200 |
2.95e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 30 FGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEARE--DTRLMF--QDSRLLPWKR 105
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyQKQLCFvgHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 106 VIDNVGLGLRGDWRAKALQALRAVGLAERANEWPAAL-SGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLI 184
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLlSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170
....*....|....*.
gi 15598638 185 EGlWREHGFTVLLVTH 200
Cdd:PRK13540 171 QE-HRAKGGAVLLTSH 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-239 |
3.13e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.46 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 24 RGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAAlaEARE-DTRL----MFQD 97
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLFGQPV--DAGDiATRRrvgyMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDNVGLGLR------GDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:NF033858 348 FSLYGELTVRQNLELHARlfhlpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 172 LDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAvAVADRVILIEDGEI-GLDLPVELprPRSRGSARL 239
Cdd:NF033858 428 VDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVlASDTPAAL--VAARGAATL 493
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
28-220 |
4.91e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.83 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 28 RRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPS---RGELLAGSAALAEAREdtrlmfqdsrllPWK 104
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE------------KYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 105 RVIDNVGlglRGDWRAKAL---QALRAVGLAeRANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQ 181
Cdd:cd03233 83 GEIIYVS---EEDVHFPTLtvrETLDFALRC-KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15598638 182 QLIEGLWREHGFTVLLVTHDVS-EAVAVADRVILIEDGEI 220
Cdd:cd03233 159 KCIRTMADVLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQ 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-220 |
5.50e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.62 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 27 ARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLD------QPSRgeLLAGSAALAE-------------- 86
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgvkgSGSV--LLNGMPIDAKemraisayvqqddl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 87 ------AREDtrLMFQdSRLlpwkRVIDNVGLGLRgdwRAKALQALRAVGLAERAN------EWPAALSGGQKQRVALAR 154
Cdd:TIGR00955 110 fiptltVREH--LMFQ-AHL----RMPRRVTKKEK---RERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 155 ALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHD-VSEAVAVADRVILIEDGEI 220
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
23-227 |
7.38e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSG---------------------------CGKSTLLRLLAGLDQPSRG 75
Cdd:NF000106 16 VRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*Gaa**rgalpahv*gpdagrrpwrf*twCANRRALRRTIG*HRPVR* 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 76 ellaGSAALAEAREDtrlMFQDSRLLPWKRvidnvglglrGDWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARA 155
Cdd:NF000106 96 ----GRRESFSGREN---LYMIGR*LDLSR----------KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598638 156 LIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLPVE 227
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVD 229
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-221 |
8.62e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 70.90 E-value: 8.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEARED-----------TRLMFQDSrl 100
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswrsrlavvsqTPFLFSDT-- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 lpwkrVIDNVGLGlRGDwrAKALQALRAVGLAE--------------RANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:PRK10789 405 -----VANNIALG-RPD--ATQQEIEHVARLASvhddilrlpqgydtEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 167 EPLGALDALTRiemQQLIEGL--WREhGFTVLLVTHDVSeAVAVADRVILIEDGEIG 221
Cdd:PRK10789 477 DALSAVDGRTE---HQILHNLrqWGE-GRTVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-220 |
8.95e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.10 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLdQPSRGELLAGSAALAE------AREdtRLMF-QDSRLLPWKRVID 108
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwsaaelARH--RAYLsQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLRGDWRAKALQAL-----RAVGLAERANEWPAALSGGQKQRVALARAL--IH-----EPRLLLLDEPLGALDALT 176
Cdd:COG4138 89 YLALHQPAGASSEAVEQLlaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptinpEGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15598638 177 RIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:COG4138 169 QAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-220 |
1.33e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 70.20 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDL-LVPaGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAE--------ARED 90
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLnLVP-GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYfaqhqlefLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 91 TRLMFQDSRLLPW---KRVIDNVG-LGLRGDwrakalqalravglaeRANEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:PRK10636 392 ESPLQHLARLAPQeleQKLRDYLGgFGFQGD----------------KVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 15598638 167 EPLGALDALTRiemQQLIEGLWREHGFTVlLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10636 456 EPTNHLDLDMR---QALTEALIDFEGALV-VVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
43-200 |
1.53e-13 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 70.16 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 43 VPAGQFVAIVGRSGCGKSTLLRLLAGLdQPSRGELLAGSAA-----LAEAREDTRLMFQDSRLLPwKRVIDNVGLGLRGD 117
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAKgklfyVPQRPYMTLGTLRDQIIYP-DSSEDMKRRGLSDK 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 118 WRAKALQALRAVGLAERANEWPAA------LSGGQKQRVALARALIHEPRLLLLDEPLGALDaltrIEMQQLIEGLWREH 191
Cdd:TIGR00954 553 DLEQILDNVQLTHILEREGGWSAVqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVS----VDVEGYMYRLCREF 628
|
....*....
