|
Name |
Accession |
Description |
Interval |
E-value |
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
20-215 |
7.42e-82 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 250.40 E-value: 7.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDekefLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:COG3842 23 DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPdSGRILLDGRDVTG----LPPEKRNVGMVFQDYALFPHLTVAENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:COG3842 99 AFglrmrgVPKAeiRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG3842 179 RRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
20-216 |
9.10e-77 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 236.97 E-value: 9.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWqdeKEFLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:COG1118 20 DVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPdSGRIVLNGRDL---FTNLPPRERRVGFVFQHYALFPHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:COG1118 97 AFglrvrpPSKAeiRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1118 177 RRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
20-210 |
7.44e-74 |
|
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: 225.09 E-value: 7.44e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQDekefLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03259 18 DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILIDGRDVTG----VPPERRNIGMVFQDYALFPHLTVAENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF------VNKDKELANH--LLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:cd03259 94 AFglklrgVPKAEIRARVreLLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03259 174 KELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
20-211 |
1.17e-73 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 229.19 E-value: 1.17e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDekefLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:COG3839 21 DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEILIGGRDVTD----LPPKDRNIAMVFQSYALYPHMTVYENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:COG3839 97 AFplklrkVPKAeiDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:COG3839 177 KRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-216 |
2.98e-73 |
|
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: 228.45 E-value: 2.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEIKKELHGSNgvmnLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDEKE--FLPVQKR 77
Cdd:COG4148 2 MLEVDFRLRRGGFT----LDVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPdSGRIRLGGEVLQDSARgiFLPPHRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 78 KIGFVFQDYALFPNMTVLENLFF------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLM 151
Cdd:COG4148 78 RIGYVFQEARLFPHLSVRGNLLYgrkrapRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 152 DEPLSALDPTMRiklqDEIL----QLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4148 158 DEPLAALDLARK----AEILpyleRLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
20-209 |
1.38e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 223.43 E-value: 1.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdekeflPVQK--RKIGFVFQDYALFPNMTVLE 96
Cdd:COG1116 29 DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtSGEVLVDGK---------PVTGpgPDRGVVFQEPALLPWLTVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:COG1116 100 NVALglelrgVPKAerRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1441214933 169 EILQLHKEFETTTILVSHDPSE-IYkLSNRVIVLKD--GKIVDD 209
Cdd:COG1116 180 ELLRLWQETGKTVLFVTHDVDEaVF-LADRVVVLSArpGRIVEE 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-210 |
2.78e-72 |
|
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: 221.01 E-value: 2.78e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEIKKELHGsngvMNLDVNLDIrSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQD--EKEFLPVQKR 77
Cdd:cd03297 1 MLCVDIEKRLPD----FTLKIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDgGTIVLNGTVLFDsrKKINLPPQQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 78 KIGFVFQDYALFPNMTVLENLFFV------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLM 151
Cdd:cd03297 76 KIGLVFQQYALFPHLNVRENLAFGlkrkrnREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 152 DEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
20-211 |
2.46e-65 |
|
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: 204.01 E-value: 2.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDekefLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPtSGEILLDGKDITN----LPPHKRPVNTVFQNYALFPHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:cd03300 94 AFglrlkkLPKAeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:cd03300 174 KRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-205 |
2.88e-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: 2.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 19 LDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:cd03229 17 NDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTDLEDELPPLRRRIGMVFQDFALFPHLTVLEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFvnkdkelanhlleitelwelknrlpnSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEF 177
Cdd:cd03229 97 IAL--------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQL 150
|
170 180
....*....|....*....|....*...
gi 1441214933 178 ETTTILVSHDPSEIYKLSNRVIVLKDGK 205
Cdd:cd03229 151 GITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-209 |
1.47e-63 |
|
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: 198.85 E-value: 1.47e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEiwqdekeflPVQ--KRKIGFVFQDYALFPNMTVLE 96
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLVDGE---------PVTgpGPDRGYVFQQDALLPWLTVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:cd03293 93 NVALglelqgVPKAeaRERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1441214933 169 EILQLHKEFETTTILVSHDPSE-IYkLSNRVIVL--KDGKIVDD 209
Cdd:cd03293 173 ELLDIWRETGKTVLLVTHDIDEaVF-LADRVVVLsaRPGRIVAE 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
20-209 |
1.57e-63 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 199.11 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDN-EIWQ-DEKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIDGqDISSlSERELARLRRRHIGFVFQFFNLLPELTALE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NL--------FFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:COG1136 106 NValplllagVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1441214933 169 EILQLHKEFETTTILVSHDPsEIYKLSNRVIVLKDGKIVDD 209
Cdd:COG1136 186 LLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-206 |
6.92e-62 |
|
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: 194.63 E-value: 6.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDN-EIWQ-DEKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVDGtDISKlSEKELAAFRRRHIGFVFQSFNLLPDLTALE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 N----LFFVNK----DKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:cd03255 102 NvelpLLLAGVpkkeRRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVME 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1441214933 169 EILQLHKEFETTTILVSHDPsEIYKLSNRVIVLKDGKI 206
Cdd:cd03255 182 LLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-216 |
1.24e-61 |
|
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: 195.94 E-value: 1.24e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 3 KIEIKKELHGSNGVMnlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNE--IWQDEKEFLPVQKRKI 79
Cdd:cd03294 27 KEEILKKTGQTVGVN--DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLiEPTSGKVLIDGQdiAAMSRKELRELRRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQDYALFPNMTVLENLFF------VNKDK--ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLM 151
Cdd:cd03294 105 SMVFQSFALLPHRTVLENVAFglevqgVPRAEreERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 152 DEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
20-229 |
1.34e-61 |
|
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: 194.87 E-value: 1.34e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdEKEFLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILFGGE----DATDVPVQERNVGFVFQHYALFRHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF----------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:cd03296 96 AFglrvkprserPPEAeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 167 QDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTSGSAKFSFEG 229
Cdd:cd03296 176 RRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLG 238
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
20-216 |
1.14e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 192.20 E-value: 1.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQDEKEFlpvqKRKIGFVFQDYALFPNMTVLEN 97
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTsGEVRVLGEdVARDPAEV----RRRIGYVPQEPALYPDLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:COG1131 94 LRFFarlyglprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 170 ILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1131 174 LRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
20-216 |
1.89e-59 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 188.70 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQdeKEFLPVQKRKIGFVFQ--DYALFpNMTVLE 96
Cdd:COG1122 19 DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTsGEVLVDGKDIT--KKNLRELRRKVGLVFQnpDDQLF-APTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:COG1122 96 DVAFgpenlgLPREeiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1441214933 169 EILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1122 176 LLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
20-207 |
1.68e-58 |
|
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: 185.92 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDekefLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03301 18 DLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYIGGRDVTD----LPPKDRDIAMVFQNYALYPHMTVYDNI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF-----------VNKDKELANHLLEITELWelkNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:cd03301 94 AFglklrkvpkdeIDERVREVAELLQIEHLL---DRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 168 DEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:cd03301 171 AELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-216 |
2.00e-58 |
|
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: 190.32 E-value: 2.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 2 IKIEIKKELhgsnGVMNLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQD--EKEFLPVQKRK 78
Cdd:TIGR02142 1 LSARFSKRL----GDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDeGEIVLNGRTLFDsrKGIFLPPEKRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 79 IGFVFQDYALFPNMTVLENLFFVNKD---KELANHLLEITELW---ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:TIGR02142 77 IGYVFQEARLFPHLSVRGNLRYGMKRarpSERRISFERVIELLgigHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 153 EPLSALDptmrIKLQDEIL----QLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:TIGR02142 157 EPLAALD----DPRKYEILpyleRLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
7.76e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.81 E-value: 7.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEikkELH---GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQDEKEfLPVQ 75
Cdd:COG1126 1 MIEIE---NLHksfGDLEVLK-GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTITVDGEdLTDSKKD-INKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 76 KRKIGFVFQDYALFPNMTVLENLFF-------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRP 146
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLapikvkkMSKAeaEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 147 KLLLMDEPLSALDPTMRiklqDEILQLHKEF---ETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1126 156 KVMLFDEPTSALDPELV----GEVLDVMRDLakeGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
1.58e-57 |
|
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: 184.41 E-value: 1.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIE-IKKElHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQ-DEKEFLPVQk 76
Cdd:COG1127 5 MIEVRnLTKS-FGDRVVLD-GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDsGEILVDGQdITGlSEKELYELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 77 RKIGFVFQDYALFPNMTVLENLFF-------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPK 147
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFplrehtdLSEAeiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 148 LLLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
12-215 |
1.42e-56 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 185.92 E-value: 1.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDekefLPVQKRKIGFVFQDYALFP 90
Cdd:PRK09452 25 DGKEVIS-NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIMLDGQDITH----VPAENRHVNTVFQSYALFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENLFFVNKDKELANHllEITE----------LWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:PRK09452 100 HMTVFENVAFGLRMQKTPAA--EITPrvmealrmvqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 161 TMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK09452 178 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-215 |
4.47e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.13 E-value: 4.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 4 IEIKK--ELHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLE-KAQGIIKVDNeiwQDEKEfLPVQKRKIG 80
Cdd:PRK10851 3 IEIANikKSFGRTQVLN-DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEhQTSGHIRFHG---TDVSR-LHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 81 FVFQDYALFPNMTVLENLFF----------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKL 148
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFgltvlprrerPNAAaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 149 LLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-216 |
4.99e-56 |
|
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: 188.19 E-value: 4.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNE-IWQDEKEFLPVQKRKIGFVFQD--YALFPNMTV- 94
Cdd:COG1123 283 DVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFDGKdLTKLSRRSLRELRRRVQMVFQDpySSLNPRMTVg 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 ------LENLFFVNKD--KELANHLLEITEL-WELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIK 165
Cdd:COG1123 363 diiaepLRLHGLLSRAerRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQ 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 166 LQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1123 443 ILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
20-220 |
1.20e-55 |
|
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: 179.45 E-value: 1.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGlekaqgIIKVDN-EIWQDEKEF--LPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAG------FIKPDSgKILLNGKDItnLPPEKRDISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF-----VNKDKELANHLLEITELW---ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:cd03299 91 NIAYglkkrKVDKKEIERKVLEIAEMLgidHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 169 EILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTS 220
Cdd:cd03299 171 ELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
20-216 |
1.23e-55 |
|
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: 179.42 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEiwqDEKEFLPVQ-KRKIGFVFQDYALFPNMTVLEN 97
Cdd:cd03295 19 NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIDGE---DIREQDPVElRRKIGYVIQQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFV--------NKDKELANHLLEITEL--WELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:cd03295 96 IALVpkllkwpkEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1441214933 168 DEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:cd03295 176 EEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-210 |
4.96e-55 |
|
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: 177.31 E-value: 4.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIE-IKKELHGSNGVMNL--DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDN-EIWQDEKEFLPVQ 75
Cdd:cd03257 1 LLEVKnLSVSFPTGGGSVKAldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKpTSGSIIFDGkDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 76 KRKIGFVFQDY--ALFPNMTV-------LENLFFVNKDKELANHLLEITELWELK----NRLPNSLSGGQKQRVSLCRAL 142
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIgeqiaepLRIHGKLSKKEARKEAVLLLLVGVGLPeevlNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 143 MNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
20-212 |
7.36e-54 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 175.25 E-value: 7.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDN-EIWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:COG3638 21 DVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPtSGEILVDGqDVTALRGRALRRLRRRIGMIFQQFNLVPRLSVLTN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 --------------LF--FVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP- 160
Cdd:COG3638 101 vlagrlgrtstwrsLLglFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPk 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 161 ----TMRIklqdeILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTA 212
Cdd:COG3638 181 tarqVMDL-----LRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-215 |
2.56e-53 |
|
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: 176.14 E-value: 2.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 33 LTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEiwqdEKEFLPVQKRKIGFVFQDYALFPNMTVLENLFFVNKD------- 104
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQpDSGSIMLDGE----DVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMrkvprae 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 105 -KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFETTTIL 183
Cdd:TIGR01187 77 iKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180 190
....*....|....*....|....*....|..
gi 1441214933 184 VSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:TIGR01187 157 VTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
20-210 |
2.72e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 172.93 E-value: 2.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNeiwQD----EKEFLPVQKRKIGFVFQDYALFPNMTV 94
Cdd:COG2884 20 DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNG---QDlsrlKRREIPYLRRRIGVVFQDFRLLPDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRikl 166
Cdd:COG2884 97 YENVALPlrvtgksrKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETS--- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 167 qDEILQLHKEF---ETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:COG2884 174 -WEIMELLEEInrrGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
3-217 |
3.27e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 177.60 E-value: 3.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 3 KIEIKKELHGSNGVMnlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNE-IWQ-DEKEFLPVQKRKI 79
Cdd:COG4175 30 KDEILEKTGQTVGVN--DASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLiEPTAGEVLIDGEdITKlSKKELRELRRKKM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQDYALFPNMTVLENLFF------VNKD--KELANHLLEITEL--WElkNRLPNSLSGGQKQRVSLCRALMNRPKLL 149
Cdd:COG4175 108 SMVFQHFALLPHRTVLENVAFgleiqgVPKAerRERAREALELVGLagWE--DSYPDELSGGMQQRVGLARALATDPDIL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 150 LMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLL 217
Cdd:COG4175 186 LMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILT 253
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-206 |
4.11e-53 |
|
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: 171.94 E-value: 4.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 4 IEIKKeLH---GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKEFLPVQKRKI 79
Cdd:cd03262 1 IEIKN-LHksfGDFHVLK-GIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIIIDGLKLTDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQDYALFPNMTVLENLFF-------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLL 150
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLapikvkgMSKAeaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 151 MDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
20-274 |
5.72e-53 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 176.58 E-value: 5.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNE--IWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:TIGR01186 11 DADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLiEPTAGQIFIDGEniMKQSPVELREVRRKKIGMVFQQFALFPHMTILQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:TIGR01186 91 NTSLGpellgwpeQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDSMQD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 169 EILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTSGSAKFSFEGKlLDIIKV-DVIYVAIIAi 247
Cdd:TIGR01186 171 ELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK-VDLSQVfDAERIAQRM- 248
|
250 260
....*....|....*....|....*..
gi 1441214933 248 GQQLVEVTISSNEAKELRVGQDVRVST 274
Cdd:TIGR01186 249 NTGPITKTADKGPRSALQLMRDERVDS 275
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-215 |
7.50e-53 |
|
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: 172.37 E-value: 7.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 4 IEIKK-ELHGSNGVMNL-DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKV-DNEIWQDEKEFLPVQKRKI 79
Cdd:cd03256 1 IEVENlSKTYPNGKKALkDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLvEPTSGSVLIdGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQDYALFPNMTVLENL----------------FFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALM 143
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsgrlgrrstwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 144 NRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
12-211 |
3.95e-52 |
|
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: 170.38 E-value: 3.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQD--EKEFLPVQKRkIGFVFQDYAL 88
Cdd:cd03261 11 GGRTVLK-GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGlsEAELYRLRRR-MGMLFQSGAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 89 FPNMTVLENL-FFVNKDKELANHllEITELWELK----------NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:cd03261 89 FDSLTVFENVaFPLREHTRLSEE--EIREIVLEKleavglrgaeDLYPAELSGGMKKRVALARALALDPELLLYDEPTAG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 158 LDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:cd03261 167 LDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
20-215 |
3.93e-51 |
|
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: 167.36 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDEKEFLPVQ------KRKIGFVFQDYALFPnMT 93
Cdd:cd03260 18 DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDvdvlelRRRVGMVFQKPNPFP-GS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFFVNKD---------KELANHLLEITELW-ELKNRL-PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:cd03260 97 IYDNVAYGLRLhgiklkeelDERVEEALRKAALWdEVKDRLhALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPIS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 163 RIKLQDEILQLHKefETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:cd03260 177 TAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-213 |
8.92e-51 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 170.29 E-value: 8.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQDEKeflpVQKRKIGFVFQDYALFP 90
Cdd:PRK11432 17 GSNTVID-NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGEDVTHRS----IQQRDICMVFQSYALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:PRK11432 92 HMSLGENVGYglkmlgVPKEerKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 163 RIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAK 213
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQ 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-216 |
1.32e-50 |
|
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: 166.90 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEI--WQDEKEFlpvqKRKIGFVFQDY--ALFPNMTV 94
Cdd:COG1124 23 DVSLEVAPGESFGLVGESGSGKSTLLRALAGLERpWSGEVTFDGRPvtRRRRKAF----RRRVQMVFQDPyaSLHPRHTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 -------LENLFFVNKDKELANhLLEITEL-WELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMrikl 166
Cdd:COG1124 99 drilaepLRIHGLPDREERIAE-LLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSV---- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 167 QDEIL----QLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1124 174 QAEILnllkDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-215 |
1.60e-50 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 169.49 E-value: 1.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEiwqdEKEFLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:NF040840 18 DISLEVKEGEYFIILGPSGAGKTVLLELIAGIwPPDSGKIYLDGK----DITNLPPEKRGIAYVYQNYMLFPHKTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNK-----DKELANHLLEITELW---ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:NF040840 94 AFGLKlrkvpKEEIERKVKEIMELLgisHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:NF040840 174 KRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREV 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
20-216 |
2.78e-50 |
|
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: 165.99 E-value: 2.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDN-EIWQ-DEKEFLpvqkRKIGFVFQDYALFPNMTVLE 96
Cdd:COG1120 19 DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSsGEVLLDGrDLASlSRRELA----RRIAYVPQEPPAPFGLTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 ----------NLFFVN--KDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:COG1120 95 lvalgryphlGLFGRPsaEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 165 KLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1120 175 EVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
20-205 |
2.09e-49 |
|
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: 162.64 E-value: 2.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNeiwQDEKEFLPVQKRK-IGFVFQ--DYALFpNMTVL 95
Cdd:cd03225 19 DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTsGEVLVDG---KDLTKLSLKELRRkVGLVFQnpDDQFF-GPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:cd03225 95 EEVAFglenlgLPEEeiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1441214933 168 DEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGK 205
Cdd:cd03225 175 ELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
20-206 |
4.14e-49 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 166.36 E-value: 4.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQDekefLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFIGEKRMND----VPPAERGVGMVFQSYALYPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:PRK11000 97 SFglklagAKKEeiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEI 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PRK11000 177 SRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
20-206 |
5.29e-49 |
|
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: 160.26 E-value: 5.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQDEKEFlpvqKRKIGFVFQDYALFPNMTVLEN 97
Cdd:cd03230 18 DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDsGEIKVLGKdIKKEPEEV----KRRIGYLPEEPSLYENLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LffvnkdkelanhlleitelwelknrlpnSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEf 177
Cdd:cd03230 94 L----------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE- 144
|
170 180
....*....|....*....|....*....
gi 1441214933 178 ETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:cd03230 145 GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-215 |
1.75e-48 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 164.28 E-value: 1.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEIKKELhgsnGVMNLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQD--EKEFLPVQKR 77
Cdd:PRK11144 1 MLELNFKQQL----GDLCLTVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQkGRIVLNGRVLFDaeKGICLPPEKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 78 KIGFVFQDYALFPNMTVLENLFF--VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPL 155
Cdd:PRK11144 77 RIGYVFQDARLFPHYKVRGNLRYgmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 156 SALD-PTMRiklqdEIL----QLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK11144 157 ASLDlPRKR-----ELLpyleRLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-226 |
3.36e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 159.92 E-value: 3.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEikkELHGSNGVMNLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNeiwQDEKEfLPVQKRKI 79
Cdd:COG3840 1 MLRLD---DLTYRYGDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPpDSGRILWNG---QDLTA-LPPAERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQDYALFPNMTVLENLFF--------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRAL-MNRPkLLL 150
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNIGLglrpglklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvRKRP-ILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 151 MDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAkSVLLKTSGSAKFS 226
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT-AALLDGEPPPALA 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-216 |
7.11e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.48 E-value: 7.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIwqdekefLPVQKRKIGFVFQDYAL---FPnMTVL 95
Cdd:COG1121 24 DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGKP-------PRRARRRIGYVPQRAEVdwdFP-ITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 E----------NLF--FVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:COG1121 96 DvvlmgrygrrGLFrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 164 IKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLkDGKIVDDGTAKSVL 216
Cdd:COG1121 176 EALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-215 |
2.70e-47 |
|
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: 158.23 E-value: 2.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEIKKELHGSNGVMNLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDN-EIWQDEKEFLPVQKRK 78
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLvEPSSGSILLEGtDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 79 IGFVFQDYALFPNMTVLENL----------------FFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRAL 142
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykptwrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 143 MNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
20-206 |
4.08e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.51 E-value: 4.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQDekefLPVQK--RKIGFVFQDYALFPNmTVLE 96
Cdd:COG4619 18 PVSLTLEAGECVAITGPSGSGKSTLLRALADLDPpTSGEIYLDGKPLSA----MPPPEwrRQVAYVPQEPALWGG-TVRD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVNK------DKELANHLLE---ITElwELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:COG4619 93 NLPFPFQlrerkfDRERALELLErlgLPP--DILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1441214933 168 DEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:COG4619 171 ELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
20-216 |
1.21e-46 |
|
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: 165.78 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDN-EIWQDEKEFLpvqKRKIGFVFQDYALFpNMTVLEN 97
Cdd:COG2274 493 NISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTsGRILIDGiDLRQIDPASL---RRQIGVVLQDVFLF-SGTIREN 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNK--DKELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:COG2274 569 ITLGDPdaTDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEA 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 165 KLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG2274 649 IILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-218 |
1.84e-46 |
|
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: 155.82 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIE-IKKELHGSNGVMNL--DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQDEKEF-LPVQ 75
Cdd:cd03258 1 MIELKnVSKVFGDTGGKVTAlkDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLVDGTDLTLLSGKeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 76 KRKIGFVFQDYALFPNMTVLEN------LFFVNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPK 147
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENvalpleIAGVPKAeiEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 148 LLLMDEPLSALDPtmriKLQDEILQL----HKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLK 218
Cdd:cd03258 161 VLLCDEATSALDP----ETTQSILALlrdiNRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
20-212 |
3.60e-46 |
|
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: 154.90 E-value: 3.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNE-IWQ-DEKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAGQdLFAlDEDARARLRARHVGFVFQSFQLLPTLTALE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 N------LFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:COG4181 110 NvmlpleLAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1441214933 171 LQLHKEFETTTILVSHDPsEIYKLSNRVIVLKDGKIVDDGTA 212
Cdd:COG4181 190 FELNRERGTTLVLVTHDP-ALAARCDRVLRLRAGRLVEDTAA 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
4.71e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 157.55 E-value: 4.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIE-IKKELHGSNG-VMNL-DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDN-EIWQ-DEKEfLPV 74
Cdd:COG1135 1 MIELEnLSKTFPTKGGpVTALdDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLVDGvDLTAlSERE-LRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 75 QKRKIGFVFQDYALFPNMTVLENLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRP 146
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALpleiagVPKAeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 147 KLLLMDEPLSALDP--TmriklqDEILQL----HKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLK 218
Cdd:COG1135 160 KVLLCDEATSALDPetT------RSILDLlkdiNRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-231 |
5.32e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 158.46 E-value: 5.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNeiwQDEKEFLPVQkRKIGFVFQDYALFPNMTVLENL 98
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQpTAGQIMLDG---VDLSHVPPYQ-RPINMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNKDKELA--------NHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:PRK11607 113 AFGLKQDKLPkaeiasrvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLL--KTSGSAKF-----SFEGKL 231
Cdd:PRK11607 193 VDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEhpTTRYSAEFigsvnVFEGVL 260
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-216 |
1.52e-45 |
|
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: 154.53 E-value: 1.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQDEKEFLPVQKRKIGFVFQ--DYALFPNmTVL 95
Cdd:TIGR04521 23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTsGTVTIDGRdITAKKKKKLKDLRKKVGLVFQfpEHQLFEE-TVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFF------VNKD--KELANHLLEITELWE-LKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:TIGR04521 102 KDIAFgpknlgLSEEeaEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1441214933 167 QDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:TIGR04521 182 LDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-216 |
1.86e-45 |
|
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: 160.07 E-value: 1.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGiiKVDNEIWQDEKE--FLPVQKR--KIGFVFQD--YALFPnMT 93
Cdd:COG1123 24 GVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG--RISGEVLLDGRDllELSEALRgrRIGMVFQDpmTQLNP-VT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFFV--NKD------KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIK 165
Cdd:COG1123 101 VGDQIAEAleNLGlsraeaRARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 166 LQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1123 181 ILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-236 |
3.35e-45 |
|
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: 152.70 E-value: 3.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEikkELH---GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEiwqDEKEFLPVQK 76
Cdd:COG4555 1 MIEVE---NLSkkyGKVPALK-DVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIDGE---DVRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 77 RKIGFVFQDYALFPNMTVLENL-FF-------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKL 148
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIrYFaelyglfDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 149 LLMDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTSGSakfSFE 228
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE---NLE 229
|
....*...
gi 1441214933 229 GKLLDIIK 236
Cdd:COG4555 230 DAFVALIG 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-233 |
4.55e-45 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 152.91 E-value: 4.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDEKEflpvqkrKIGFVFQDYALFP 90
Cdd:PRK11247 23 GERTVLN-QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsAGELLAGTAPLAEARE-------DTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLEN--LFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:PRK11247 95 WKKVIDNvgLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 169 EILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTSGSAKFS-FEGKLLD 233
Cdd:PRK11247 175 LIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPRPRRRGSARLAeLEAEVLQ 240
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-211 |
5.96e-44 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 152.69 E-value: 5.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEI---KKELHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQDEKeflPVQk 76
Cdd:PRK11650 1 MAGLKLqavRKSYDGKTQVIK-GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWIGGRVVNELE---PAD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 77 RKIGFVFQDYALFPNMTVLENLFFVNKDKELANHLLE--------ITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKL 148
Cdd:PRK11650 76 RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEervaeaarILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 149 LLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-210 |
1.51e-43 |
|
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: 147.64 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 13 SNGVMNLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEiwqdEKEFLPVQKRKIGFVFQDYALFPN 91
Cdd:cd03298 9 SYGEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLINGV----DVTAAPPADRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVLEN--------LFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:cd03298 85 LTVEQNvglglspgLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 164 IKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-205 |
3.06e-43 |
|
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: 145.22 E-value: 3.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDN-EIWQDEKEFLPvqkRKIGFVFQDYALFpNMTVLEN 97
Cdd:cd03228 20 DVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTsGEILIDGvDLRDLDLESLR---KNIAYVPQDPFLF-SGTIREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LffvnkdkelanhlleitelwelknrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKef 177
Cdd:cd03228 96 I-----------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK-- 144
|
170 180
....*....|....*....|....*...
gi 1441214933 178 ETTTILVSHDPSEIyKLSNRVIVLKDGK 205
Cdd:cd03228 145 GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-216 |
4.03e-43 |
|
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: 149.43 E-value: 4.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGI----IKVDNE-IWQ-DEKEFLPVQKRKIGFVFQD-Y-ALFPN 91
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGItsgeILFDGEdLLKlSEKELRKIRGREIQMIFQDpMtSLNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTV-------LENLFFVNKD--KELANHLLE---ITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALD 159
Cdd:COG0444 103 MTVgdqiaepLRIHGGLSKAeaRERAIELLErvgLPDPERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 160 PTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG0444 183 VTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
20-210 |
5.44e-43 |
|
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: 144.89 E-value: 5.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNeiwQDEKEFLPVQK-RKIGFVFQdyalfpnmtvlen 97
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSsGEILLDG---KDLASLSPKELaRKIAYVPQ------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 lffvnkdkelanhLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEF 177
Cdd:cd03214 81 -------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARER 147
|
170 180 190
....*....|....*....|....*....|...
gi 1441214933 178 ETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03214 148 GKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-201 |
8.84e-43 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 145.32 E-value: 8.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAqgiIKVDNEIWQDEKEF--LPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPA---FSASGEVLLNGRRLtaLPAEQRRIGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF-----VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:COG4136 96 NLAFalpptIGRAqrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
170 180 190
....*....|....*....|....*....|..
gi 1441214933 170 ILQLHKEFETTTILVSHDPSEIyKLSNRVIVL 201
Cdd:COG4136 176 VFEQIRQRGIPALLVTHDEEDA-PAAGRVLDL 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-205 |
9.68e-43 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 143.54 E-value: 9.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQdeKEFLPVQKRKIGFVFQdyalfpnmtvlenl 98
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIA--KLPLEELRRRIGYVPQ-------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 ffvnkdkelanhlleitelwelknrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEfE 178
Cdd:cd00267 81 -----------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-G 130
|
170 180
....*....|....*....|....*..
gi 1441214933 179 TTTILVSHDPSEIYKLSNRVIVLKDGK 205
Cdd:cd00267 131 RTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-205 |
1.34e-41 |
|
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: 142.39 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDEKE-FLPVQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:TIGR02673 20 DVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPsRGQVRIAGEDVNRLRGrQLPLLRRRIGVVFQDFRLLPDRTVYEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTmrikLQDE 169
Cdd:TIGR02673 100 VALPlevrgkkeREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPD----LSER 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 1441214933 170 ILQLHKEFE---TTTILVSHDPSEIYKLSNRVIVLKDGK 205
Cdd:TIGR02673 176 ILDLLKRLNkrgTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-216 |
1.58e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 143.72 E-value: 1.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKEFLPVqKRKIGFVFQDyalfP-----NMT 93
Cdd:TIGR04520 20 NVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTsGKVTVDGLDTLDEENLWEI-RKKVGMVFQN----PdnqfvGAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 V-------LENLFFVNKD-KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIK 165
Cdd:TIGR04520 95 VeddvafgLENLGVPREEmRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 166 LQDEILQLHKEFETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:TIGR04520 175 VLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIF 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-216 |
3.22e-41 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 142.15 E-value: 3.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKeflpVQKRKI----GFVFQDY 86
Cdd:PRK09493 12 GPTQVLH-NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITsGDLIVDGLKVNDPK----VDERLIrqeaGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 87 ALFPNMTVLENLFF-------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK09493 87 YLFPHLTALENVMFgplrvrgASKEeaEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 158 LDPTMRiklqDEILQLHKEFET---TTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK09493 167 LDPELR----HEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-207 |
1.49e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 141.15 E-value: 1.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEiwqdekeflPVQ----KRkiGFVFQDYALFPNMTV 94
Cdd:COG4525 25 DVSLTIESGEFVVALGASGCGKTTLLNLIAGfLAPSSGEITLDGV---------PVTgpgaDR--GVVFQKDALLPWLNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:COG4525 94 LDNVAFglrlrgVPKAerRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1441214933 167 QDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKD--GKIV 207
Cdd:COG4525 174 QELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-205 |
1.83e-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: 139.15 E-value: 1.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNE-IWQDEKEFlpvqKRKIGFVFQDYALFPNMTVLEN 97
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPsAGEVLWNGEpIRDAREDY----RRRLAYLGHADGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNK------DKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQdEIL 171
Cdd:COG4133 96 LRFWAAlyglraDREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA-ELI 174
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 172 QLHKEFETTTILVSHDPSEIykLSNRVIVLKDGK 205
Cdd:COG4133 175 AAHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
12-212 |
3.85e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 139.76 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQ-----DEKEFLPVqKRKIGFVFQD 85
Cdd:COG4161 13 GSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDsGQLNIAGHQFDfsqkpSEKAIRLL-RQKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 86 YALFPNMTVLENL-------FFVNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:COG4161 91 YNLWPHLTVMENLieapckvLGLSKEqaREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 157 ALDPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTA 212
Cdd:COG4161 171 ALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
11-212 |
5.59e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 138.99 E-value: 5.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 11 HGSNGVMnLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQ-----DEKEFLPVqKRKIGFVFQ 84
Cdd:PRK11124 12 YGAHQAL-FDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRsGTLNIAGNHFDfsktpSDKAIREL-RRNVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 85 DYALFPNMTVLENL-------FFVNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPL 155
Cdd:PRK11124 90 QYNLWPHLTVQQNLieapcrvLGLSKDqaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 156 SALDPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTA 212
Cdd:PRK11124 170 AALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
6.70e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 139.11 E-value: 6.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEIK---KELHGsNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVdNEIWQDEKEFLPVQK 76
Cdd:PRK11264 1 MSAIEVKnlvKKFHG-QTVLH-GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEaGTIRV-GDITIDTARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 77 RKI-------GFVFQDYALFPNMTVLENLF----FVNKDK-----ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCR 140
Cdd:PRK11264 78 GLIrqlrqhvGFVFQNFNLFPHRTVLENIIegpvIVKGEPkeeatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 141 ALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-206 |
1.18e-39 |
|
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: 137.28 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDneiwqdeKEFLPVQKRKIGFVFQDYAL---FPnMTVL 95
Cdd:cd03235 17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVF-------GKPLEKERKRIGYVPQRRSIdrdFP-ISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 EnlfFV---------------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:cd03235 89 D---VVlmglyghkglfrrlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1441214933 161 TMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-204 |
1.71e-39 |
|
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: 137.60 E-value: 1.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK--AQGIIKVDNEIWQdekeflPVQKRKIgfVFQDYALFPNMTVLEN 97
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQptSGGVILEGKQITE------PGPDRMV--VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF----VNKD------KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:TIGR01184 75 IALavdrVLPDlskserRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1441214933 168 DEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDG 204
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-207 |
3.91e-39 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 135.85 E-value: 3.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEiWQDEKEFLpvqkRKIGFVFQD--YALFPNmTVLE 96
Cdd:cd03226 18 DLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKeSSGSILLNGK-PIKAKERR----KSIGYVMQDvdYQLFTD-SVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVNKD----KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQ 172
Cdd:cd03226 92 ELLLGLKEldagNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRE 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1441214933 173 LHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:cd03226 172 LAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
20-207 |
1.01e-38 |
|
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: 135.15 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKV-DNEIWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:TIGR02982 23 DINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQeGSLKVlGQELHGASKKQLVQLRRRIGYIFQAHNLLGFLTARQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 L---------FFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP-TMRIKLq 167
Cdd:TIGR02982 103 VqmalelqpnLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSkSGRDVV- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1441214933 168 dEILQ-LHKEFETTTILVSHDPsEIYKLSNRVIVLKDGKIV 207
Cdd:TIGR02982 182 -ELMQkLAKEQGCTILMVTHDN-RILDVADRILQMEDGKLL 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-216 |
1.20e-38 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 134.87 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqDEKEFLPVQ--KRKIGFVFQDYALFPNMTVLE 96
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSIRFDGR---DITGLPPHEraRAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NL---FFVNKDKELANHLLEITELW----ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:cd03224 95 NLllgAYARRRAKRKARLERVYELFprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 170 ILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:cd03224 175 IRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-156 |
1.89e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 132.39 E-value: 1.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDN-EIWQDEKEFLpvqKRKIGFVFQDYALFPNMTVLEN 97
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGqDLTDDERKSL---RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 98 LFFVNKDKEL--------ANHLLEITELWELKNRL----PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:pfam00005 80 LRLGLLLKGLskrekdarAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-216 |
3.74e-38 |
|
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: 134.44 E-value: 3.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGlekaqgiikvdnEIWQDEKEFLPVQ------------KRKIGFV---FQ 84
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITG------------DLPPTYGNDVRLFgerrggedvwelRKRIGLVspaLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 85 DYaLFPNMTVLENL---FF---------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:COG1119 89 LR-FPRDETVLDVVlsgFFdsiglyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 153 EPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
20-221 |
4.41e-38 |
|
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: 140.66 E-value: 4.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFPnMTVLEN 97
Cdd:COG4988 355 GLSLTIPPGERVALVGPSGAGKSTLLNLLLGfLPPYSGSILING---VDLSDLDPASWRRqIAWVPQNPYLFA-GTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNK---DKELAnHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:COG4988 431 LRLGRPdasDEELE-AALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETE 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 164 IKLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSvLLKTSG 221
Cdd:COG4988 510 AEILQALRRLAK--GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEE-LLAKNG 563
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
20-216 |
4.87e-38 |
|
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: 133.72 E-value: 4.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNE-IWQdekefLPVQKRK---IGFVFQDYALFPNMTV 94
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPtSGSVLFDGEdITG-----LPPHEIArlgIGRTFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENL---------------FFVNKDKEL---ANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:cd03219 93 LENVmvaaqartgsglllaRARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 157 ALDPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:cd03219 173 GLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
20-221 |
6.16e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 140.69 E-value: 6.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFpNMTVLEN 97
Cdd:COG1132 358 DISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTSGRILIDG---VDIRDLTLESLRRqIGVVPQDTFLF-SGTIREN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKD--KELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:COG1132 434 IRYGRPDatDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 165 KLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSvLLKTSG 221
Cdd:COG1132 514 LIQEALERLMK--GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEE-LLARGG 566
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-215 |
2.61e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.63 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDEKEFLPVQKRKIGFVFQ--DYALFPNmTVLE 96
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPtSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-TIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVNK-----DKELANHLLEITELW-----ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:PRK13637 104 DIAFGPInlglsEEEIENRVKRAMNIVgldyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1441214933 167 QDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK13637 184 LNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
20-211 |
4.32e-37 |
|
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: 131.09 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKV-DNEIWQDEKEflpvQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTsGTAYInGYSIRTDRKA----ARQSLGYCPQFDALFDELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF--------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:cd03263 96 LRFyarlkglpKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1441214933 170 ILQLHKefETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:cd03263 176 ILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGS 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
20-216 |
2.59e-36 |
|
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: 130.16 E-value: 2.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GiikvdnEIWQDEKEF--LPVQKR-KIGFV--FQDYALFPNMT 93
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTsG------RILFDGRDItgLPPHRIaRLGIArtFQNPRLFPELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENL--------------------FFVNKDKEL---ANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLL 150
Cdd:COG0411 96 VLENVlvaaharlgrgllaallrlpRARREEREArerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 151 MDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-216 |
2.16e-35 |
|
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: 127.02 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdekeflPVQKRK--------IGFVFQDYALFP 90
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIRFDGE---------DITGLPphriarlgIGYVPEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENL---FFVNKDKELANHLLE-ITELW----ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:COG0410 92 SLTVEENLllgAYARRDRAEVRADLErVYELFprlkERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 163 RIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG0410 172 VEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-216 |
2.42e-35 |
|
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: 132.89 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQ--DEKEFLPVqKRKIGFVFQD-YA-LFPNMTVL 95
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDglSRRALRPL-RRRMQVVFQDpFGsLSPRMTVG 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 E------NLFFVNKDK----ELANHLLEITEL-WELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTmri 164
Cdd:COG4172 383 QiiaeglRVHGPGLSAaerrARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVS--- 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 165 kLQDEILQL----HKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4172 460 -VQAQILDLlrdlQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-210 |
2.66e-35 |
|
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: 126.16 E-value: 2.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDN-EIWQdekefLPVQ--KRKIGFVFQDYALFpNMTVL 95
Cdd:cd03245 22 NVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTsGSVLLDGtDIRQ-----LDPAdlRRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFFVN---KDKELANhLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPT 161
Cdd:cd03245 96 DNITLGAplaDDERILR-AAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1441214933 162 MRIKLQDEILQLHKefETTTILVSHDPSeIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03245 175 SEERLKERLRQLLG--DKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-206 |
3.18e-35 |
|
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: 125.98 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 14 NGVMNL-DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDN-EIWQDEKEFLPVQKRKIGFVFQDYALFP 90
Cdd:cd03292 12 NGTAALdGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGqDVSDLRGRAIPYLRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENLFFV-----NKDKELANHLLEITELWELKNR---LPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:cd03292 92 DRNVYENVAFAlevtgVPPREIRKRVPAALELVGLSHKhraLPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 163 riklQDEILQLHKEFE---TTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:cd03292 172 ----TWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-206 |
5.64e-35 |
|
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: 125.36 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 22 NLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNeiwQDEKEFLPVQkRKIGFVFQDYALFPNMTVLEN--- 97
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGfIEPASGSIKVND---QSHTGLAPYQ-RPVSMLFQENNLFAHLTVRQNigl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 -----LFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQ 172
Cdd:TIGR01277 94 glhpgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 173 LHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
7.85e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 126.07 E-value: 7.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 2 IKIEIKkELH---GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEI--WQDEK--EFLP 73
Cdd:COG4598 7 PALEVR-DLHksfGDLEVLK-GVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPdSGEIRVGGEEirLKPDRdgELVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 74 VQKR-------KIGFVFQDYALFPNMTVLENLFF-------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVS 137
Cdd:COG4598 85 ADRRqlqrirtRLGMVFQSFNLWSHMTVLENVIEapvhvlgRPKAeaIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 138 LCRALMNRPKLLLMDEPLSALDPtmriKLQDEIL----QLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAK 213
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDP----ELVGEVLkvmrDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
...