gi 15598638 192 GFTVLLVTH 200
Cdd:TIGR00954 629 GITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
41-203 |
1.68e-13 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 68.55 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 41 LLVPA-GQFVAIVGRSGCGKSTLLRLLAGLDQPSRG------------ELLAGSA------ALAEAREDTRLMFQDSRLL 101
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeilDEFRGSElqnyftKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 PwKRVIDNVGLGL-RGDWRAK---ALQALRAVGLAERANEwpaALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTR 177
Cdd:cd03236 100 P-KAVKGKVGELLkKKDERGKldeLVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|....*.
gi 15598638 178 IEMQQLIEGLwREHGFTVLLVTHDVS 203
Cdd:cd03236 176 LNAARLIREL-AEDDNYVLVVEHDLA 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-225 |
2.09e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE----------------LLAGSAALAEAREDTRLmFQD 97
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRimlngkeinalstaqrLARGLVYLPEDRQSSGL-YLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLlPWKR---VIDNVGLGLRGDWRAKALQAL-RAVGLAERANEWPA-ALSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:PRK15439 356 APL-AWNVcalTHNRRGFWIKPARENAVLERYrRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 173 DALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLP 225
Cdd:PRK15439 435 DVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALT 486
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-201 |
2.15e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.58 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 24 RGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGsaalaearEDTRLMFQD-SR--L 100
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--------ETVKLAYVDqSRdaL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVGLGLR----GDWRAKALQALRAVGLAERANEWPA-ALSGGQKQRVALARALIHEPRLLLLDEPLGALDAL 175
Cdd:TIGR03719 398 DPNKTVWEEISGGLDiiklGKREIPSRAYVGRFNFKGSDQQKKVgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
170 180
....*....|....*....|....*.
gi 15598638 176 TrieMQQLIEGLwREHGFTVLLVTHD 201
Cdd:TIGR03719 478 T---LRALEEAL-LNFAGCAVVISHD 499
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-220 |
3.66e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.89 E-value: 3.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 20 PLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGlDQPS--------------RGELL------- 78
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQgysndltlfgrrrgSGETIwdikkhi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 79 --AGSAALAEAREDTRLmfqdsrllpwKRVI-----DNVGL--GLRGDWRAKALQALRAVGLAERANEWP-AALSGGQkQ 148
Cdd:PRK10938 339 gyVSSSLHLDYRVSTSV----------RNVIlsgffDSIGIyqAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQ-Q 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598638 149 RVAL-ARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVA-VADRVILIEDGEI 220
Cdd:PRK10938 408 RLALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPAcITHRLEFVPDGDI 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
11-220 |
6.08e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.46 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 11 TPQRLKRGIPLALRGVARRFGEREV-LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAALAEAR 88
Cdd:PRK10522 313 RPQAFPDWQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEiLLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 89 EDTRLM----FQDSRLLpwkrviDNVgLGLRGDWRAKALQA--LRAVGLAERANE-----WPAALSGGQKQRVALARALI 157
Cdd:PRK10522 393 EDYRKLfsavFTDFHLF------DQL-LGPEGKPANPALVEkwLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598638 158 HEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDvSEAVAVADRVILIEDGEI 220
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-219 |
7.75e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKS----TLLRLL--AGLDQPSRGELLA---------GSAALAEARE----DTRLMFQ 96
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRrrsrqvielSEQSAAQMRHvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 D--SRLLPWKRVIDNVGLGLR---GDWRAKALQALRAVGLAERANE-------WPAALSGGQKQRVALARALIHEPRLLL 164
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRlhqGASREEAMVEAKRMLDQVRIPEaqtilsrYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 165 LDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-220 |
1.07e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGldqpsrgELLAGSAALAEAREDTRLMFQdsrlLPW---KRVID 108
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-------ELSHAETSSVVIRGSVAYVPQ----VSWifnATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVGLGLRGD----WRAKALQALR----------AVGLAERAnewpAALSGGQKQRVALARALIHEPRLLLLDEPLGALDA 174
Cdd:PLN03232 698 NILFGSDFEseryWRAIDVTALQhdldllpgrdLTEIGERG----VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 175 LTrieMQQLIEGLWRE--HGFTVLLVTHDVsEAVAVADRVILIEDGEI 220
Cdd:PLN03232 774 HV---AHQVFDSCMKDelKGKTRVLVTNQL-HFLPLMDRIILVSEGMI 817
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
39-225 |
1.33e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 39 IDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL--AEAREDTR----LMFQDSR---LLPWKRVIDN 109
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdiRSPRDAIRagimLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 110 V-----------GLGLRGDWRAK-ALQALRAVGLAERANEWP-AALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:PRK11288 352 InisarrhhlraGCLINNRWEAEnADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 177 RIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEIGLDLP 225
Cdd:PRK11288 432 KHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGELA 479
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-218 |
1.84e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 18 GIPLALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPS--RGELLAGSAALA-EAREDTRLM 94
Cdd:PLN03211 66 GHKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTkQILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWKRVIDN-VGLGL--------RGDWRAKALQALRAVGLAE-----RANEWPAALSGGQKQRVALARALIHEP 160
Cdd:PLN03211 146 TQDDILYPHLTVRETlVFCSLlrlpksltKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 161 RLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAV-AVADRVILIEDG 218
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVyQMFDSVLVLSEG 283
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-228 |
3.32e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 34 EVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSA------ALAEAREDTRLMFQDSrLLPWKRVI 107
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdiNLKWWRSKIGVVSQDP-LLFSNSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNV--------------------------GLGLRGDWRAKA-------LQALRAVGLAERANEW---------------- 138
Cdd:PTZ00265 478 NNIkyslyslkdlealsnyynedgndsqeNKNKRNSCRAKCagdlndmSNTTDSNELIEMRKNYqtikdsevvdvskkvl 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 139 -------------------PAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVT 199
Cdd:PTZ00265 558 ihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
|
250 260
....*....|....*....|....*....