gi 1441214933 214 SVL 216
Cdd:COG4598 240 EVF 242
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
20-215 |
1.11e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.92 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDEKEFL-----PVQ-KRKIGFVFQDYALFPnMT 93
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYdpdvdVVElRRRVGMVFQKPNPFP-KS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFF------VNKDKELAnhllEITE-------LW-ELKNRL---PNSLSGGQKQRvsLC--RALMNRPKLLLMDEP 154
Cdd:COG1117 108 IYDNVAYglrlhgIKSKSELD----EIVEeslrkaaLWdEVKDRLkksALGLSGGQQQR--LCiaRALAVEPEVLLMDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 155 LSALDP--TMRIklQDEILQLHKEFetTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG1117 182 TSALDPisTAKI--EELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-216 |
1.23e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 129.00 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDN-EIWQ-DEKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGvDIAKiSDAELREVRRKKIAMVFQSFALMPHMTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF--------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:PRK10070 126 NTAFgmelaginAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1441214933 169 EILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
20-210 |
1.58e-34 |
|
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: 123.87 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDEKEFLpvqkRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03268 18 DISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQKNIEAL----RRIGALIEAPGFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNK----DKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPtMRIKLQDEILQLH 174
Cdd:cd03268 94 RLLARllgiRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP-DGIKELRELILSL 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1441214933 175 KEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03268 173 RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-221 |
2.08e-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: 130.66 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFpNMTVLEN 97
Cdd:COG4987 353 GLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSITLGG---VDLRDLDEDDLRRrIAVVPQRPHLF-DTTLREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNK---DKELAnHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:COG4987 429 LRLARPdatDEELW-AALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 164 IKLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSvLLKTSG 221
Cdd:COG4987 508 QALLADLLEALA--GRTVLLITHRLAGL-ERMDRILVLEDGRIVEQGTHEE-LLAQNG 561
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
20-212 |
2.56e-34 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 123.63 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQG--IIKVDNEIWQDEKEFlpvqKRKIGFVFQDYALFPNMTVLEN 97
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSgrATVAGHDVVREPREV----RRRIGIVFQDLSVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:cd03265 94 LYIHarlygvpgAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1441214933 170 ILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTA 212
Cdd:cd03265 174 IEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-211 |
3.30e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 126.45 E-value: 3.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIE-IKKELH-GSNGVMNL-DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDN-EIWQ-DEKEfLPV 74
Cdd:PRK11153 1 MIELKnISKVFPqGGRTIHALnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERpTSGRVLVDGqDLTAlSEKE-LRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 75 QKRKIGFVFQDYALFPNMTVLENLFF----VNKDKEL----ANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRP 146
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALplelAGTPKAEikarVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 147 KLLLMDEPLSALDP-TMRiklqdEILQLHK----EFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK11153 160 KVLLCDEATSALDPaTTR-----SILELLKdinrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-211 |
4.42e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 124.41 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 11 HGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKvdneiWQDE----------KEFlpvqKRKI 79
Cdd:PRK10419 22 HQHQTVLN-NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVS-----WRGEplaklnraqrKAF----RRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQDY--ALFPNMTV-------LENLFFVNKDKELAN--HLLEITEL-WELKNRLPNSLSGGQKQRVSLCRALMNRPK 147
Cdd:PRK10419 92 QMVFQDSisAVNPRKTVreiirepLRHLLSLDKAERLARasEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 148 LLLMDEPLSALDptmrIKLQDEILQLHK----EFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK10419 172 LLILDEAVSNLD----LVLQAGVIRLLKklqqQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
20-210 |
5.30e-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: 5.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIrSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNeiwQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03264 18 GVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPsSGTIRIDG---QDVLKQPQKLRRRIGYLPQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:cd03264 94 DYIawlkgipsKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 171 LQLHKefETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03264 174 SELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-201 |
6.85e-34 |
|
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: 122.34 E-value: 6.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK---AQGIIKVDNEIWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:TIGR03608 16 DLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKfdsGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENETVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NL----FFVNKDK----ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:TIGR03608 96 NLdlglKYKKLSKkekrEKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLD 175
|
170 180 190
....*....|....*....|....*....|...
gi 1441214933 169 EILQLHKEfETTTILVSHDPsEIYKLSNRVIVL 201
Cdd:TIGR03608 176 LLLELNDE-GKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
7.00e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.48 E-value: 7.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEIK--KELHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDEKEFLPVQ--- 75
Cdd:PRK14247 1 MNKIEIRdlKVSFGQVEVLD-GVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDvie 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 76 -KRKIGFVFQDYALFPNMTVLENLFF-------VNKDKELANHL---LEITELW-ELKNRL---PNSLSGGQKQRVSLCR 140
Cdd:PRK14247 80 lRRRVQMVFQIPNPIPNLSIFENVALglklnrlVKSKKELQERVrwaLEKAQLWdEVKDRLdapAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 141 ALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFetTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-209 |
8.46e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 123.66 E-value: 8.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLekaqgiIKVDN-EIWQDEKE--FLPVQKR--KIGFVFQDYAL--FPNM 92
Cdd:COG1101 24 GLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGS------LPPDSgSILIDGKDvtKLPEYKRakYIGRVFQDPMMgtAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 93 TVLENL-------------FFVNK-DKELANHLLEITELwELKNRLPN---SLSGGQKQRVSLCRALMNRPKLLLMDEPL 155
Cdd:COG1101 98 TIEENLalayrrgkrrglrRGLTKkRRELFRELLATLGL-GLENRLDTkvgLLSGGQRQALSLLMATLTKPKLLLLDEHT 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 156 SALDPtmriKLQDEILQLH----KEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDD 209
Cdd:COG1101 177 AALDP----KTAALVLELTekivEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
21-216 |
1.91e-33 |
|
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: 127.61 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVD-NEIWQDEKEFLPVQ----KRKIGFVFQDYALFPNMTV 94
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGvLEPTSGEVNVRvGDEWVDMTKPGPDGrgraKRYIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENL---FFVNKDKELAN----HLLEITELWELK-----NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:TIGR03269 383 LDNLteaIGLELPDELARmkavITLKMVGFDEEKaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPIT 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 163 RIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:TIGR03269 463 KVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-216 |
5.41e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 121.49 E-value: 5.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 11 HGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNE-------IWQDEKEFLPVqKRKIGFVF 83
Cdd:PRK14267 14 YGSNHVIK-GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEvrlfgrnIYSPDVDPIEV-RREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 84 QDYALFPNMTVLENLFFVNKDKELANHLLEITE----------LW-ELKNRL---PNSLSGGQKQRVSLCRALMNRPKLL 149
Cdd:PRK14267 92 QYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDErvewalkkaaLWdEVKDRLndyPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 150 LMDEPLSALDPTMRIKLQDEILQLHKEFetTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
20-206 |
5.49e-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: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFPNmTVLEN 97
Cdd:cd03246 20 NVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDG---ADISQWDPNELGDhVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LffvnkdkelanhlleitelwelknrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLhKEF 177
Cdd:cd03246 96 I-----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAL-KAA 145
|
170 180
....*....|....*....|....*....
gi 1441214933 178 ETTTILVSHDPSEIyKLSNRVIVLKDGKI 206
Cdd:cd03246 146 GATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
11-208 |
1.88e-32 |
|
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: 120.30 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 11 HGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNE-IWQDEKEFLPVQKRKIGFVFQDY-- 86
Cdd:TIGR02769 21 KQRAPVLT-NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQdLYQLDRKQRRAFRRDVQLVFQDSps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 87 ALFPNMTV-------LENLFFVNKDKELAN--HLLEITELW-ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:TIGR02769 100 AVNPRMTVrqiigepLRHLTSLDESEQKARiaELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 157 ALDptmrIKLQDEILQ----LHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVD 208
Cdd:TIGR02769 180 NLD----MVLQAVILEllrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-234 |
5.08e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 5.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 22 NLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNeiwQDEKEFLPVQkRKIGFVFQDYALFPNMTVLEN--- 97
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNG---QDHTTTPPSR-RPVSMLFQENNLFSHLTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 -----LFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIklqdEILQ 172
Cdd:PRK10771 95 glnpgLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ----EMLT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 173 LHKEF----ETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLlktSGSAKfsfEGKLLDI 234
Cdd:PRK10771 171 LVSQVcqerQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL---SGKAS---ASALLGI 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
8.50e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.97 E-value: 8.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEIWQ---DEKEFLPVQKrKIGFVFQ--DYALFPNmT 93
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGERVITagkKNKKLKPLRK-KVGIVFQfpEHQLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFF------VNKD--KELANHLLEITELWE-LKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:PRK13634 103 VEKDICFgpmnfgVSEEdaKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 165 KLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKT 219
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-206 |
3.05e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.03 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQG--IIKVDNEIWQ-DEKEFLPVQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSgeVSLVGQPLHQmDEEARAKLRAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:PRK10584 109 VELPallrgessRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 1441214933 170 ILQLHKEFETTTILVSHDPsEIYKLSNRVIVLKDGKI 206
Cdd:PRK10584 189 LFSLNREHGTTLILVTHDL-QLAARCDRRLRLVNGQL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-215 |
4.12e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.89 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdEKEFLPV---QKRKIGFVFQDYALFPNMTVL 95
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLDGE----PVRFRSPrdaQAAGIAIIHQELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLF---------FVNKdKELANHLLEITELWELK---NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:COG1129 98 ENIFlgreprrggLIDW-RAMRRRARELLARLGLDidpDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 164 IKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG1129 177 ERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-216 |
5.21e-31 |
|
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: 121.51 E-value: 5.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDN-EIWQDEKEFLpvqKRKIGFVFQDYALFpNMTVLEN 97
Cdd:TIGR03375 483 NVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTeGSVLLDGvDIRQIDPADL---RRNIGYVPQDPRLF-YGTLRDN 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVN---KDKELANhLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPT-- 161
Cdd:TIGR03375 559 IALGApyaDDEEILR-AAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRse 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 162 MRIK--LQDEILqlhkefETTTILVSHDPSeIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:TIGR03375 638 ERFKdrLKRWLA------GKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKDQVL 687
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-210 |
5.59e-31 |
|
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: 114.19 E-value: 5.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL---EKAQGIIKVdNEIWQDEKEFlpvqKRKIGFVFQDYALFPNMTVLE 96
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtgLGVSGEVLI-NGRPLDKRSF----RKIIGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVNKdkelanhlleitelweLKnrlpnSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKE 176
Cdd:cd03213 102 TLMFAAK----------------LR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1441214933 177 fETTTILVSHDPS-EIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03213 161 -GRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-211 |
1.89e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 116.34 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEI-WQDEKEFLpvqkRKIGFVF-QDYALFPNMTVLE 96
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPTSGEVRVLGYVpFKRRKEFA----RRIGVVFgQRSQLWWDLPAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NlFFVNK------DKELANHLLEITELWELKNRL--P-NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:COG4586 116 S-FRLLKaiyripDAEYKKRLDELVELLDLGELLdtPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIR 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1441214933 168 DEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:COG4586 195 EFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-218 |
2.10e-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: 113.86 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDN-EIWQDEKEFLpvqKRKIGFVFQDYALFPNmTVLEN 97
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGiDIRDISRKSL---RSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF--VNKDKELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:cd03254 97 IRLgrPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 165 KLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSVLLK 218
Cdd:cd03254 177 LIQEALEKLMK--GRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
20-270 |
2.57e-30 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 115.57 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK---AQGIIKVDNEIWQDEKeflpvQKRKIGFVFQDYALFPNMTVLE 96
Cdd:TIGR01188 11 GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRptsGTARVAGYDVVREPRK-----VRRSIGIVPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:TIGR01188 86 NLEMmgrlygLPKDeaEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 169 EILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSvlLKTSGSAKFsFEGKLLDIIKVDVIyvaiiaIG 248
Cdd:TIGR01188 166 YIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE--LKRRLGKDT-LESRPRDIQSLKVE------VS 235
|
250 260
....*....|....*....|..