gi 15598638 200 HDVSeAVAVADRVILIEDGEIGLDLPVEL 228
Cdd:PTZ00265 638 HRLS-TIRYANTIFVLSNRERGSTVDVDI 665
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-220 |
4.03e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 65.97 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGERE-----VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL-AEAREDTRLM 94
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 ----FQD----SRLlpwkrvidnvgLGLRGDwrakalqalravGLAERANEWPA------------------ALSGGQKQ 148
Cdd:COG4615 408 fsavFSDfhlfDRL-----------LGLDGE------------ADPARARELLErleldhkvsvedgrfsttDLSQGQRK 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 149 RVALARALIhEPR-LLLLDEplGALD---ALTRIEMQQLIeGLWREHGFTVLLVTHDvSEAVAVADRVILIEDGEI 220
Cdd:COG4615 465 RLALLVALL-EDRpILVFDE--WAADqdpEFRRVFYTELL-PELKARGKTVIAISHD-DRYFDLADRVLKMDYGKL 535
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-220 |
4.55e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 24 RGVARRfgEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL----------------AGSAALAEA 87
Cdd:PRK09700 269 RNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRlngkdisprspldavkKGMAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 88 REDTRLM--FQDSRLLPWKRVIDNVGLGlrGDW-------------RAKALQALRAVGLAERANEwpaaLSGGQKQRVAL 152
Cdd:PRK09700 347 RRDNGFFpnFSIAQNMAISRSLKDGGYK--GAMglfhevdeqrtaeNQRELLALKCHSVNQNITE----LSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 153 ARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-221 |
5.41e-12 |
|
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: 65.58 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaeaREDTRLMFQDSRLLP--WKRVIDNVGLGLRGDWRAKAL 123
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKISYKPQYISPdyDGTVEEFLRSANTDDFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 124 QA--LRAVGLaERANEWPAA-LSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTH 200
Cdd:COG1245 436 KTeiIKPLGL-EKLLDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
170 180
....*....|....*....|.
gi 15598638 201 DVSEAVAVADRvILIEDGEIG 221
Cdd:COG1245 515 DIYLIDYISDR-LMVFEGEPG 534
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-221 |
1.04e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAG------------------SAALAEAREDtrlmFQDSrllPWKRVI 107
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyikpdydgtvEDLLRSITDD----LGSS---YYKSEI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 dnvglglrgdwrAKALQALRavgLAER-ANEwpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEG 186
Cdd:PRK13409 438 ------------IKPLQLER---LLDKnVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
|
170 180 190
....*....|....*....|....*....|....*
gi 15598638 187 LWREHGFTVLLVTHDVSEAVAVADRVILIEdGEIG 221
Cdd:PRK13409 499 IAEEREATALVVDHDIYMIDYISDRLMVFE-GEPG 532
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-216 |
1.66e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEArEDTRLMFQDSRL 100
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-DRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVG-----LGLRGdWRAKAL--QALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PRK13543 91 PGLKADLSTLEnlhflCGLHG-RRAKQMpgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15598638 174 ALTRIEMQQLIEGLWREHGFTvLLVTHDVSEAVAVADRVILIE 216
Cdd:PRK13543 170 LEGITLVNRMISAHLRGGGAA-LVTTHGAYAAPPVRTRMLTLE 211
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
49-220 |
1.95e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.11 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 49 VAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGS----AALAEAREDTrLMFQDSRLL---------PWKRVIDNVG-LGL 114
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkvrmAVFSQHHVDG-LDLSSNPLLymmrcfpgvPEQKLRAHLGsFGV 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 115 RGDWrakALQALRAvglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDaLTRIEmqQLIEGLWREHGfT 194
Cdd:PLN03073 617 TGNL---ALQPMYT-------------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-LDAVE--ALIQGLVLFQG-G 676
|
170 180
....*....|....*....|....*.
gi 15598638 195 VLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
43-218 |
2.33e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 63.88 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 43 VPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGE-LLAGSAALAEAREdtrlMFQDSRLLPWKRVIDNVGLG-------- 113
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDaTVAGKSILTNISD----VHQNMGYCPQFDAIDDLLTGrehlylya 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 114 -LRG----DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLW 188
Cdd:TIGR01257 2038 rLRGvpaeEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180 190
....*....|....*....|....*....|
gi 15598638 189 REhGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:TIGR01257 2118 RE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
140-224 |
3.38e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.92 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 140 AALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:TIGR02633 402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
....*
gi 15598638 220 IGLDL 224
Cdd:TIGR02633 481 LKGDF 485
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
39-215 |
3.86e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.23 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 39 IDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPS----------RG-ELLAGSAAlaEARE----DTRLMFQD--SRLL 101
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwNGiDLLKLSPR--ERRKiigrEIAMIFQEpsSCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 PWKRV-------IDNVGLG----LRGDWRAK-ALQALRAVGLAERA---NEWPAALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:COG4170 104 PSAKIgdqlieaIPSWTFKgkwwQRFKWRKKrAIELLHRVGIKDHKdimNSYPHELTEGECQKVMIAMAIANQPRLLIAD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15598638 167 EPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEAVAVADRVILI 215
Cdd:COG4170 184 EPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
46-221 |
4.27e-11 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 60.28 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELlagsaalaearedtrlmfqdsrllPWKRVidnvglglRGDWRAKALQa 125
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDND------------------------EWDGI--------TPVYKPQYID- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 126 lravglaeranewpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSEA 205
Cdd:cd03222 72 ----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVL 135
|
170
....*....|....*.
gi 15598638 206 VAVADRVILIEdGEIG 221
Cdd:cd03222 136 DYLSDRIHVFE-GEPG 150
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
142-227 |
4.73e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 142 LSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGlWREHGFTVLLVTHDVSEAVAVADRVILIEDGEIG 221
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQ-FKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
....*.
gi 15598638 222 LDLPVE 227
Cdd:PRK10762 475 GEFTRE 480
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
36-213 |
6.52e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 59.64 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLrllagldqpsrgelLAGSAALAEAR-EDTRLMFQDSRLLpwkrVIDNvglgl 114
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--------------NEGLYASGKARlISFLPKFSRNKLI----FIDQ----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 115 rgdwrakaLQALRAVGLAERANEWPAA-LSGGQKQRVALARALIHEPR--LLLLDEPLGALDaltRIEMQQLIEGL--WR 189
Cdd:cd03238 68 --------LQFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDINQLLEVIkgLI 136
|
170 180
....*....|....*....|....
gi 15598638 190 EHGFTVLLVTHDVsEAVAVADRVI 213
Cdd:cd03238 137 DLGNTVILIEHNL-DVLSSADWII 159
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
46-219 |
7.30e-11 |
|
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: 58.92 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAalaearedtrlmfqdsrllpwkrvidnvglglrgdwrAKALQA 125
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------------------------------------EDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 126 LRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIE-----GLWREHGFTVLLVTH 200
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTN 124
|
170 180
....*....|....*....|....
gi 15598638 201 DVS-----EAVAVADRVILIEDGE 219
Cdd:smart00382 125 DEKdlgpaLLRRRFDRRIVLLLIL 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
140-227 |
8.02e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.87 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 140 AALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
....*...
gi 15598638 220 IGLDLPVE 227
Cdd:PRK13549 483 LKGDLINH 490
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
25-175 |
1.05e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 25 GVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGsaalaearEDTRLMFQD-SR--LL 101
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--------ETVKLAYVDqSRdaLD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 PWKRVIDNVGLGLrgDW----------RA-------KALQALRAVGLaeranewpaaLSGGQKQRVALARALIHEPRLLL 164
Cdd:PRK11819 401 PNKTVWEEISGGL--DIikvgnreipsRAyvgrfnfKGGDQQKKVGV----------LSGGERNRLHLAKTLKQGGNVLL 468
|
170 180
....*....|....*....|
gi 15598638 165 LDEP--------LGAL-DAL 175
Cdd:PRK11819 469 LDEPtndldvetLRALeEAL 488
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
43-218 |
1.18e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.33 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 43 VPAGQFVAIVGRSGCGKSTLLRLLAGLdQPSRGELLAGSAALAE------AREDTRLMFQDSR--LLP-WKRVIDNVGLG 113
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwsaaelARHRAYLSQQQTPpfAMPvFQYLTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 114 LRGDWRAKALQAL-RAVGLAERANEWPAALSGGQKQRVALARAL--IH-----EPRLLLLDEPLGALDALTRIEMQQLIE 185
Cdd:PRK03695 98 TRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdinpAGQLLLLDEPMNSLDVAQQAALDRLLS 177
|
170 180 190
....*....|....*....|....*....|...