gi 1441214933 249 QQLVEVTISSNEAKELRVGQDV 270
Cdd:TIGR01188 236 MLIAELGETGLGLLAVTVDSDR 257
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-211 |
2.62e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 114.32 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNEiwqdEKEFLPVQK--RKiGFV--FQDYALFPNMTVL 95
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKpTGGTILLRGQ----HIEGLPGHQiaRM-GVVrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLF--------------------FVNKDKE---LANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:PRK11300 99 ENLLvaqhqqlktglfsgllktpaFRRAESEaldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 153 EPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
20-217 |
2.83e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 114.10 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDEKE-FLP----VQKRK-IGFVFQDYALFPnMT 93
Cdd:PRK14239 23 SVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNiYSPrtdtVDLRKeIGMVFQQPNPFP-MS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFF---VN--KDKELANHLLEIT----ELW-ELKNRLPNS---LSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:PRK14239 102 IYENVVYglrLKgiKDKQVLDEAVEKSlkgaSIWdEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 161 TMRIKLQDEILQLHKEFetTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLL 217
Cdd:PRK14239 182 ISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFM 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
20-204 |
5.28e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 113.64 E-value: 5.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDekeflPVQKRkiGFVFQDYALFPNMTVLENL 98
Cdd:PRK11248 19 DINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEG-----PGAER--GVVFQNEGLLPWRNVQDNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF------VNKDK--ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:PRK11248 92 AFglqlagVEKMQrlEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 171 LQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDG 204
Cdd:PRK11248 172 LKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
20-207 |
6.21e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 111.99 E-value: 6.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIWQDEKeflpvqKRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPdSGEVLFDGKPLDIAA------RNRIGYLPEERGLYPKMKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNKDKEL--------ANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:cd03269 92 VYLAQLKGLkkeearrrIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1441214933 171 LQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:cd03269 172 REL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-211 |
8.51e-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: 112.32 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEF-LPVQKRKIGFVFQDYALFpNMTVLEN 97
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRILIDG---HDVRDYtLASLRRQIGLVSQDVFLF-NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKDKELAN--HLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:cd03251 96 IAYGRPGATREEveEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSALDTESER 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 165 KLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGT 211
Cdd:cd03251 176 LVQAALERLMK--NRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGT 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
20-216 |
1.42e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 112.17 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDN---EIWQDEK-----EFLPvQKRKIGFVFqdyalfp 90
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGrplADWSPAElarrrAVLP-QHSSLSFPF------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 nmTVLE--------NLFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALM------NRPKLLLMDEPLS 156
Cdd:PRK13548 92 --TVEEvvamgrapHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 157 ALDptmrIKLQDEILQLHKEF----ETTTILVSHDpseiykL------SNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK13548 170 ALD----LAHQHHVLRLARQLaherGLAVIVVLHD------LnlaaryADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-210 |
1.49e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 111.31 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDN-EIWQDEKEflpvQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:cd03266 23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPdAGFATVDGfDVVKEPAE----ARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF------VNKDKELA--NHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:cd03266 99 LEYfaglygLKGDELTArlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1441214933 170 ILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03266 179 IRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-216 |
1.50e-29 |
|
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: 117.16 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDN-EIWQDEKEFLpvqKRKIGFVFQDYALFPNmTVLEN 97
Cdd:COG4618 350 GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPpTAGSVRLDGaDLSQWDREEL---GRHIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LF-FVNKDKE-------LAN-HlleitelwELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:COG4618 426 IArFGDADPEkvvaaakLAGvH--------EMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 158 LDPTMRIKLQDEILQLhKEFETTTILVSHDPSeIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4618 498 LDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-216 |
5.93e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.59 E-value: 5.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNeiwQDEKEFLPVQK-RKIGFVFQDYAL-FPnMTVLE 96
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPSSGEVRLNG---RPLAAWSPWELaRRRAVLPQHSSLaFP-FTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 nlfFV-----------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRAL-------MNRPKLLLMDEPLSAL 158
Cdd:COG4559 95 ---VValgraphgssaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 159 DptmrIKLQDEILQLHKEF---ETTTILVSHDPseiyklsN-------RVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4559 172 D----LAHQHAVLRLARQLarrGGGVVAVLHDL-------NlaaqyadRILLLHQGRLVAQGTPEEVL 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-234 |
8.53e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVdNEIWQDEKEFLPVqKRKIGFVFQDY-ALFPNMTVLEN 97
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITV-GGMVLSEETVWDV-RRQVGMVFQNPdNQFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFvnkdkELANHLLEITEL-----WELK--------NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:PRK13635 103 VAF-----GLENIGVPREEMvervdQALRqvgmedflNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 165 KLQDEILQLHKEFETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSVllktsgsakFSFEGKLLDI 234
Cdd:PRK13635 178 EVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI---------FKSGHMLQEI 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-209 |
1.98e-28 |
|
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: 106.74 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdEKEFLPV---QKRKIGFVFQdyalfpnmtvl 95
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDGK----EVSFASPrdaRRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 enlffvnkdkelanhlleitelwelknrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHK 175
Cdd:cd03216 83 --------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRA 130
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 176 EfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDD 209
Cdd:cd03216 131 Q-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
20-213 |
2.35e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 114.05 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKV--DNEIWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPtSGTYRVagQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF--------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP-----TMR 163
Cdd:PRK10535 106 NVEVpavyagleRKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgeeVMA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 164 I--KLQDeilQLHkefetTTILVSHDPsEIYKLSNRVIVLKDGKIVDDGTAK 213
Cdd:PRK10535 186 IlhQLRD---RGH-----TVIIVTHDP-QVAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-215 |
3.66e-28 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.21 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNeiwQD-----EKEFLPVQkRKIGFVFQD-YA-LFPN 91
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPtSGEILFDG---QDitglsGRELRPLR-RRMQMVFQDpYAsLNPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVLENL---FFVNKDKELANHLLEITELWEL-------KNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDpt 161
Cdd:COG4608 112 MTVGDIIaepLRIHGLASKAERRERVAELLELvglrpehADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-- 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 162 mrIKLQDEIL----QLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG4608 190 --VSIQAQVLnlleDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-221 |
4.23e-28 |
|
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: 108.01 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLrSLagLEK----AQGIIKVDNeiwQDEKEF-LPVQKRKIGFVFQDYALFpNMTV 94
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVV-SL--LERfydpTSGEILLDG---VDIRDLnLRWLRSQIGLVSQEPVLF-DGTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFF---------VNKDKELANHLLEITELwelknrlPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEP 154
Cdd:cd03249 94 AENIRYgkpdatdeeVEEAAKKANIHDFIMSL-------PDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 155 LSALDPTMRIKLQDEILQLHKefETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSvLLKTSG 221
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE-LMAQKG 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
20-216 |
6.78e-28 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 108.00 E-value: 6.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdEKEFLPVQKR--KIGFVFQD--YALFPNMTV 94
Cdd:COG4167 31 PVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPtSGEILINGH----KLEYGDYKYRckHIRMIFQDpnTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 ---LENLFFVNKD------KELANHLLEITELW-ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:COG4167 107 gqiLEEPLRLNTDltaeerEERIFATLRLVGLLpEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRS 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 165 KLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4167 187 QIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVF 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
20-212 |
7.99e-28 |
|
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: 106.86 E-value: 7.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGiikvdnEIWQDEKEF--LPVQKRK---IGFVFQDYALFPNMT 93
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSG------KILLDGQDItkLPMHKRArlgIGYLPQEASIFRKLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFFV----NKDK----ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIK 165
Cdd:cd03218 92 VEENILAVleirGLSKkereEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 166 LQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTA 212
Cdd:cd03218 172 IQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-218 |
9.05e-28 |
|
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: 111.67 E-value: 9.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDN-EIWQDEKEFLpvqKRKIGFVFQDYALFPNmTVLEN 97
Cdd:TIGR01842 336 GISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPpTSGSVRLDGaDLKQWDRETF---GKHIGYLPQDVELFPG-TVAEN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 L--FFVNKDKELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:TIGR01842 412 IarFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 165 KLQDEILQLHKEfETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSVLLK 218
Cdd:TIGR01842 492 ALANAIKALKAR-GITVVVITHRPSLL-GCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
20-210 |
1.60e-27 |
|
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: 106.26 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEI-WQDEKEFLpvqkRKIGFVF-QDYALFPNMTVLE 96
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTSGEVRVAGLVpWKRRKKFL----RRIGVVFgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVN-----KDKELANHLLEITELWELKNRLPN---SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:cd03267 115 SFYLLAaiydlPPARFKKRLDELSELLDLEELLDTpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRN 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1441214933 169 EILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03267 195 FLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
20-206 |
2.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.12 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKEFlpVQKRKIGFVFQDY-ALFPNMTV--- 94
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLLTEENVW--DIRHKIGMVFQNPdNQFVGATVedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 ----LENLFFVNKD-KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:PRK13650 103 vafgLENKGIPHEEmKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKT 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1441214933 170 ILQLHKEFETTTILVSHDPSEIyKLSNRVIVLKDGKI 206
Cdd:PRK13650 183 IKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-206 |
2.85e-27 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 104.05 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdEKEFLPVQ---KRKIGFVFQD---YALFPNM 92
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGK----PVTRRSPRdaiRAGIAYVPEDrkrEGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 93 TVLENLFfvnkdkelanhlleitelwelknrLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptmrIKLQDEILQ 172
Cdd:cd03215 94 SVAENIA------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD----VGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 1441214933 173 LHKEFE---TTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:cd03215 146 LIRELAdagKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-216 |
4.96e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.35 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVD-NEI--WQDEKeflpVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAtSGRIVFDgKDItdWQTAK----IMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NL----FFVNKDKelanHLLEITELWELKNRL-------PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIK 165
Cdd:PRK11614 100 NLamggFFAERDQ----FQERIKWVYELFPRLherriqrAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 166 LQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK11614 176 IFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
20-260 |
5.59e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.84 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQdeKEFLPVQKRKIGFVFQDY-ALFPNMTV--- 94
Cdd:PRK13632 27 NVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKIDGITIS--KENLKEIRKKIGIIFQNPdNQFIGATVedd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 ----LEN-LFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:PRK13632 105 iafgLENkKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 170 ILQLHKEFETTTILVSHDPSEIYkLSNRVIVLKDGKIVDDGTAKSVLLktsgsakfsfEGKLLDIIKVDVIYVAIIAIGQ 249
Cdd:PRK13632 185 MVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN----------NKEILEKAKIDSPFIYKLSKKL 253
|
250
....*....|.
gi 1441214933 250 QLVEVTISSNE 260
Cdd:PRK13632 254 KGIDPTYNEEE 264
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-216 |
5.86e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.50 E-value: 5.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVD------NEIWQDEKEFLPVQKRKIGFVFQDYALFPnMTV 94
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEgrveffNQNIYERRVNLNRLRRQVSMVHPKPNLFP-MSV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFFVNKD---------KELANHLLEITELW-ELKNRLPNS---LSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPT 161
Cdd:PRK14258 105 YDNVAYGVKIvgwrpkleiDDIVESALKDADLWdEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 162 MRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKD-----GKIVDDGTAKSVL 216
Cdd:PRK14258 185 ASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-215 |
6.12e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.94 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSL-AGLEKAQGIIKVDNEIWQDEKEFLPVqKRKIGFVFQ-------------D 85
Cdd:PRK13633 28 DVNLEVKKGEFLVILGRNGSGKSTIAKHMnALLIPSEGKVYVDGLDTSDEENLWDI-RNKAGMVFQnpdnqivativeeD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 86 YALFPnmtvlENLFFVNKD-KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:PRK13633 107 VAFGP-----ENLGIPPEEiRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 165 KLQDEILQLHKEFETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-215 |
1.92e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 18 NLDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdekeflPVQ--------KRKIGFVFQDYAL 88
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIDGK---------PVRirsprdaiALGIGMVHQHFML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 89 FPNMTVLENL---------FFVNKdKELANHLLEITELWELK---NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:COG3845 92 VPNLTVAENIvlgleptkgGRLDR-KAARARIRELSERYGLDvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 157 ALDP--------TMRiKLQDEilqlhkefETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG3845 171 VLTPqeadelfeILR-RLAAE--------GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-218 |
2.24e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 103.46 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEF-LPVQKRKIGFVFQDYALFpNMTVLEN 97
Cdd:cd03253 19 DVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFyDVSSGSILIDG---QDIREVtLDSLRRAIGVVPQDTVLF-NDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKD--KELANHLLEITELWELKNRLPNS-----------LSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:cd03253 95 IRYGRPDatDEEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTER 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 165 KLQDEILQLHKefETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSVLLK 218
Cdd:cd03253 175 EIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-201 |
4.28e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.99 E-value: 4.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFPNmTVLEN 97
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVNG---VPLADADADSWRDqIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKD---KELANhLLEITELWELKNRLP-----------NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:TIGR02857 416 IRLARPDasdAEIRE-ALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 1441214933 164 IKLQDEILQLHKefETTTILVSHDPSEIYkLSNRVIVL 201
Cdd:TIGR02857 495 AEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-215 |
5.56e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 103.31 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNE-IWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEILFDGEnIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF-VNKDKELANHLLEITELWELK--------NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP-TMRI--K 165
Cdd:PRK11831 105 VAYpLREHTQLPAPLLHSTVMMKLEavglrgaaKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPiTMGVlvK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1441214933 166 LQDEilqLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK11831 185 LISE---LNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-216 |
5.95e-26 |
|
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: 106.69 E-value: 5.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKT----TLLRSLA-GLEKAQGIIKVDNE--IWQDEKEFLPVQKRKIGFVFQD--YALFP 90
Cdd:COG4172 28 GVSFDIAAGETLALVGESGSGKSvtalSILRLLPdPAAHPSGSILFDGQdlLGLSERELRRIRGNRIAMIFQEpmTSLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTV----LENLFF---VNKD--KELANHLLEITELWELKNRL---PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSAL 158
Cdd:COG4172 108 LHTIgkqiAEVLRLhrgLSGAaaRARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAMALANEPDLLIADEPTTAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 159 DPTmrikLQDEILQL----HKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4172 188 DVT----VQAQILDLlkdlQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELF 245
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-216 |
7.52e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 102.35 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNE---IWQD--------EKEFLPVQKRKIGFVFQDYAL 88
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNGQtinLVRDkdgqlkvaDKNQLRLLRTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 89 FPNMTVLENLFFV---------NKDKELANHLLE---ITElwELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:PRK10619 104 WSHMTVLENVMEApiqvlglskQEARERAVKYLAkvgIDE--RAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 157 ALDPtmriKLQDEILQLHKEFE---TTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK10619 182 ALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
10-204 |
7.86e-26 |
|
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: 101.74 E-value: 7.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 10 LHGSNG----VMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQG--IIKVDNEIWQD-----EKEFLPVQKRK 78
Cdd:COG4778 16 LHLQGGkrlpVLD-GVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSgsILVRHDGGWVDlaqasPREILALRRRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 79 IGFVFQdyalF----PNMT----VLENLFFVNKDKELAN-------HLLEITE-LWELKnrlPNSLSGGQKQRVSLCRAL 142
Cdd:COG4778 95 IGYVSQ----FlrviPRVSaldvVAEPLLERGVDREEARararellARLNLPErLWDLP---PATFSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 143 MNRPKLLLMDEPLSALDPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDG 204
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-215 |
8.46e-26 |
|
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: 101.45 E-value: 8.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEiwqdEKEFLPVQKRK---IGFVFQDYALFPNMTVL 95
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKsGSIRLDGE----DITKLPPHERAragIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFFV-----NKDKELANHLLEITE-LWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:TIGR03410 94 ENLLTGlaalpRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1441214933 170 ILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:TIGR03410 174 IRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
20-232 |
2.24e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.09 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL------------------EKAQGIIKVDNEIWQDEKEFLPVQK----- 76
Cdd:PRK13651 25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknkKKTKEKEKVLEKLVIQKTRFKKIKKikeir 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 77 RKIGFVFQ--DYALFPNmTVLENLFF------VNKD--KELANHLLEITELWE--LKnRLPNSLSGGQKQRVSLCRALMN 144
Cdd:PRK13651 105 RRVGVVFQfaEYQLFEQ-TIEKDIIFgpvsmgVSKEeaKKRAAKYIELVGLDEsyLQ-RSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 145 RPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFEtTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTsgsaK 224
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDN----K 257
|
....*...
gi 1441214933 225 FSFEGKLL 232
Cdd:PRK13651 258 FLIENNME 265
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-213 |
2.45e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.24 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGL---EKAQG--IIKVDNEIWQDEKEFLPVQKRK--IGFVFQDYALFPNMT 93
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGshIELLGRTVQREGRLARDIRKSRanTGYIFQQFNLVNRLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENL----------------FFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK09984 103 VLENVligalgstpfwrtcfsWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 158 LDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAK 213
Cdd:PRK09984 183 LDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-207 |
2.60e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 100.33 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIE--IKKELHGSNGVMNLDVNLdiRSKDFVALTGLSGSGKTTLLRSLAGLEK--AQGIIKVDNEIWQDEKEFLPVQK 76
Cdd:PRK10908 1 MIRFEhvSKAYLGGRQALQGVTFHM--RPGEMAFLTGHSGAGKSTLLKLICGIERpsAGKIWFSGHDITRLKNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 77 RKIGFVFQDYALFPNMTVLEN----LFFVNKDKE-----LANHLLEITELWELKNrLPNSLSGGQKQRVSLCRALMNRPK 147
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNvaipLIIAGASGDdirrrVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 148 LLLMDEPLSALDPTmrikLQDEILQLHKEFE---TTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:PRK10908 158 VLLADEPTGNLDDA----LSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-205 |
2.63e-25 |
|
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: 99.47 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVdneiwqdekeflpvqKRKIGFVFQdYALFPNMTVLEN- 97
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEKLSGSVSV---------------PGSIAYVSQ-EPWIQNGTIRENi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKDKELANHLLEITELWE-LKNrLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIK 165
Cdd:cd03250 87 LFGKPFDEERYEKVIKACALEPdLEI-LPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1441214933 166 LQDEILQLHKEFETTTILVSHdpsEIYKLS--NRVIVLKDGK 205
Cdd:cd03250 166 IFENCILGLLLNNKTRILVTH---QLQLLPhaDQIVVLDNGR 204
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-215 |
2.73e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.79 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 2 IKIEIKKELHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQ--DEKEFLPVqKRKI 79
Cdd:PRK15134 287 IRKGILKRTVDHNVVVK-NISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHnlNRRQLLPV-RHRI 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQD--YALFPNMTVLE-----------NLFFVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRP 146
Cdd:PRK15134 365 QVVFQDpnSSLNPRLNVLQiieeglrvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 147 KLLLMDEPLSALDPTmrikLQDEILQLHKEFETT----TILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK15134 445 SLIILDEPTSSLDKT----VQAQILALLKSLQQKhqlaYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-216 |
3.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.73 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 19 LDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEI---WQDEKEFLPVQKrKIGFVFQ--DYALFPNm 92
Cdd:PRK13643 23 FDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGKVTVGDIVvssTSKQKEIKPVRK-KVGVVFQfpESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 93 TVLENLFF------VNKDK--ELANHLLEIT----ELWElknRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:PRK13643 101 TVLKDVAFgpqnfgIPKEKaeKIAAEKLEMVgladEFWE---KSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 161 TMRIKLQDEILQLHKEFEtTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-215 |
3.34e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdekEFLPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPdSGEVLWDGE------PLDPEDRRRIGYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:COG4152 93 VYLarlkglskAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 171 LQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG4152 173 RELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-215 |
8.38e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLE-KAQGIIKVDN-EIWQDE--KEFLPVQKrKIGFVFQdyalFPNM--- 92
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDtLITSTSknKDIKQIRK-KVGLVFQ----FPESqlf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 93 --TVLENLFF------VNKDK--ELAN---HLLEITElwELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALD 159
Cdd:PRK13649 100 eeTVLKDVAFgpqnfgVSQEEaeALAReklALVGISE--SLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 160 PTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK13649 178 PKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-215 |
1.04e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.95 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVD-----NEIWQ-DEKEFLPVQKRKIGFVFQD--YALFPN 91
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSatfngREILNlPEKELNKLRAEQISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVLENLFFV-------NKDK--ELANHLLEITELWELKNRL---PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALD 159
Cdd:PRK09473 114 MRVGEQLMEVlmlhkgmSKAEafEESVRMLDAVKMPEARKRMkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 160 PTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK09473 194 VTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-215 |
1.69e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.17 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA---------QGIIKVDNEIWQDekeflpvqKRK-IGFVFQD--YA 87
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAtdgevawlgKDLLGMKDDEWRA--------VRSdIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 88 LFPNMTVLE------NLFFVNKDKE-----LANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:PRK15079 111 LNPRMTIGEiiaeplRTYHPKLSRQevkdrVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 157 ALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
20-216 |
1.77e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 98.43 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEiwqdEKEFLPVQ---KRKIGFVFQDYALFPNMTVL 95
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDE----DISLLPLHaraRRGIGYLPQEASIFRRLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFFV---------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:PRK10895 97 DNLMAVlqirddlsaEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1441214933 167 QdEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK10895 177 K-RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-210 |
2.29e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.60 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIwqdekeflpvqkrkIGFVFQDYALFPNMTVLENL 98
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPdSGTVTVRGRV--------------SSLLGLGGGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFV-----NKDKELANHLLEITELWELKNR--LP-NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:cd03220 106 YLNgrllgLSRKEIDEKIDEIIEFSELGDFidLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 171 LQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:cd03220 186 RELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-215 |
2.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.13 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNE--IWQDEKEFLPVQKRKIGFVFQ--DYALFPNmTV 94
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGYhiTPETGNKNLKKLRKKVSLVFQfpEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFFVNKD--------KELANHLLEITELWE-LKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPtmriK 165
Cdd:PRK13641 104 LKDVEFGPKNfgfsedeaKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP----E 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 166 LQDEILQLHKEFET---TTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK13641 180 GRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-216 |
2.86e-24 |
|
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: 97.94 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVD-NEIWQDEKEFLpvqKRKIGFVFQDYALFpNMTVLEN 97
Cdd:cd03252 20 NISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPeNGRVLVDgHDLALADPAWL---RRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNK--DKE-------LANHLLEITELWELKNRLPN----SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:cd03252 96 IALADPgmSMErvieaakLAGAHDFISELPEGYDTIVGeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 165 KLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:cd03252 176 AIMRNMHDICA--GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELL 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-207 |
3.20e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 97.34 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKvdNEIWQDEKEFLPVQ-KRKIGFVFQDYALFPNMTVLENL 98
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTS--GQILFNGQPRKPDQfQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFV------------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTmrikL 166
Cdd:cd03234 103 TYTailrlprkssdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF----T 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 167 QDEILQLHKEFETT--TILVS-HDP-SEIYKLSNRVIVLKDGKIV 207
Cdd:cd03234 179 ALNLVSTLSQLARRnrIVILTiHQPrSDLFRLFDRILLLSSGEIV 223
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-211 |
4.91e-24 |
|
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: 96.79 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEIWQDekefLPVQK--RKIGFVFQDYALFPNmTVLE 96
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLvELSSGSILIDGVDISK----IGLHDlrSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVNK--DKELaNHLLEITELWELKNRLP-----------NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTmr 163
Cdd:cd03244 97 NLDPFGEysDEEL-WQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASVDPE-- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 164 iklQDEILQ--LHKEF-ETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGT 211
Cdd:cd03244 174 ---TDALIQktIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-216 |
6.35e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.43 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEIWQDEKEFLPVQ----KRKIGFVFQDYALFPNMTV 94
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSKIKVDGKVLYFGKDIFQIDaiklRKEVGMVFQQPNPFPHLSI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFFVNKD---------KELANHLLEITELW-ELKNRL---PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPT 161
Cdd:PRK14246 108 YDNIAYPLKShgikekreiKKIVEECLRKVGLWkEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 162 MRIKLQDEILQLHKEFetTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK14246 188 NSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
20-216 |
1.01e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.25 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdEKEFLPVQKRK---IGFVFQDYALFPNMTVL 95
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGE----DITHLPMHKRArlgIGYLPQEASIFRKLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENL------FFVNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:COG1137 97 DNIlavlelRKLSKKerEERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 168 DEILQLhkefetTT----ILVS-HDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1137 177 KIIRHL------KErgigVLITdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-211 |
1.12e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 100.30 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFPNmTVLENLF 99
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKING---IELRELDPESWRKhLSWVGQNPQLPHG-TLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 FVNKD--KELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:PRK11174 445 LGNPDasDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 167 QDEILQLHKefETTTILVSHDPSEIYKLsNRVIVLKDGKIVDDGT 211
Cdd:PRK11174 525 MQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-187 |
1.37e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.77 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLE------KAQG-IIKVDNEIWqdEKEFLPVQ-KRKIGFVFQDYALFPN 91
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVEGkVTFHGKNLY--APDVDPVEvRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 mTVLENLFF---VNKDK----ELANHLLEITELW-ELKNRLPNS---LSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:PRK14243 106 -SIYDNIAYgarINGYKgdmdELVERSLRQAALWdEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDEPCSALDP 184
|
170 180
....*....|....*....|....*..
gi 1441214933 161 TMRIKLQDEILQLHKEFetTTILVSHD 187
Cdd:PRK14243 185 ISTLRIEELMHELKEQY--TIIIVTHN 209
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-208 |
2.02e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIwqdekeflpvqkrKIGFVFQDYALF-PNMTVLEN 97
Cdd:COG0488 333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDsGTVKLGETV-------------KIGYFDQHQEELdPDKTVLDE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LffvnkdKELANHLLEItelwELKNRL------------P-NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRi 164
Cdd:COG0488 400 L------RDGAPGGTEQ----EVRGYLgrflfsgddafkPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL- 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 165 klqdEIL-QLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVD 208
Cdd:COG0488 469 ----EALeEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
20-216 |
2.36e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.21 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDEKEFLPVQKRKIGFVFQD-YALFPNMTVLENL 98
Cdd:PRK13644 20 NINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNKD--------KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:PRK13644 100 AFGPENlclppieiRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1441214933 171 LQLHKEFEtTTILVSHDPSEIYkLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK13644 180 KKLHEKGK-TIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVL 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-188 |
2.66e-23 |
|
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: 98.97 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEIWQDEKEFLPvqKRKIGFVFQDYALFp 90
Cdd:TIGR02868 346 GAPPVLD-GVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEV--RRRVSVCAQDAHLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENLFFVNK---DKELANhLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:TIGR02868 422 DTTVRENLRLARPdatDEELWA-ALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|..
gi 1441214933 157 ALDPTMRIKLQDEILQlhKEFETTTILVSHDP 188
Cdd:TIGR02868 501 HLDAETADELLEDLLA--ALSGRTVVLITHHL 530
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
7-211 |
7.09e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 97.81 E-value: 7.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 7 KKELHGSNGVmnldvnldIRSKDFVALTGLSGSGKTTLL-----RSLAGLEKaQGIIKVDNEiwqdekeflPVQKRKI-- 79
Cdd:TIGR00955 38 KHLLKNVSGV--------AKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG-SGSVLLNGM---------PIDAKEMra 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 --GFVFQDYALFPNMTVLENLFF---------VNKD--KELANHLLEITELWELKNRL---PN---SLSGGQKQRVSLCR 140
Cdd:TIGR00955 100 isAYVQQDDLFIPTLTVREHLMFqahlrmprrVTKKekRERVDEVLQALGLRKCANTRigvPGrvkGLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 141 ALMNRPKLLLMDEPLSALDPTMriklQDEILQLHKEFET---TTILVSHDPS-EIYKLSNRVIVLKDGKIVDDGT 211
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFM----AYSVVQVLKGLAQkgkTIICTIHQPSsELFELFDKIILMAEGRVAYLGS 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-207 |
9.65e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.01 E-value: 9.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdekeflPVQ--------KRKIGFVFQD---YA 87
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPAdSGEIRLDGK---------PVRirsprdaiRAGIAYVPEDrkgEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 88 LFPNMTVLENL-----------FFVNKDKE--LANHLLEitelwELKNRLPN------SLSGGQKQRVSLCRALMNRPKL 148
Cdd:COG1129 341 LVLDLSIRENItlasldrlsrgGLLDRRREraLAEEYIK-----RLRIKTPSpeqpvgNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 149 LLMDEplsaldPTMRIklqD-----EILQLHKEFE---TTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:COG1129 416 LILDE------PTRGI---DvgakaEIYRLIRELAaegKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
20-211 |
1.12e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.34 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLE---------KAQGIIKVDNEIWQDekeflpVQKRKIGFVFQDYALFP 90
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDtptsgdvifNGQPMSKLSSAAKAE------LRNQKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENL---FFVNKDK-----ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptm 162
Cdd:PRK11629 101 DFTALENVampLLIGKKKpaeinSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD--- 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 163 rIKLQDEILQLHKEFE----TTTILVSHDPSEIYKLSnRVIVLKDGKIVDDGT 211
Cdd:PRK11629 178 -ARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAELS 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-216 |
1.36e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEI---------WQDEKEFlpvqKRKIGFVFQDYALFPn 91
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrsifnYRDVLEF----RRRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVLENLFFVNKDKEL---------ANHLLEITELWE-LKNRLPNS---LSGGQKQRVSLCRALMNRPKLLLMDEPLSAL 158
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLvprkefrgvAQARLTEVGLWDaVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 159 DPTMRIKLQDEILQLHKEFetTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK14271 195 DPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-220 |
1.79e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.00 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 1 MIKIEIKKELHGSNGVmnldvNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEIWQDEKEFlpVQKRKI 79
Cdd:PRK13642 11 VFKYEKESDVNQLNGV-----SFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDGELLTAENVW--NLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 80 GFVFQDY-ALFPNMTVLENLFFVNKD---------KELANHLLEITELwELKNRLPNSLSGGQKQRVSLCRALMNRPKLL 149
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGMENqgipreemiKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 150 LMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGtAKSVLLKTS 220
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEA-APSELFATS 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-217 |
3.02e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 4 IEIKkELH-----GSNGVMNLDVNLDIRSKdfVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKV-DNEIWQDEKEFLpvqK 76
Cdd:PRK13647 5 IEVE-DLHfrykdGTKALKGLSLSIPEGSK--TALLGPNGAGKSTLLLHLNGIYLPQrGRVKVmGREVNAENEKWV---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 77 RKIGFVFQDY--ALFpNMTVLENLFF--VNKD------KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRP 146
Cdd:PRK13647 79 SKVGLVFQDPddQVF-SSTVWDDVAFgpVNMGldkdevERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 147 KLLLMDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGtAKSVLL 217
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLT 226
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-216 |
3.52e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.45 E-value: 3.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEI-WQDEkeflpvqkrkIGFVFQdyalfPNMTVLEN 97
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPtSGRVEVNGRVsALLE----------LGAGFH-----PELTGREN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFV-----NKDKELANHLLEITELWELKN--RLP-NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:COG1134 109 IYLNgrllgLSRKEIDEKFDEIVEFAELGDfiDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLAR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 170 ILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG1134 189 IRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-221 |
3.78e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.94 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL----EKAQGIIKVDNeIWQDEKEFLPVqKRKIGFVFQDY-ALFPNMTV 94
Cdd:PRK13640 25 DISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDG-ITLTAKTVWDI-REKVGIVFQNPdNQFVGATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFF--------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:PRK13640 103 GDDVAFglenravpRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 167 QDEILQLHKEFETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGT-----AKSVLLKTSG 221
Cdd:PRK13640 183 LKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSpveifSKVEMLKEIG 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-206 |
4.49e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 4.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIwqdekeflpvqkrKIGFVFQDYALFPNMTVLENL 98
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPKGL-------------RIGYLPQEPPLDDDLTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNKD-------KELANHLL--------EITEL---------WELK-----------------NRLPNSLSGGQKQRVS 137
Cdd:COG0488 83 LDGDAElraleaeLEELEAKLaepdedleRLAELqeefealggWEAEaraeeilsglgfpeedlDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 138 LCRALMNRPKLLLMDEPLSALDPTMRIKLQDEIlqlhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSHDRYFLDRVATRILELDRGKL 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
20-205 |
4.54e-22 |
|
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: 89.43 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDneiwqdekeflpvQKRKIGFVFQdyalfpnmtvlenl 98
Cdd:cd03221 18 DISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIVTWG-------------STVKIGYFEQ-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 ffvnkdkelanhlleitelwelknrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEIlqlhKEFE 178
Cdd:cd03221 71 -----------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL----KEYP 117
|
170 180
....*....|....*....|....*..
gi 1441214933 179 TTTILVSHDPSEIYKLSNRVIVLKDGK 205
Cdd:cd03221 118 GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-216 |
4.81e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 92.30 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDN--EIWQDEKEFLPVQKRKI-----GFVFQDYALFPN 91
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSArLAPDAGEVHYRMrdGQLRDLYALSEAERRRLlrtewGFVHQHPRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVL------ENLFFVN-----KDKELANHLLEITELWElkNR---LPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK11701 104 MQVSaggnigERLMAVGarhygDIRATAGDWLERVEIDA--ARiddLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 158 LDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK11701 182 LDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-215 |
5.50e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.49 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 32 ALTGLSGSGKTTLLRSLAGLEK-AQGIIKVD-NEIWQDEKEFLPVQKRKIGFVFQD-YA-LFPNMTV---LENLFFVNKD 104
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETpTGGELYYQgQDLLKADPEAQKLLRQKIQIVFQNpYGsLNPRKKVgqiLEEPLLINTS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 105 ---KELANHLLEITELWELK----NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEF 177
Cdd:PRK11308 125 lsaAERREKALAMMAKVGLRpehyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQEL 204
|
170 180 190
....*....|....*....|....*....|....*...