gi 15598638 186 GLWREhGFTVLLVTHDVSEAVAVADRVILIEDG 218
Cdd:PRK03695 178 ELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
29-216 |
4.07e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 29 RFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDTRLMFQDSrllpWKRVI 107
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGNWQLAWVNQETPALPQPA----LEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 D------------------NVG---------LGLRGDW--RAKALQALRAVGLAERANEWP-AALSGGQKQRVALARALI 157
Cdd:PRK10636 86 DgdreyrqleaqlhdanerNDGhaiatihgkLDAIDAWtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 158 HEPRLLLLDEPLGALDALTRIEMQQLIeglwREHGFTVLLVTHDVSEAVAVADRVILIE 216
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
31-216 |
4.59e-10 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.92 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLL----RLLAGLDQPSRGELLAGSAALAEAREDTRLMFQD--------- 97
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKvfifsgtfr 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 98 SRLLPWKRVIDnvglglRGDWRAKalqalRAVGLAERANEWPA-----------ALSGGQKQRVALARALIHEPRLLLLD 166
Cdd:TIGR01271 1310 KNLDPYEQWSD------EEIWKVA-----EEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15598638 167 EPLGALDALTrieMQQLIEGLwrEHGF---TVLLVTHDVsEAVAVADRVILIE 216
Cdd:TIGR01271 1379 EPSAHLDPVT---LQIIRKTL--KQSFsncTVILSEHRV-EALLECQQFLVIE 1425
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
115-212 |
5.56e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 115 RGDWRA-KALQALRAVGLAERAN---EWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWRE 190
Cdd:PRK15093 128 RFGWRKrRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQN 207
|
90 100
....*....|....*....|..
gi 15598638 191 HGFTVLLVTHDVSEAVAVADRV 212
Cdd:PRK15093 208 NNTTILLISHDLQMLSQWADKI 229
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
141-217 |
8.38e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 8.38e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 141 ALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSeAVAVADRVILIED 217
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNN 1433
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
35-220 |
2.30e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.79 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTL----LRLLAGLDQPSRGELLAGSAALAEAREDTRLMFQDSRLL--PWKRVID 108
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFsgTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NvglglRGDWRAKAL-QALRAVGLAERANEWPA-----------ALSGGQKQRVALARALIHEPRLLLLDEPLGALDALT 176
Cdd:cd03289 99 P-----YGKWSDEEIwKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15598638 177 riemQQLIEGLWReHGF---TVLLVTHDVsEAVAVADRVILIEDGEI 220
Cdd:cd03289 174 ----YQVIRKTLK-QAFadcTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-228 |
2.31e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAE-AREDTRLMFQdsrLLPWKRVIDNVGLG 113
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLS---IIPQSPVLFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 114 LRGD----------WRAKALQALRAV------GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTR 177
Cdd:PLN03232 1328 FNIDpfsehndadlWEALERAHIKDVidrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15598638 178 IEMQQLIEGLWREhgFTVLLVTHDVSEAVAvADRVILIEDGEI-GLDLPVEL 228
Cdd:PLN03232 1408 SLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVlEYDSPQEL 1456
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
46-201 |
3.12e-09 |
|
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: 57.10 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGL---------DQPSRGELL---AGSA------ALAEAREDTRLMFQDSRLLPwKRVI 107
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGElkpnlgdydEEPSWDEVLkrfRGTElqdyfkKLANGEIKVAHKPQYVDLIP-KVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNVGLGLRG-DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEG 186
Cdd:COG1245 178 GTVRELLEKvDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
170
....*....|....*
gi 15598638 187 LWREhGFTVLLVTHD 201
Cdd:COG1245 258 LAEE-GKYVLVVEHD 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-173 |
6.08e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLA--GLDQ-PSRGELL------------AGSAALAEAREDTRLMF 95
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhAIDGiPKNCQILhveqevvgddttALQCVLNTDIERTQLLE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 96 QDSRLLPWKRVIDNVGL----------GLRGDWRA-------KALQALRAVGLAERANEWPAALS--------------G 144
Cdd:PLN03073 268 EEAQLVAQQRELEFETEtgkgkgankdGVDKDAVSqrleeiyKRLELIDAYTAEARAASILAGLSftpemqvkatktfsG 347
|
170 180
....*....|....*....|....*....
gi 15598638 145 GQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PLN03073 348 GWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-232 |
6.88e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.33 E-value: 6.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 14 RLKRGIPLALRGVARRFGEREVlkdidllvpagqfVAIVGRSGCGKSTLLRLLAGLDQPSRGELLA-----GSAALAEAR 88
Cdd:PTZ00243 1317 RYREGLPLVLRGVSFRIAPREK-------------VGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVngreiGAYGLRELR 1383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 89 EDTRLMFQDSRLLPwKRVIDNVGLGLRGD----WRAKALQALR------AVGLAERANEWPAALSGGQKQRVALARALIH 158
Cdd:PTZ00243 1384 RQFSMIPQDPVLFD-GTVRQNVDPFLEASsaevWAALELVGLRervaseSEGIDSRVLEGGSNYSVGQRQLMCMARALLK 1462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598638 159 EPR-LLLLDEPLGALD-ALTRiEMQQLIEGLWREHgfTVLLVTHDVsEAVAVADRVILIEDGEIGldlpvELPRPR 232
Cdd:PTZ00243 1463 KGSgFILMDEATANIDpALDR-QIQATVMSAFSAY--TVITIAHRL-HTVAQYDKIIVMDHGAVA-----EMGSPR 1529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-219 |
7.56e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 7.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 23 LRGVARRFGEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAAL-----AEAREDTRLMF-Q 96
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkssKEALENGISMVhQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 97 DSRLLPWKRVIDNVGLG---LRGDW--RAKALQALRAV----GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDE 167
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrypTKGMFvdQDKMYRDTKAIfdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 168 PlgaLDALTRIEMQQL---IEGLwREHGFTVLLVTHDVSEAVAVADRVILIEDGE 219
Cdd:PRK10982 161 P---TSSLTEKEVNHLftiIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
46-201 |
8.44e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 8.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 46 GQFVAIVGRSGCGKSTLLRLLAGL---------DQPSRGELL---AGSA------ALAEAREDTRLMFQDSRLLPwKRVI 107
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSWDEVLkrfRGTElqnyfkKLYNGEIKVVHKPQYVDLIP-KVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 DNVGLGLRG-DWRAKALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEG 186
Cdd:PRK13409 178 GKVRELLKKvDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRE 257
|
170
....*....|....*
gi 15598638 187 LWREHgfTVLLVTHD 201
Cdd:PRK13409 258 LAEGK--YVLVVEHD 270
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
36-220 |
2.98e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.13 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAredtrlmfqDSRLLPWKRVIDNVGL-G 113
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVdIKGSAALIAI---------SSGLNGQLTGIENIELkG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 114 LRGDWRAKALQAL--RAVGLAERA---NEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD-ALTRIEMQQLIEgl 187
Cdd:PRK13545 111 LMMGLTKEKIKEIipEIIEFADIGkfiYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDKMNE-- 188
|
170 180 190
....*....|....*....|....*....|...
gi 15598638 188 WREHGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK13545 189 FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
40-217 |
3.07e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 40 DLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAgsaalaEAREDTRLMF-QDSRLLP--WKR--------VID 108
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQS------QFSHITRLSFeQLQKLVSdeWQRnntdmlspGED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 109 NVG--------LGLRGDWRAKALQALRAVG-LAERANEWpaaLSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIE 179
Cdd:PRK10938 97 DTGrttaeiiqDEVKDPARCEQLAQQFGITaLLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 15598638 180 MQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIED 217
Cdd:PRK10938 174 LAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-220 |
3.63e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 141 ALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEI 220
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-216 |
3.97e-08 |
|
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: 52.22 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 21 LALRGVaRRFGEREVlkdIDLLVPagqFVAIVGRSGCGKSTLLR-LLAGL--DQPSRGELLAGSAALA---EAREDTRLM 94
Cdd:cd03240 4 LSIRNI-RSFHERSE---IEFFSP---LTLIVGQNGAGKTTIIEaLKYALtgELPPNSKGGAHDPKLIregEVRAQVKLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSRLLPWK-----RVIDNVGLGLRGDWRAKALqalravglaeranEWPAALSGGQKQ------RVALARALIHEPRLL 163
Cdd:cd03240 77 FENANGKKYTitrslAILENVIFCHQGESNWPLL-------------DMRGRCSGGEKVlasliiRLALAETFGSNCGIL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15598638 164 LLDEPLGALDAlTRIEMQ--QLIEGLWREHGFTVLLVTHDvSEAVAVADRVILIE 216
Cdd:cd03240 144 ALDEPTTNLDE-ENIEESlaEIIEERKSQKNFQLIVITHD-EELVDAADHIYRVE 196
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
31-218 |
5.21e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 51.86 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPS--RGELLAGSAALAE--AREDTRLMFQDsrllpwkrv 106
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKnfQRSTGYVEQQD--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 107 IDNVGLGLRGDWRAKALqaLRavglaeranewpaALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEG 186
Cdd:cd03232 89 VHSPNLTVREALRFSAL--LR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
170 180 190
....*....|....*....|....*....|...
gi 15598638 187 LwREHGFTVLLVTHDVSEAV-AVADRVILIEDG 218
Cdd:cd03232 154 L-ADSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
31-178 |
1.79e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGldQPS----RGELLAGSAALAEAREDTR------LMFQDSRL 100
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERahlgifLAFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LP------WKRVIDNVGLGLRGDWRAKALQ-------ALRAVGLAER-----ANEwpaALSGGQKQRVALARALIHEPRL 162
Cdd:CHL00131 96 IPgvsnadFLRLAYNSKRKFQGLPELDPLEfleiineKLKLVGMDPSflsrnVNE---GFSGGEKKRNEILQMALLDSEL 172
|
170
....*....|....*...