gi 1441214933 178 ETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK11308 205 GLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-215 |
6.97e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.92 E-value: 6.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 6 IKKELHGSNgvmnlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQG--IIKVDNEIWQDEKEFLPVQKRKIGFVF 83
Cdd:PRK10261 333 VTREVHAVE-----KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGgeIIFNGQRIDTLSPGKLQALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 84 QD-YA-LFPNMTV---------LENLFFVNKDKELANHLLEITELW-ELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLM 151
Cdd:PRK10261 408 QDpYAsLDPRQTVgdsimeplrVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 152 DEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK10261 488 DEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
20-206 |
7.37e-22 |
|
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: 90.92 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEIWQDEkeflpvQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:TIGR03740 18 NISLTVPKNSVYGLLGPNGAGKSTLLKMITGiLRPTSGEIIFDGHPWTRK------DLHKIGSLIESPPLYENLTARENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNK----DKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPtmrIKLQD--EILQ 172
Cdd:TIGR03740 92 KVHTTllglPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP---IGIQElrELIR 168
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 173 LHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:TIGR03740 169 SFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
20-217 |
9.73e-22 |
|
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: 94.81 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQD-EKEFLpvqKRKIGFVFQDYALFPNmTVLEN 97
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsGEILLNGFSLKDiDRHTL---RQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKDKELANHLLEITELWELKNRLPN--------------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:TIGR01193 568 LLLGAKENVSQDEIWAACEIAEIKDDIENmplgyqtelseegsSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 164 IKLQDEILQLHkefETTTILVSHDPSeIYKLSNRVIVLKDGKIVDDGTAKSVLL 217
Cdd:TIGR01193 648 KKIVNNLLNLQ---DKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-215 |
1.14e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 91.68 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVD-NEIWQDEKEFLPVQKrKIGFVFQ--DYALFPNmTVLE 96
Cdd:PRK13639 21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIKgEPIKYDKKSLLEVRK-TVGIVFQnpDDQLFAP-TVEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF------VNKD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:PRK13639 99 DVAFgplnlgLSKEevEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1441214933 169 EILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK13639 179 LLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-211 |
1.21e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL---EKAQGIIKvDNEIWQDEKEFLPVQ--KRKIGFVFQ--DYALFPNm 92
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisETGQTIVG-DYAIPANLKKIKEVKrlRKEIGLVFQfpEYQLFQE- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 93 TVLENLFF----VNKDKELA----NHLLEITEL-WELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:PRK13645 107 TIEKDIAFgpvnLGENKQEAykkvPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1441214933 164 IKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK13645 187 EDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-201 |
1.64e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.16 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALF 89
Cdd:PRK10247 18 GDAKILN-NISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEG---EDISTLKPEIYRQqVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 90 PNmTVLENLFF---VNKDKELANHLLEITELWELKNRL----PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:PRK10247 94 GD-TVYDNLIFpwqIRNQQPDPAIFLDDLERFALPDTIltknIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1441214933 163 RIKLQDEILQLHKEFETTTILVSHDPSEIyKLSNRVIVL 201
Cdd:PRK10247 173 KHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITL 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-237 |
2.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDN-EIWQD--EKEFLPVQKRkIGFVFQ--DYALFPNMT 93
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDiTITHKtkDKYIRPVRKR-IGMVFQfpESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLF----F---VNKDKELANHLLeiTELWELKNRL---PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:PRK13646 104 EREIIFgpknFkmnLDEVKNYAHRLL--MDLGFSRDVMsqsPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 164 IKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTSGSAKFSFEgkLLDIIKV 237
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIG--LPEIVQL 253
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-204 |
2.43e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKV--DNEIWqdekeFLPvQKrkigfvfqdyALFPNMTVLE 96
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPyGSGRIARpaGARVL-----FLP-QR----------PYLPLGTLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVN-----KDKELAnHLLEITELWELKNRL------PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPtmriK 165
Cdd:COG4178 445 ALLYPAtaeafSDAELR-EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE----E 519
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1441214933 166 LQDEILQ-LHKEFETTTIL-VSHDPSEIyKLSNRVIVLKDG 204
Cdd:COG4178 520 NEAALYQlLREELPGTTVIsVGHRSTLA-AFHDRVLELTGD 559
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-216 |
2.90e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEIWQD--EKEFlpvqKRKIGFVFQDYALFPNMTVLE 96
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmTPAHGHVWLDGEHIQHyaSKEV----ARRIGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 ----------NLF--FVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:PRK10253 101 lvargryphqPLFtrWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 165 KLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-221 |
3.17e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.20 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQDEKEFLpvqKRKIGFVFQD-YALFPNMTV-- 94
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQaITDDNFEKL---RKHIGIVFQNpDNQFVGSIVky 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 -----LENlFFVNKDK--ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:PRK13648 104 dvafgLEN-HAVPYDEmhRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 168 DEILQLHKEFETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSVLLKTSG 221
Cdd:PRK13648 183 DLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
20-236 |
4.25e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 90.29 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEIWQDEKEFLPVQKRKIGFVFQ--DYALFpNMTVLE 96
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGiLKPSSGRILFDGKPIDYSRKGLMKLRESVGMVFQdpDNQLF-SASVYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF--VN----KD--KELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:PRK13636 103 DVSFgaVNlklpEDevRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMK 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 169 EILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKT----SGSAKFSFEGKLLDIIK 236
Cdd:PRK13636 183 LLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKemlrKVNLRLPRIGHLMEILK 254
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
20-187 |
4.54e-21 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 87.86 E-value: 4.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKEFLPVQKRKIGFVFQ--DYALFpNMTVLE 96
Cdd:TIGR01166 10 GLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQsGAVLIDGEPLDYSRKGLLERRQRVGLVFQdpDDQLF-AADVDQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF--VN---KDKELANHL---LEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:TIGR01166 89 DVAFgpLNlglSEAEVERRVreaLTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLA 168
|
170
....*....|....*....
gi 1441214933 169 EILQLHKEfETTTILVSHD 187
Cdd:TIGR01166 169 ILRRLRAE-GMTVVISTHD 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
20-218 |
4.57e-21 |
|
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: 92.56 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTL---LRSLAGLEKAQGII-------------------------------KVDNEIW 65
Cdd:TIGR03269 18 NISFTIEEGEVLGILGRSGAGKSVLmhvLRGMDQYEPTSGRIiyhvalcekcgyverpskvgepcpvcggtlePEEVDFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 66 Q-DEKEFLPVQKRkIGFVFQ-DYALFPNMTVLENLFFVNKD-----KELANHLLEITELWELKNR---LPNSLSGGQKQR 135
Cdd:TIGR03269 98 NlSDKLRRRIRKR-IAIMLQrTFALYGDDTVLDNVLEALEEigyegKEAVGRAVDLIEMVQLSHRithIARDLSGGEKQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 136 VSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:TIGR03269 177 VVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
...
gi 1441214933 216 LLK 218
Cdd:TIGR03269 257 VAV 259
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-219 |
8.83e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 8.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQdekeFLPVQ-KRKIGFVFQDYALFPNMTVLE 96
Cdd:PRK11231 20 DLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKpISM----LSSRQlARRLALLPQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 ----------NLF--FVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptmrI 164
Cdd:PRK11231 96 lvaygrspwlSLWgrLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD----I 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 165 KLQDEILQLHKEFET---TTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV----LLKT 219
Cdd:PRK11231 172 NHQVELMRLMRELNTqgkTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVmtpgLLRT 233
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
9-216 |
1.91e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 89.19 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 9 ELHGSNG-VMNLD-VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDeKEFL---PVQKRK----- 78
Cdd:COG4170 12 EIDTPQGrVKAVDrVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNG-IDLLklsPRERRKiigre 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 79 IGFVFQD--YALFPNMTVLENLFFVNKDKELANH--------------LLE---ITELWELKNRLPNSLSGGQKQRVSLC 139
Cdd:COG4170 91 IAMIFQEpsSCLDPSAKIGDQLIEAIPSWTFKGKwwqrfkwrkkraieLLHrvgIKDHKDIMNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 140 RALMNRPKLLLMDEPLSALDPTMRI---KLQDEILQLHKefeTTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAqifRLLARLNQLQG---TSILLISHDLESISQWADTITVLYCGQTVESGPTEQIL 247
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-205 |
4.65e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.94 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 29 DFVALTGLSGSGKTTLLRSLAGleKAQGIIKVDNEIWQDEKEFLPVQKRkIGFVFQDYALFPNMTVLENLFFV------- 101
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAG--RIQGNNFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETLVFCsllrlpk 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 102 --NKDKELANHLLEITELWELK-------NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQ 172
Cdd:PLN03211 172 slTKQEKILVAESVISELGLTKcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGS 251
|
170 180 190
....*....|....*....|....*....|...
gi 1441214933 173 LHKEFETTTILVSHDPSEIYKLSNRVIVLKDGK 205
Cdd:PLN03211 252 LAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-188 |
4.76e-20 |
|
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: 85.49 E-value: 4.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVDNeiwQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENLF 99
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRpDSGEVRWNG---TPLAEQRDEPHENILYLGHLPGLKPELSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 FVNKDKELANH----LLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTmRIKLQDEILQLHK 175
Cdd:TIGR01189 96 FWAAIHGGAQRtiedALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA-GVALLAGLLRAHL 174
|
170
....*....|...
gi 1441214933 176 EFETTTILVSHDP 188
Cdd:TIGR01189 175 ARGGIVLLTTHQD 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-203 |
1.29e-19 |
|
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: 83.36 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIK--VDNEIWqdekeFLPvQKrkigfvfqdyALFPNMTVLE 96
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSGRIGmpEGEDLL-----FLP-QR----------PYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFvnkdkelanhlleiteLWELKnrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMriklQDEILQLHKE 176
Cdd:cd03223 83 QLIY----------------PWDDV------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES----EDRLYQLLKE 136
|
170 180
....*....|....*....|....*..
gi 1441214933 177 FETTTILVSHDPSeIYKLSNRVIVLKD 203
Cdd:cd03223 137 LGITVISVGHRPS-LWKFHDRVLDLDG 162
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
20-211 |
1.54e-19 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 88.08 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEiwqdEKEFLP--VQKRKIGFVFQDYALFPNmTVLE 96
Cdd:TIGR03796 497 NFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLyQPWSGEILFDGI----PREEIPreVLANSVAMVDQDIFLFEG-TVRD 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVN------------KDKELANHLLEI-----TELWE-LKNrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSAL 158
Cdd:TIGR03796 572 NLTLWDptipdadlvracKDAAIHDVITSRpggydAELAEgGAN-----LSGGQRQRLEIARALVRNPSILILDEATSAL 646
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 159 DPTMRIKLQDEIlqlhKEFETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGT 211
Cdd:TIGR03796 647 DPETEKIIDDNL----RRRGCTCIIVAHRLSTI-RDCDEIIVLERGKVVQRGT 694
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-207 |
1.94e-19 |
|
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: 83.85 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL----EKAQGIIKVDNEiwqDEKEFLPVQKRKIGFVFQDYALFPNMTVL 95
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVEGDIHYNGI---PYKEFAEKYPGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFFVNKDKelanhlleitelwelKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHK 175
Cdd:cd03233 102 ETLDFALRCK---------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAD 166
|
170 180 190
....*....|....*....|....*....|...
gi 1441214933 176 EFETTTILVSHDPS-EIYKLSNRVIVLKDGKIV 207
Cdd:cd03233 167 VLKTTTFVSLYQASdEIYDLFDKVLVLYEGRQI 199
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-207 |
2.15e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.24 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 19 LDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK---AQGIIKV-DNEIWQDEkeflpvqkrkigfvfqdyalfpnmTV 94
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtpVAGCVDVpDNQFGREA------------------------SL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFfVNKDKELANHLLEITELWE--LKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQ 172
Cdd:COG2401 103 IDAIG-RKGDFKDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 1441214933 173 LHKEFETTTILVSHDPsEIYK-LSNRVIVLKDGKIV 207
Cdd:COG2401 182 LARRAGITLVVATHHY-DVIDdLQPDLLIFVGYGGV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-211 |
7.32e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 7.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLA-GLEKAQGIIKVD-NEIWQDEKEFLpvqKRKIGFVFQDYALFpNMTVLEN 97
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQrVFDPQSGRILIDgTDIRTVTRASL---RRNIAVVFQDAGLF-NRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LfFVNK----DKELANhLLEITELWELKNRLP-----------NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:PRK13657 429 I-RVGRpdatDEEMRA-AAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVET 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1441214933 163 RIKLQDEILQLHKefETTTILVSHDPSEIyKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK13657 507 EAKVKAALDELMK--GRTTFIIAHRLSTV-RNADRILVFDNGRVVESGS 552
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-191 |
7.86e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.90 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVdneiwqdekeflpVQKRKIGFVFQDYAL---FPnMTVL 95
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRR-------------AGGARVAYVPQRSEVpdsLP-LTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 E----NLF--------FVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:NF040873 76 DlvamGRWarrglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180
....*....|....*....|....*...
gi 1441214933 164 IKLQDEILQLHKEfETTTILVSHDPSEI 191
Cdd:NF040873 156 ERIIALLAEEHAR-GATVVVVTHDLELV 182
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-216 |
1.11e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.30 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNE----------------IWQDEKEFLPVQKRkIGFV 82
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMiEPTSGELLIDDHplhfgdysyrsqrirmIFQDPSTSLNPRQR-ISQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 83 FqDYALFPNmTVLENlffVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:PRK15112 110 L-DFPLRLN-TDLEP---EQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 163 RIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-218 |
1.46e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEiwQDEKEFLPVQKRKIGFVFQ--DYALFpNMTVLEN 97
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGE--PITKENIREVRKFVGLVFQnpDDQIF-SPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF----VNKDKELANH----LLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDE 169
Cdd:PRK13652 100 IAFgpinLGLDEETVAHrvssALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1441214933 170 ILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLK 218
Cdd:PRK13652 180 LNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-187 |
2.23e-18 |
|
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: 84.60 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 35 GLSGSGKTTLLRSLAGLEKaqgiiKVDNEIWqdekeflPVQKRKIGFVFQDYALFPNMTVLENLF--------------- 99
Cdd:TIGR03719 38 GLNGAGKSTLLRIMAGVDK-----DFNGEAR-------PQPGIKVGYLPQEPQLDPTKTVRENVEegvaeikdaldrfne 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 ----FVNKDKELANHLLEITEL---------WELKN---------RLP------NSLSGGQKQRVSLCRALMNRPKLLLM 151
Cdd:TIGR03719 106 isakYAEPDADFDKLAAEQAELqeiidaadaWDLDSqleiamdalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1441214933 152 DEPLSALDPTMRIKLQdeilQLHKEFETTTILVSHD 187
Cdd:TIGR03719 186 DEPTNHLDAESVAWLE----RHLQEYPGTVVAVTHD 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-210 |
2.46e-18 |
|
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: 80.43 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQgiikvDNEIWQDEKEFLPVQK---RKIGFVFQDYALFpNMTVLE 96
Cdd:cd03247 20 NLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-----QGEITLDGVPVSDLEKalsSLISVLNQRPYLF-DTTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLffvnkdkelanhlleitelwelknrlPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKe 176
Cdd:cd03247 94 NL--------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK- 146
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 177 fETTTILVSHDPSEIYKLsNRVIVLKDGKIVDDG 210
Cdd:cd03247 147 -DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-215 |
2.50e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 2.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEIWQDEKEFLPVQkRKIGFVFQDYALFPNMTVLENL 98
Cdd:PRK09700 23 SVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNINYNKLDHKLAAQ-LGIGIIYQELSVIDELTVLENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF---------------VNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:PRK09700 102 YIgrhltkkvcgvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEV 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 164 IKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK09700 182 DYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-210 |
3.94e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 2 IKIEIKKELHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEiwqDEKEFLPVQKRKIG 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVD-GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGE---PVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 81 FVFQDYALFPNMTVLENLFFVNK--------DKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENLLVFGRyfglsaaaARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 153 EPLSALDPTMRiKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:PRK13537 164 EPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-219 |
4.14e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 4.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIkvdneIWQDE-----KEFLPVQKRKIGFVFQDyalfPNmtv 94
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAV-----LWQGKpldysKRGLLALRQQVATVFQD----PE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 lENLFFVNKDKELANHL-----------------LEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK13638 88 -QQIFYTDIDSDIAFSLrnlgvpeaeitrrvdeaLTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 158 LDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKT 219
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACT 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-211 |
5.36e-18 |
|
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: 83.72 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFpNMTVLEN 97
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFyDVTSGRILIDG---QDIRDVTQASLRAaIGIVPQDTVLF-NDTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF---------VNKDKELAnHLLE-ITEL---WE-------LKnrlpnsLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:COG5265 452 IAYgrpdaseeeVEAAARAA-QIHDfIESLpdgYDtrvgergLK------LSGGEKQRVAIARTLLKNPPILIFDEATSA 524
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 158 LDPTMRIKLQDEILQLHKefETTTILVSHdpseiyKLS-----NRVIVLKDGKIVDDGT 211
Cdd:COG5265 525 LDSRTERAIQAALREVAR--GRTTLVIAH------RLStivdaDEILVLEAGRIVERGT 575
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-216 |
7.96e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.83 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKT----TLLRSLAG--LEKAQGIIKVDNE--IWQDEKEFLPVQKRKIGFVFQD--YALF 89
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYPSGDIRFHGEslLHASEQTLRGVRGNKIAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 90 PNMTVLENLFFV-----NKDKELAN----HLLEITELWELKNRL---PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK15134 107 PLHTLEKQLYEVlslhrGMRREAARgeilNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 158 LDPTmrikLQDEILQLHKEFE----TTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK15134 187 LDVS----VQAQILQLLRELQqelnMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLF 245
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
35-211 |
1.21e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.05 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 35 GLSGSGKTTLLRSLAGLEK-AQGIIKVDN-----EIWQDEKEFLPVQK---------RKIGFVFQ--DYALFPNmTVLEN 97
Cdd:PRK13631 59 GNSGSGKSTLVTHFNGLIKsKYGTIQVGDiyigdKKNNHELITNPYSKkiknfkelrRRVSMVFQfpEYQLFKD-TIEKD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFF--------VNKDKELANHLLEITEL-WELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQD 168
Cdd:PRK13631 138 IMFgpvalgvkKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ 217
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1441214933 169 EILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK13631 218 LILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-233 |
1.43e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 80.26 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG---LEKAQGIIKVDNEIWQD--------------EKEFLPVQKRKiGFV 82
Cdd:PRK13547 19 DLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltGGGAPRGARVTGDVTLNgeplaaidaprlarLRAVLPQAAQP-AFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 83 FQDYAL-----FPNMTVLENLffVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRAL---------MNRPKL 148
Cdd:PRK13547 98 FSAREIvllgrYPHARRAGAL--THRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 149 LLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTSGSAKFSFE 228
Cdd:PRK13547 176 LLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCYGFA 255
|
....*
gi 1441214933 229 GKLLD 233
Cdd:PRK13547 256 VRLVD 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
15-208 |
1.97e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 15 GVMNLD-VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEiwqdekeflPVQKRK--------IGFVFQ 84
Cdd:PRK11288 16 GVKALDdISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDaGSILIDGQ---------EMRFASttaalaagVAIIYQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 85 DYALFPNMTVLENLF---------FVNKdKELANHLLEitELWELKNRL-PN----SLSGGQKQRVSLCRALMNRPKLLL 150
Cdd:PRK11288 87 ELHLVPEMTVAENLYlgqlphkggIVNR-RLLNYEARE--QLEHLGVDIdPDtplkYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 151 MDEPLSAL-----DPTMRIklqdeILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVD 208
Cdd:PRK11288 164 FDEPTSSLsareiEQLFRV-----IRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
31-199 |
2.49e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGL-EKAQGIIKvdneiWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENL-F---FVNKDK 105
Cdd:PRK13539 31 LVLTGPNGSGKTTLLRLIAGLlPPAAGTIK-----LDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLeFwaaFLGGEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 106 ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALM-NRPkLLLMDEPLSALDPTMrIKLQDEILQLHKEFETTTILV 184
Cdd:PRK13539 106 LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALDAAA-VALFAELIRAHLAQGGIVIAA 183
|
170
....*....|....*
gi 1441214933 185 SHDPSEIYklSNRVI 199
Cdd:PRK13539 184 THIPLGLP--GAREL 196
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-210 |
2.75e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 11 HGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIwqdekefLPVQKR----KIGFVFQD 85
Cdd:PRK13536 51 YGDKAVVN-GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdAGKITVLGVP-------VPARARlaraRIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 86 YALFPNMTVLENL-----FFVNKDKELAN---HLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK13536 123 DNLDLEFTVRENLlvfgrYFGMSTREIEAvipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 158 LDPTMRiKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDG 210
Cdd:PRK13536 203 LDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-215 |
3.82e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 10 LHGSNGVMNL-DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDekefLPVQKR---KIGFVFQ 84
Cdd:COG3845 265 VRDDRGVPALkDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAsGSIRLDGEDITG----LSPRERrrlGVAYIPE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 85 D---YALFPNMTVLENL-------------FFVNKDK--ELANHLLEitelwELKNRLPN------SLSGGQKQRVSLCR 140
Cdd:COG3845 341 DrlgRGLVPDMSVAENLilgryrrppfsrgGFLDRKAirAFAEELIE-----EFDVRTPGpdtparSLSGGNQQKVILAR 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 141 ALMNRPKLLLMDEPLSALDP--TMRIklQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVgaIEFI--HQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
31-215 |
5.15e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 5.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIW--QDEKEFLPVQKRKI-----GFVFQDyalfpNMTVLENLFFV-- 101
Cdd:PRK11022 36 VGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFngQDLQRISEKERRNLvgaevAMIFQD-----PMTSLNPCYTVgf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 102 ------------NKD--KELANHLLEITELWELKNRL---PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:PRK11022 111 qimeaikvhqggNKKtrRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 165 KLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK11022 191 QIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-216 |
7.67e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.06 E-value: 7.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLlrslAGL-----EKAQGIIKVDNEIWQDEKefLPVQKRKIGFVFQDYALFpNMTV 94
Cdd:PRK11176 361 NINFKIPAGKTVALVGRSGSGKSTI----ANLltrfyDIDEGEILLDGHDLRDYT--LASLRNQVALVSQNVHLF-NDTI 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFFVNKDK---ELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:PRK11176 434 ANNIAYARTEQysrEQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 161 TMRIKLQDEILQLHKefETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK11176 514 ESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-208 |
8.07e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 79.94 E-value: 8.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKvdneiWQDekeflpvqKRKIGFVFQDYAL-FPN-MTVLE 96
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTVK-----WSE--------NANIGYYAQDHAYdFENdLTLFD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 --NLFFVNKDKELA-----NHLL----EItelwelkNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptMR-I 164
Cdd:PRK15064 404 wmSQWRQEGDDEQAvrgtlGRLLfsqdDI-------KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD--MEsI 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 165 klqdEILQLH-KEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVD 208
Cdd:PRK15064 475 ----ESLNMAlEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-215 |
8.52e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKT-TLLRSLAGLEKAQGIIKVDNEIW------------QDEKEFLPVQKRKIGFVFQD- 85
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLVQCDKMLLrrrsrqvielseQSAAQMRHVRGADMAMIFQEp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 86 -YALFPNMTVLENLF-------FVNKDKEL--ANHLLE---ITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:PRK10261 114 mTSLNPVFTVGEQIAesirlhqGASREEAMveAKRMLDqvrIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIAD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 153 EPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK10261 194 EPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-230 |
1.27e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEiwqdekeflPVQKRKIGFVFQDYALFPNMTVLENL 98
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGtLTPTAGTVLVAGD---------DVEALSARAASRRVASVPQDTSLSFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNKDKELANH-------------------LLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALD 159
Cdd:PRK09536 92 FDVRQVVEMGRTphrsrfdtwtetdraaverAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 160 ptmrIKLQDEILQLHKEF---ETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLlkTSGSAKFSFEGK 230
Cdd:PRK09536 172 ----INHQVRTLELVRRLvddGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL--TADTLRAAFDAR 239
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-187 |
1.47e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 12 GSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDneiwqdekeflpvQKRKIGFVFQDYALFP 90
Cdd:PRK09544 15 GQRRVLS-DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRN-------------GKLRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENLFF-----VNKDKEL-------ANHLLEITElwelknrlpNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSAL 158
Cdd:PRK09544 81 TLPLTVNRFLrlrpgTKKEDILpalkrvqAGHLIDAPM---------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180
....*....|....*....|....*....