gi 15598638 163 LLLDEPLGAL--DALTRI 178
Cdd:CHL00131 173 AILDETDSGLdiDALKII 190
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
31-213 |
1.84e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 49.67 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLR---LLAGLDQPSRGELLAGSAALAEAREDTRLMFQDSRLlpwkrvi 107
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQL------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 108 dnvglglrgdwrakalqalravglaeranewpaalSGGQKQRVALARALIHE---PR-LLLLDEPLGALDALTRIEMQQL 183
Cdd:cd03227 79 -----------------------------------SGGEKELSALALILALAslkPRpLYILDEIDRGLDPRDGQALAEA 123
|
170 180 190
....*....|....*....|....*....|
gi 15598638 184 IEGLwREHGFTVLLVTHDvSEAVAVADRVI 213
Cdd:cd03227 124 ILEH-LVKGAQVIVITHL-PELAELADKLI 151
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
36-213 |
3.13e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 49.95 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLL---------------------RLLAGLDQPSRGELLAGSAALAEareDTRLM 94
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAIAI---DQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 95 FQDSR--------LLPWKRVI-DNVGLGLRgdwrakaLQALRAVGLA----ERANEwpaALSGGQKQRVALARALIHEPR 161
Cdd:cd03270 88 SRNPRstvgtvteIYDYLRLLfARVGIRER-------LGFLVDVGLGyltlSRSAP---TLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15598638 162 --LLLLDEP-LGaldaLTRIEMQQLIEGL--WREHGFTVLLVTHDvSEAVAVADRVI 213
Cdd:cd03270 158 gvLYVLDEPsIG----LHPRDNDRLIETLkrLRDLGNTVLVVEHD-EDTIRAADHVI 209
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
52-201 |
3.82e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 52 VGRSGCGKSTLLRLLAGLDQPSRGEL-LAGSAALAEAREDtRLMFQDsrllpwKRVIDNVGLGLRGDWRAK----ALQAL 126
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQD-QFAFEE------FTVLDTVIMGHTELWEVKqerdRIYAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 127 ----------------------------RA------VGLAERANEWP-AALSGGQKQRVALARALIHEPRLLLLDEPLGA 171
Cdd:PRK15064 106 pemseedgmkvadlevkfaemdgytaeaRAgelllgVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNN 185
|
170 180 190
....*....|....*....|....*....|
gi 15598638 172 LDaltrIEMQQLIEGLWREHGFTVLLVTHD 201
Cdd:PRK15064 186 LD----INTIRWLEDVLNERNSTMIIISHD 211
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
33-220 |
6.61e-07 |
|
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: 49.14 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 33 REVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEA-----REDTRLMFQDSRLL------ 101
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLplhtlRSRLSIILQDPILFsgsirf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 102 ---PWKRVIDNVglglrgDWRAKALQALRAV------GLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGAL 172
Cdd:cd03288 114 nldPECKCTDDR------LWEALEIAQLKNMvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15598638 173 DALTRIEMQQLIEGLWREHgfTVLLVTHDVSeAVAVADRVILIEDGEI 220
Cdd:cd03288 188 DMATENILQKVVMTAFADR--TVVTIAHRVS-TILDADLVLVLSRGIL 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-228 |
1.10e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELL-----AGSAALAEARE------DTRLMFQDS---RL 100
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILidgcdISKFGLMDLRKvlgiipQAPVLFSGTvrfNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDnvglglrGD-W----RAKALQALR--AVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALD 173
Cdd:PLN03130 1334 DPFNEHND-------ADlWesleRAHLKDVIRrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 174 ALTRIEMQQLIeglwREH--GFTVLLVTHDVSeAVAVADRVILIEDGEI-GLDLPVEL 228
Cdd:PLN03130 1407 VRTDALIQKTI----REEfkSCTMLIIAHRLN-TIIDCDRILVLDAGRVvEFDTPENL 1459
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-218 |
1.82e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 140 AALSGGQKQRVALARALIHEPR--LLLLDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDvSEAVAVADRVILIED 217
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHD-EQMISLADRIIDIGP 552
|
.
gi 15598638 218 G 218
Cdd:PRK00635 553 G 553
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
35-201 |
1.49e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 45.05 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 35 VLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAgsaalaeAREDTRLMFQDSRLLPWKRVIDNVGL-- 112
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIG-------LRGDALPLGANSFILPGLTGEENARMma 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 113 ---GLRGDWRAKALQALRAVG--LAERANEWPAALsggqKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGL 187
Cdd:PRK15177 75 slyGLDGDEFSHFCYQLTQLEqcYTDRVSEYSVTM----KTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALACQ 150
|
170
....*....|....
gi 15598638 188 WREHGFTVLlvTHD 201
Cdd:PRK15177 151 LQQKGLIVL--THN 162
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-220 |
1.87e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAG-LDQPSRG-----------------ELLAGSAALAEAreDTR- 92
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIGvegvitydgitpeeikkHYRGDVVYNAET--DVHf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 93 --LMFQDS-----RLlpwkRVIDNVGLGLRGDWRAKALQ--ALRAVGLAER-----ANEWPAALSGGQKQRVALARALIH 158
Cdd:TIGR00956 151 phLTVGETldfaaRC----KTPQNRPDGVSREEYAKHIAdvYMATYGLSHTrntkvGNDFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598638 159 EPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGFTVLLVTHDVSE-AVAVADRVILIEDGEI 220
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQ 289
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-200 |
3.61e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQPSRGELLAGSAALAEARE----------DTRL-MFQDSRL 100
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyighnlGLKLeMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 101 LPWKRVIDNVGLglrgdwrakALQALRAVGLAERANEWPAALSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEM 180
Cdd:PRK13541 92 KFWSEIYNSAET---------LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|
gi 15598638 181 QQLIeGLWREHGFTVLLVTH 200
Cdd:PRK13541 163 NNLI-VMKANSGGIVLLSSH 181
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
36-63 |
6.77e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 6.77e-05
10 20
....*....|....*....|....*...