gi 1441214933 159 DPTMRIKLQDEILQLHKEFETTTILVSHD 187
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-216 |
1.57e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 79.38 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEiwqdekeflPVQ-------KRKIGFVFQDyalfPn 91
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTeGEIRLDGR---------PLSslshsvlRQGVAMVQQD----P- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 mTVLENLFFVNK------DKELANHLLEITELWELKNRLP-----------NSLSGGQKQRVSLCRALMNRPKLLLMDEP 154
Cdd:PRK10790 425 -VVLADTFLANVtlgrdiSEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 155 LSALDPTMRIKLQdEILQLHKEfETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK10790 504 TANIDSGTEQAIQ-QALAAVRE-HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
20-212 |
2.12e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 76.64 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK---AQGIIKVDNEiwqDEKEfLPVQKRK---IGFVFQDYALFPNMT 93
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyevTSGSILLDGE---DILE-LSPDERAragIFLAFQYPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 V---------------LENLFFVNKDKELANhLLEITElwELKNR-LPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:COG0396 94 VsnflrtalnarrgeeLSAREFLKLLKEKMK-ELGLDE--DFLDRyVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 158 LD-PTMRIkLQDEILQLHKEfETTTILVSHDPsEI--YKLSNRVIVLKDGKIVDDGTA 212
Cdd:COG0396 171 LDiDALRI-VAEGVNKLRSP-DRGILIITHYQ-RIldYIKPDFVHVLVDGRIVKSGGK 225
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-213 |
2.22e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNE-IWQDEKEFLpvqKRKIGFVFQDYALFpNMTVLEN 97
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPTGGQVLLDGVpLVQYDHHYL---HRQVALVGQEPVLF-SGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKDKELAnhllEITELWELKN------RLPNS-----------LSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:TIGR00958 575 IAYGLTDTPDE----EIMAAAKAANahdfimEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 161 TMRIKLQdeilQLHKEFETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAK 213
Cdd:TIGR00958 651 ECEQLLQ----ESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHK 698
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
20-210 |
4.92e-16 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.49 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK---AQGIIKVDNEiwqDEKEfLPVQKRK---IGFVFQDYALFPNMT 93
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyevTEGEILFKGE---DITD-LPPEERArlgIFLAFQYPPEIPGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFFVNKdkelanhlleitelwelknrlpnSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDpTMRIKLQDEILQL 173
Cdd:cd03217 94 NADFLRYVNE-----------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-IDALRLVAEVINK 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1441214933 174 HKEFETTTILVSHDPsEI--YKLSNRVIVLKDGKIVDDG 210
Cdd:cd03217 150 LREEGKSVLIITHYQ-RLldYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-186 |
1.04e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 33 LTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNeiwQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENLFFvnkDKELANHL 111
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEkGEILFER---QSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY---DIHFSPGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 112 LEITEL---WELKNRLP---NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEIlQLHKEFETTTILVS 185
Cdd:PRK13540 106 VGITELcrlFSLEHLIDypcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI-QEHRAKGGAVLLTS 184
|
.
gi 1441214933 186 H 186
Cdd:PRK13540 185 H 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
15-207 |
1.33e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 15 GVMNLD-VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNeiwQDEKEFLPVQKRKIG--FVFQDYALFP 90
Cdd:PRK15439 23 GVEVLKgIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGG---NPCARLTPAKAHQLGiyLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLEN-LFFVNKDKELANHLLEIteLWELKNRLPNSLSGG-----QKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:PRK15439 100 NLSVKENiLFGLPKRQASMQKMKQL--LAALGCQLDLDSSAGslevaDRQIVEILRGLMRDSRILILDEPTASLTPAETE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1441214933 165 KLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:PRK15439 178 RLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-207 |
1.36e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 76.40 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 15 GVMNLD-VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQgiiKVDNEIWQDEKEFLP-----VQKRKIGFVFQDYAL 88
Cdd:TIGR02633 13 GVKALDgIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG---TWDGEIYWSGSPLKAsnirdTERAGIVIIHQELTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 89 FPNMTVLENLFFVNK---------DKEL---ANHLLEITELWELKNRLPNS-LSGGQKQRVSLCRALMNRPKLLLMDEPL 155
Cdd:TIGR02633 90 VPELSVAENIFLGNEitlpggrmaYNAMylrAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 156 SALDPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:TIGR02633 170 SSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-234 |
1.97e-15 |
|
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: 73.98 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 24 DIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGiikVDNEIWQDEKEFLPvQKRKIGFvfqdyalfpNMTVLENLFFVNK 103
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDE---GDIEIELDTVSYKP-QYIKADY---------EGTVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 104 DK--------ELANHLleitELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHK 175
Cdd:cd03237 88 DFythpyfktEIAKPL----QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 176 EFETTTILVSHDPSEIYKLSNRVIVLkDGKIVDDGTAKSVLLKTSGSAKFSfegKLLDI 234
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIVF-EGEPSVNGVANPPQSLRSGMNRFL---KNLDI 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-206 |
1.98e-15 |
|
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: 73.66 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNE-IWQDEKEFLpvqKRKIGFVFQDYALFPNmTVLEN 97
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKpISQYEHKYL---HSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKDKEL---------ANHLLEITEL----WELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:cd03248 108 IAYGLQSCSFecvkeaaqkAHAHSFISELasgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1441214933 165 KLQDEILQLHKefETTTILVSHDPSEIYKlSNRVIVLKDGKI 206
Cdd:cd03248 188 QVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-206 |
2.72e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.47 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGiikvdNEIWQDEKEFL---PVQKRKIGFVF-----QDYALF-- 89
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG-----GRIMLNGKEINalsTAQRLARGLVYlpedrQSSGLYld 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 90 -------PNMTVLENLFFVNKDKELA-----NHLLEITelWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK15439 356 aplawnvCALTHNRRGFWIKPARENAvleryRRALNIK--FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1441214933 158 LDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
20-211 |
5.19e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 72.06 E-value: 5.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSL-AGLEKAQGIIKVDNeiwQDEKEfLPVQK--RKIGFVFQDYALFPNmTVLE 96
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALfRFLEAEEGKIEIDG---IDIST-IPLEDlrSSLTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVNK--DKELANhLLEITELwelknrlPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEIlqlH 174
Cdd:cd03369 101 NLDPFDEysDEEIYG-ALRVSEG-------GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI---R 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1441214933 175 KEFETTTIL-VSHDPSEIYKLsNRVIVLKDGKIVDDGT 211
Cdd:cd03369 170 EEFTNSTILtIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-204 |
5.88e-15 |
|
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: 71.51 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGlEKAQGIIKvdNEIWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENLF 99
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAG-RKTAGVIT--GEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 FvnkdkelanhlleitelwELKNRlpnSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP-----TMRI--KLQDEILq 172
Cdd:cd03232 102 F------------------SALLR---GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSqaaynIVRFlkKLADSGQ- 159
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 173 lhkefettTILVS-HDPSE-IYKLSNRVIVLKDG 204
Cdd:cd03232 160 --------AILCTiHQPSAsIFEKFDRLLLLKRG 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-206 |
6.74e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 8 KELHGSnGVMNldVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEiwqdekeflPVQKRK-------- 78
Cdd:PRK10762 261 DNLSGP-GVND--VSFTLRKGEILGVSGLMGAGRTELMKVLYGaLPRTSGYVTLDGH---------EVVTRSpqdglang 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 79 IGFVFQDY---ALFPNMTVLENL------FFVNKDKELaNHLLE---ITELWELKN-RLPN------SLSGGQKQRVSLC 139
Cdd:PRK10762 329 IVYISEDRkrdGLVLGMSVKENMsltalrYFSRAGGSL-KHADEqqaVSDFIRLFNiKTPSmeqaigLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 140 RALMNRPKLLLMDEPLSALDptmrIKLQDEILQLHKEFET---TTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVD----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
31-201 |
6.86e-15 |
|
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: 71.37 E-value: 6.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENLFFVNKD--KEL 107
Cdd:cd03231 29 LQVTGPNGSGKTTLLRILAGLsPPLAGRVLLNG---GPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADhsDEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 108 ANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQlHKEFETTTILVSHD 187
Cdd:cd03231 106 VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG-HCARGGMVVLTTHQ 184
|
170
....*....|....
gi 1441214933 188 PSEIYKLSNRVIVL 201
Cdd:cd03231 185 DLGLSEAGARELDL 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-216 |
9.32e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.18 E-value: 9.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNeiwQDEKEF-LPVQKRKIGFVFQDYALFPNMTVLENLF 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNG---RPLSDWsAAELARHRAYLSQQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 F----VNKDKELANHLLEITELWELKNRLP---NSLSGGQKQRVSLCRALMN-------RPKLLLMDEPLSALDPTMRIK 165
Cdd:COG4138 92 LhqpaGASSEAVEQLLAQLAEALGLEDKLSrplTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 166 LqdeiLQLHKEFET---TTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:COG4138 172 L----DRLLRELCQqgiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-216 |
1.25e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDN---EIWQdekefLPVQKRKIGFVFQDYALFPNMTVLEN 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGqplEAWS-----AAELARHRAYLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKDK----ELANHLLEITELWELKNRLP---NSLSGGQKQRVSLCRALM-----NRP--KLLLMDEPLSALDPTmr 163
Cdd:PRK03695 90 LTLHQPDKtrteAVASALNEVAEALGLDDKLGrsvNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLDVA-- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 164 iklQDEIL-QLHKEFETTTILV---SHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK03695 168 ---QQAALdRLLSELCQQGIAVvmsSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-159 |
1.46e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.60 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKvdneiWQDEkeflPVqkRKIGFVFQDYALF--------P 90
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLaRPDAGEVL-----WQGE----PI--RRQRDEYHQDLLYlghqpgikT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 91 NMTVLENLFFVNKdkelANHLLEITELWE------LKNR--LP-NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALD 159
Cdd:PRK13538 88 ELTALENLRFYQR----LHGPGDDEALWEalaqvgLAGFedVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
35-186 |
1.54e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.65 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 35 GLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKeflpvQKRKIGFVFQDYALFPNMTVLENLFFVN-----KDKELA 108
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTATRGD-----RSRFMAYLGHLPGLKADLSTLENLHFLCglhgrRAKQMP 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 109 NHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTmRIKLQDEILQLHKEFETTTILVSH 186
Cdd:PRK13543 119 GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE-GITLVNRMISAHLRGGGAALVTTH 195
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-215 |
1.68e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 71.30 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQG--IIKVDNEIWQ-DEKEflpVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:COG4674 28 DLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSgsVLFGGTDLTGlDEHE---IARLGIGRKFQKPTVFEELTVFE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NL--------------FFVNKDKELA--NHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:COG4674 105 NLelalkgdrgvfaslFARLTAEERDriEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 161 TMRIKLQDEILQLHKefETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:COG4674 185 AETERTAELLKSLAG--KHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEV 237
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-216 |
1.97e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 71.36 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 32 ALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEI---WqDEKEFlpvqKRKIGFVFQDYALFPNMTVLENLF-------- 99
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPsEGEILLDAQPlesW-SSKAF----ARKVAYLPQQLPAAEGMTVRELVAigrypwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 ----FVNKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHK 175
Cdd:PRK10575 116 algrFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1441214933 176 EFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK10575 196 ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-211 |
3.68e-14 |
|
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: 72.74 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENLF 99
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLlPPTSGTVLVGG---KDIETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 FV----NKDKELAN----HLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEIL 171
Cdd:TIGR01257 1026 FYaqlkGRSWEEAQlemeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 172 QLHKefETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:TIGR01257 1106 KYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-208 |
4.41e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 15 GVMNL-DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA---QGIIKVDNEiwqdEKEFLPV---QKRKIGFVFQDYA 87
Cdd:NF040905 13 GVKALdDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsyEGEILFDGE----VCRFKDIrdsEALGIVIIHQELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 88 LFPNMTVLENLFFVNK-------DKELANH----LLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:NF040905 89 LIPYLSIAENIFLGNErakrgviDWNETNRrareLLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 157 ALDPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVD 208
Cdd:NF040905 169 ALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-205 |
4.81e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 14 NGVMNLD-VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA---QGIIKVDNEiwqdEKEFLPV---QKRKIGFVFQDY 86
Cdd:PRK13549 16 GGVKALDnVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtyEGEIIFEGE----ELQASNIrdtERAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 87 ALFPNMTVLENLFFVNkdkEL-ANHLLEITELW----ELKNRL-----PNS----LSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:PRK13549 92 ALVKELSVLENIFLGN---EItPGGIMDYDAMYlraqKLLAQLkldinPATpvgnLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 153 EPLSAL-DPTMRIKLqdEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGK 205
Cdd:PRK13549 169 EPTASLtESETAVLL--DIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-234 |
7.00e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 7.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 9 ELHGSNGV--------MNLDvNLDIRSKDFVALTGLSGSGKTTLLRSLAG--------------------LEKAQGIIkv 60
Cdd:PRK10938 3 SLQISQGTfrlsdtktLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGelpllsgerqsqfshitrlsFEQLQKLV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 61 dNEIWQ---------DEKEFlpvqKRKIGFVFQDYAlfpnmtvlenlffvnKDKELANHLLEITELWELKNRLPNSLSGG 131
Cdd:PRK10938 80 -SDEWQrnntdmlspGEDDT----GRTTAEIIQDEV---------------KDPARCEQLAQQFGITALLDRRFKYLSTG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 132 QKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PRK10938 140 ETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGE 218
|
250 260
....*....|....*....|...