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLL 63
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
36-213 |
1.02e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.60 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLL----------RLLAGLDQPSRGELLAGSAAL--------------------- 84
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDRIEGLEHIdkvividqspigrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 85 -AEAREDTRLMFQDS----RLLP------WK-RVIDNVgLGLRGDWRAK----------ALQALRAVGLAERANEWPAA- 141
Cdd:cd03271 91 yTGVFDEIRELFCEVckgkRYNRetlevrYKgKSIADV-LDMTVEEALEffenipkiarKLQTLCDVGLGYIKLGQPATt 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 142 LSGGQKQRVALARALIHEPR---LLLLDEPLGAL---DaltrieMQQLIEGLWR--EHGFTVLLVTHDVsEAVAVADRVI 213
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhD------VKKLLEVLQRlvDKGNTVVVIEHNL-DVIKCADWII 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
31-218 |
1.33e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 31 GEREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAG------------------LD---QPSRG-------------- 75
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvttgvitggdrlvngrpLDssfQRSIGyvqqqdlhlptstv 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 76 -ELLAGSAALAEAREDTR---LMFQDSrllpwkrVIDNVGLglrgDWRAKALqalraVGLAEranewpAALSGGQKQRVA 151
Cdd:TIGR00956 854 rESLRFSAYLRQPKSVSKsekMEYVEE-------VIKLLEM----ESYADAV-----VGVPG------EGLNVEQRKRLT 911
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 152 LARALIHEPRLLL-LDEPLGALDALTRIEMQQLIEGLwREHGFTVLLVTHDVSeAVAVA--DRVILIEDG 218
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQPS-AILFEefDRLLLLQKG 979
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
36-63 |
1.55e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.55e-04
10 20
....*....|....*....|....*...
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTLL 63
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
120-213 |
2.30e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 120 AKALQALRAVGLaeranEW-----PAA-LSGGQKQRVALARALI---HEPRLLLLDEP------------LGALDALtri 178
Cdd:COG0178 804 ARKLQTLQDVGL-----GYiklgqPATtLSGGEAQRVKLASELSkrsTGKTLYILDEPttglhfhdirklLEVLHRL--- 875
|
90 100 110
....*....|....*....|....*....|....*..
gi 15598638 179 emqqlieglwREHGFTVLLVTH--DVseaVAVADRVI 213
Cdd:COG0178 876 ----------VDKGNTVVVIEHnlDV---IKTADWII 899
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
36-62 |
4.53e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 4.53e-04
10 20
....*....|....*....|....*..
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTL 62
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTL 647
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
142-215 |
5.07e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598638 142 LSGGQKQRVALARALIHEPR--LLLLDEP-LGaldaLTRIEMQQLIEGL--WREHGFTVLLVTHDvSEAVAVADRVILI 215
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPsIG----LHQRDNRRLINTLkrLRDLGNTLIVVEHD-EDTIRAADYVIDI 562
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
141-221 |
5.30e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 141 ALSGGQKQRVALARALIH---EPRLLLLDEPLGALDALtriEMQQLIEGLWR--EHGFTVLLVTHDVsEAVAVADRVILI 215
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTH---DIKALIYVLQSltHQGHTVVIIEHNM-HVVKVADYVLEL 884
|
....*...
gi 15598638 216 --EDGEIG 221
Cdd:PRK00635 885 gpEGGNLG 892
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
31-62 |
1.32e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 1.32e-03
10 20 30
....*....|....*....|....*....|...
gi 15598638 31 GERE-VLKDIDLLVPAGQFVAIVGRSGCGKSTL 62
Cdd:TIGR00630 6 GAREhNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
141-210 |
1.37e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598638 141 ALSGGQKQ------RVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREHGF--TVLLVTHDvSEAVAVAD 210
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDipQVIMISHH-RELLSVAD 877
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
142-227 |
2.22e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 142 LSGGQKQRVALARALIHEPRLLLLDEPLGALDALTRIEMQQLIEGLWREhGFTVLLVTHDVSEAVAVADRVILIEDGEIG 221
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
....*.
gi 15598638 222 LDLPVE 227
Cdd:NF040905 484 GELPRE 489
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
48-68 |
2.34e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 36.83 E-value: 2.34e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-213 |
2.52e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598638 120 AKALQALRAVGLAERANEWPA-ALSGGQKQRVALARALIHE---PRLLLLDEPLGAL---DaltrieMQQLIEGLWR--E 190
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdD------IKKLLEVLQRlvD 880
|
90 100
....*....|....*....|....*
gi 15598638 191 HGFTVLLVTH--DVseaVAVADRVI 213
Cdd:TIGR00630 881 KGNTVVVIEHnlDV---IKTADYII 902
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
32-71 |
5.39e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 37.46 E-value: 5.39e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 15598638 32 EREVLKDIDLLVPAGQFVAIVGRSGCGKSTLLRLLAGLDQ 71
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRED 52
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
36-62 |
6.82e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 6.82e-03
10 20
....*....|....*....|....*..
gi 15598638 36 LKDIDLLVPAGQFVAIVGRSGCGKSTL 62
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| |