gi 1441214933 212 aKSVLLKTSGSAKFSFEGKLLDI 234
Cdd:PRK10938 219 -REEILQQALVAQLAHSEQLEGV 240
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-187 |
7.76e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.30 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 35 GLSGSGKTTLLRSLAGlekaqgiikVDNEIwqdEKEFLPVQKRKIGFVFQDYALFPNMTVLENLFF-VNKDKELANHLLE 113
Cdd:PRK11819 40 GLNGAGKSTLLRIMAG---------VDKEF---EGEARPAPGIKVGYLPQEPQLDPEKTVRENVEEgVAEVKAALDRFNE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 114 ITE---------------------------LWELKN---------RLP------NSLSGGQKQRVSLCRALMNRPKLLLM 151
Cdd:PRK11819 108 IYAayaepdadfdalaaeqgelqeiidaadAWDLDSqleiamdalRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 152 DEPLSALDPtmriklqdEI---LQLH-KEFETTTILVSHD 187
Cdd:PRK11819 188 DEPTNHLDA--------ESvawLEQFlHDYPGTVVAVTHD 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-230 |
1.91e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGiikvdnEIWQDekeflpvqkRKIGFVFQDyALFPNMTVLEN- 97
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSqFEISEG------RVWAE---------RSIAYVPQQ-AWIMNATVRGNi 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFvnkDKELANHLLEITELWELKNRLPN--------------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM- 162
Cdd:PTZ00243 742 LFF---DEEDAARLADAVRVSQLEADLAQlgggleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVg 818
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 163 -RIkLQDEIL-QLHKEfetTTILVSHDpSEIYKLSNRVIVLKDGKIVDDGTAKSvLLKTSGSAKFSFEGK 230
Cdd:PTZ00243 819 eRV-VEECFLgALAGK---TRVLATHQ-VHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELK 882
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-216 |
2.33e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGlEKAQGIIKVDNEIWQD---EKEFLPVQKRKIGFVFQDYALFPNMTVLE 96
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDGFHIGVEGVITYDgitPEEIKKHYRGDVVYNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFFVNK------------DKELANHL---------LEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPL 155
Cdd:TIGR00956 158 TLDFAARcktpqnrpdgvsREEYAKHIadvymatygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 156 SALDPTMRIKLQdEILQLHKEFETTTILVS-HDPSE-IYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:TIGR00956 238 RGLDSATALEFI-RALKTSANILDTTPLVAiYQCSQdAYELFDKVIVLYEGYQIYFGPADKAK 299
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-203 |
2.65e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 82 VFQDYALFpNMTVLENLFFVNKD--KELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKL 148
Cdd:PTZ00265 1301 VSQEPMLF-NMSIYENIKFGKEDatREDVKRACKFAAIDEFIESLPNkydtnvgpygkSLSGGQKQRIAIARALLREPKI 1379
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 149 LLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIyKLSNRVIVLKD 203
Cdd:PTZ00265 1380 LLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNN 1433
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-216 |
6.52e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLA-GLEKAQGIIKVDNeiwQDEKEFLPVQKRK-IGFVFQDYALFpNMTVLEN 97
Cdd:PRK11160 358 GLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNG---QPIADYSEAALRQaISVVSQRVHLF-SATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 LFFVNKDkelAN--HLLEITELWELKNRLPNS-------------LSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP-T 161
Cdd:PRK11160 434 LLLAAPN---ASdeALIEVLQQVGLEKLLEDDkglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeT 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 162 MRiklqdEILQLHKEF--ETTTILVSHDPSEIYKLsNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK11160 511 ER-----QILELLAEHaqNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELL 561
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
96-221 |
8.26e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.45 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFFVNKDKEL--------ANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:NF000106 105 ENLYMIGR*LDLsrkdararADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 168 DEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLKTSG 221
Cdd:NF000106 185 DEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG 237
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-211 |
8.50e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 8.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGlekaqgiikvdnEIWQDEKEFLpVQKRKIGFVFQDYALFpNMTVLENLF 99
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG------------ELSHAETSSV-VIRGSVAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 FVNK----------DKELANHLLEI---TELWELKNRLPNsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:PLN03232 701 FGSDfeserywraiDVTALQHDLDLlpgRDLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1441214933 167 QDEILQlHKEFETTTILVSHDpSEIYKLSNRVIVLKDGKIVDDGT 211
Cdd:PLN03232 780 FDSCMK-DELKGKTRVLVTNQ-LHFLPLMDRIILVSEGMIKEEGT 822
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-206 |
1.02e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKeflPVQKRK-IGFVFQDYALFPNMTVLENL 98
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQsGEILLDGKPVTAEQ---PEDYRKlFSAVFTDFHLFDQLLGPEGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 ffvNKDKELANHLLEITEL---WELK-NRLPN-SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQL 173
Cdd:PRK10522 419 ---PANPALVEKWLERLKMahkLELEdGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPL 495
|
170 180 190
....*....|....*....|....*....|...
gi 1441214933 174 HKEFETTTILVSHDPSeIYKLSNRVIVLKDGKI 206
Cdd:PRK10522 496 LQEMGKTIFAISHDDH-YFIHADRLLEMRNGQL 527
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
21-216 |
1.07e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.13 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVD----NEIwqDEKEFLPVQKRK-----IGFVFQD--YALF 89
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADrmrfDDI--DLLRLSPRERRKlvghnVSMIFQEpqSCLD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 90 PNMTVLENLF--------------FVNKDKELANHLLE---ITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:PRK15093 104 PSERVGRQLMqnipgwtykgrwwqRFGWRKRRAIELLHrvgIKDHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 153 EPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-204 |
1.08e-12 |
|
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: 65.82 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEIwQDEKEFLPVQKRK---IGFVFQDYALFpNMTVL 95
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGeMQTLEGKVHWSNKN-ESEPSFEATRSRNrysVAYAAQKPWLL-NATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFF---VNKDKELAN----------HLLEITELWELKNRLPNsLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTM 162
Cdd:cd03290 97 ENITFgspFNKQRYKAVtdacslqpdiDLLPFGDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1441214933 163 RIKL-QDEILQLHKEFETTTILVSHDPSEIYKlSNRVIVLKDG 204
Cdd:cd03290 176 SDHLmQEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-225 |
1.66e-12 |
|
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: 67.66 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 30 FVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEIwqdekEFLPVQkrkigfvfqdyALFPNMTVLENLFFVNKDKE-L 107
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAeMDKVEGHVHMKGSV-----AYVPQQ-----------AWIQNDSLRENILFGKALNEkY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 108 ANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKE 176
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGV 809
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1441214933 177 FETTT-ILVSHDPSEIYKLsNRVIVLKDGKIVDDGTAKSVLLKTSGSAKF 225
Cdd:TIGR00957 810 LKNKTrILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-211 |
3.29e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG----LEKAQGIIKvdneiwqdekeflpvqkRKIGFVFQDYALFpNMTVL 95
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGelppRSDASVVIR-----------------GTVAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 EN-LFFVNKDKELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMR 163
Cdd:PLN03130 697 DNiLFGSPFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 164 IKLQDEILQlhKEFETTT-ILVShdpSEIYKLS--NRVIVLKDGKIVDDGT 211
Cdd:PLN03130 777 RQVFDKCIK--DELRGKTrVLVT---NQLHFLSqvDRIILVHEGMIKEEGT 822
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-207 |
3.39e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGlekaqgiikvdnEIWQDEKEFLPVQKRKIGFVFQDyalfPNMTVLENLF-FVNKD-KELA 108
Cdd:PRK11147 32 VCLVGRNGAGKSTLMKILNG------------EVLLDDGRIIYEQDLIVARLQQD----PPRNVEGTVYdFVAEGiEEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 109 NHL----------------------------LEITELWELKNRLP--------------NSLSGGQKQRVSLCRALMNRP 146
Cdd:PRK11147 96 EYLkryhdishlvetdpseknlnelaklqeqLDHHNLWQLENRINevlaqlgldpdaalSSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 147 KLLLMDEPLSALDptmrIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIV 207
Cdd:PRK11147 176 DVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
20-231 |
3.96e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEK-AQGIIKVdneIWQDEKEFLpvQKRKIGFVFQ----DYAlFPnmTV 94
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISI---LGQPTRQAL--QKNLVAYVPQseevDWS-FP--VL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LENLFFVN-------------KDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDpt 161
Cdd:PRK15056 97 VEDVVMMGryghmgwlrrakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD-- 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 162 mrIKLQDEILQLHKEF--ETTTILVS-HDPSEIYKLSNRVIVLKdGKIVDDGTAKSVLlkTSGSAKFSFEGKL 231
Cdd:PRK15056 175 --VKTEARIISLLRELrdEGKTMLVStHNLGSVTEFCDYTVMVK-GTVLASGPTETTF--TAENLELAFSGVL 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-209 |
1.16e-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: 64.46 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQgiikVDNEIWQDEKEF---LPVQ--KRKIGFVFQD---YALFPN 91
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGK----FEGNVFINGKPVdirNPAQaiRAGIAMVPEDrkrHGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVLENLFF-----------VNKDKELANHLLEITELwELKNRLPN----SLSGGQKQRVSLCRALMNRPKLLLMDEPLS 156
Cdd:TIGR02633 354 LGVGKNITLsvlksfcfkmrIDAAAELQIIGSAIQRL-KVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 157 ALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDD 209
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
15-209 |
1.31e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 15 GVMNLD-VNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIkvdneIWQDEkeflPV--------QKRKIGFVFQ 84
Cdd:PRK10762 16 GVKALSgAALNVYPGRVMALVGENGAGKSTMMKVLTGIyTRDAGSI-----LYLGK----EVtfngpkssQEAGIGIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 85 DYALFPNMTVLENLF----FVN--------KDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMD 152
Cdd:PRK10762 87 ELNLIPQLTIAENIFlgreFVNrfgridwkKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 153 EPLSALDPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDD 209
Cdd:PRK10762 167 EPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-215 |
1.50e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKT-TLLRSL----AGLEKAQGIIKVDNEiwqdekEFLP--VQKRKIGFVFQD--YALFP 90
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQTAGRVLLDGK------PVAPcaLRGRKIATIMQNprSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 --NMT--VLENLFFVNKDKELANhLLEITELWELKNRL------PNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDP 160
Cdd:PRK10418 95 lhTMHthARETCLALGKPADDAT-LTAALEAVGLENAArvlklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 161 TMRIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSV 215
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-209 |
1.72e-11 |
|
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: 64.05 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEiwqdekeflPVQKRKIG-----F--VFQDYALFPNM 92
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLyRPESGEILLDGQ---------PVTADNREayrqlFsaVFSDFHLFDRL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 93 TVLENLFfvnkDKELANHLL---EITELWELKN-RLPN-SLSGGQKQRVSLCRALM-NRPKLLLmDEPLSALDPTMRIKL 166
Cdd:COG4615 422 LGLDGEA----DPARARELLerlELDHKVSVEDgRFSTtDLSQGQRKRLALLVALLeDRPILVF-DEWAADQDPEFRRVF 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1441214933 167 QDEILQLHKEFETTTILVSHDpsEIY-KLSNRVIVLKDGKIVDD 209
Cdd:COG4615 497 YTELLPELKARGKTVIAISHD--DRYfDLADRVLKMDYGKLVEL 538
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-206 |
1.97e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAqgiiKVDNEIWQDEKEFL---PVQ--KRKIGFVFQD---YALFPN 91
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG----RWEGEIFIDGKPVKirnPQQaiAQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVLENLFFVNKDK----ELANHLLEIT----ELWELKNRLPN------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:PRK13549 356 MGVGKNITLAALDRftggSRIDDAAELKtileSIQRLKVKTASpelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1441214933 158 LDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-208 |
3.86e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 15 GVMNLD-VNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQG-IIKVDNEI-WQDEKEFLpvqKRKIGFVFQDYALFP 90
Cdd:PRK10982 10 GVKALDnVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGsILFQGKEIdFKSSKEAL---ENGISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 91 NMTVLENL---------FFVNKDKELANHLLEITEL---WELKNRLPNsLSGGQKQRVSLCRALMNRPKLLLMDEPLSAL 158
Cdd:PRK10982 87 QRSVMDNMwlgryptkgMFVDQDKMYRDTKAIFDELdidIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1441214933 159 DPTMRIKLQDEILQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVD 208
Cdd:PRK10982 166 TEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-221 |
4.91e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.04 E-value: 4.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNeiWQDEKEFLPVQKRKIGFVFQDYALFPNmTVLENL 98
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRiNESAEGEIIIDG--LNIAKIGLHDLRFKITIIPQDPVLFSG-SLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 --FFVNKDKELANHLlEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMrik 165
Cdd:TIGR00957 1381 dpFSQYSDEEVWWAL-ELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET--- 1456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 166 lqDEILQ--LHKEFETTTIL-VSHDPSEIYKLSnRVIVLKDGKIVDDGtAKSVLLKTSG 221
Cdd:TIGR00957 1457 --DNLIQstIRTQFEDCTVLtIAHRLNTIMDYT-RVIVLDKGEVAEFG-APSNLLQQRG 1511
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-204 |
4.94e-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: 63.11 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 25 IRSKDFVALTGLSGSGKTTLLRSLAG---------LEKAQGIIKVDNEIWQDekeflpvqkrkIGFVFQDYALFPNMTVL 95
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGdttvtsgdaTVAGKSILTNISDVHQN-----------MGYCPQFDAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 ENLFFVNKDKELANHLLEITELWELK--------NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQ 167
Cdd:TIGR01257 2031 EHLYLYARLRGVPAEEIEKVANWSIQslglslyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180 190
....*....|....*....|....*....|....*..
gi 1441214933 168 DEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDG 204
Cdd:TIGR01257 2111 NTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-219 |
6.86e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNEIWQDEKEFLPVQKRkIGFVFQDYA--LFPNMTVLE 96
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQqGRVEVLGGDMADARHRRAVCPR-IAYMPQGLGknLYPTLSVFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NL-FFVNkdkeLANH-----------LLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:NF033858 98 NLdFFGR----LFGQdaaerrrrideLLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 165 KLQDEILQLHKEFETTTILVS---HDPSEIYklsNRVIVLKDGKIVDDGTAKSVLLKT 219
Cdd:NF033858 174 QFWELIDRIRAERPGMSVLVAtayMEEAERF---DWLVAMDAGRVLATGTPAELLART 228
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-204 |
6.89e-11 |
|
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: 61.41 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKvdneiwqdekeflpvQKRKIGFVFQDYALFPNmTVLENL 98
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKIK---------------HSGRISFSSQFSWIMPG-TIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF-VNKDKELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptmrIKL 166
Cdd:cd03291 119 IFgVSYDEYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD----VFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 167 QDEILQ--LHKEFETTTILVSHDPSEIYKLSNRVIVLKDG 204
Cdd:cd03291 195 EKEIFEscVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-159 |
1.04e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.17 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 32 ALTGLSGSGKTTLLRSLAGlEKAQGIIKVDNEIwqdeKEFLPVQK---RKIGFVFQDYALFPNMTVLENLFF-------- 100
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG-RKTGGYIEGDIRI----SGFPKKQEtfaRISGYCEQNDIHSPQVTVRESLIYsaflrlpk 984
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 101 -VNKDKEL--ANHLLEITELWELKNR---LP--NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALD 159
Cdd:PLN03140 985 eVSKEEKMmfVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-206 |
3.24e-10 |
|
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: 59.48 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 8 KELHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDekefLPVQK-RK-IGFVFQD 85
Cdd:cd03289 11 KYTEGGNAVLE-NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNS----VPLQKwRKaFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 86 YALFPNmTVLENL--FFVNKDKELanhlLEITELWELK---NRLPNSL-----------SGGQKQRVSLCRALMNRPKLL 149
Cdd:cd03289 86 VFIFSG-TFRKNLdpYGKWSDEEI----WKVAEEVGLKsviEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 150 LMDEPLSALDPtmrIKLQDEILQLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:cd03289 161 LLDEPSAHLDP---ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-209 |
4.49e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEiwqdekeflPVQKRKI------GFVF------QDyA 87
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRtAGQVYLDGK---------PIDIRSPrdairaGIMLcpedrkAE-G 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 88 LFPNMTVLENL------------FFVNKDKELANHLLEITELwelKNRLPN------SLSGGQKQRVSLCRALMNRPKLL 149
Cdd:PRK11288 342 IIPVHSVADNInisarrhhlragCLINNRWEAENADRFIRSL---NIKTPSreqlimNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 150 LMDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKIVDD 209
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
126-203 |
5.29e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 5.29e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 126 NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFETTTILVSHDPSEIyKLSNRVIVLKD 203
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSN 654
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-226 |
5.98e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 10 LHGsngvmnldVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEFLPVQKRKI-GFVFQDYA 87
Cdd:PLN03130 1255 LHG--------LSFEISPSEKVGIVGRTGAGKSSMLNALFRIvELERGRILIDG---CDISKFGLMDLRKVlGIIPQAPV 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 88 LFPNmTVLENL--FFVNKDKELANHLlEITELWELKNRLPNSL-----------SGGQKQRVSLCRALMNRPKLLLMDEP 154
Cdd:PLN03130 1324 LFSG-TVRFNLdpFNEHNDADLWESL-ERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 155 LSALDPTMRIKLQDEIlqlHKEFETTTILV-SHDPSEIYKlSNRVIVLKDGKIVDDGTAKSvLLKTSGSAkFS 226
Cdd:PLN03130 1402 TAAVDVRTDALIQKTI---REEFKSCTMLIiAHRLNTIID-CDRILVLDAGRVVEFDTPEN-LLSNEGSA-FS 1468
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-225 |
1.33e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.83 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNeiwQDEKEF-LPVQKRKIGFVFQDYALFPNmTVLENL--FFVNKDKE 106
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIvELEKGRIMIDD---CDVAKFgLTDLRRVLSIIPQSPVLFSG-TVRFNIdpFSEHNDAD 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 107 LANhLLEITELWELKNRLP-----------NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptMRIklqDEILQ--L 173
Cdd:PLN03232 1341 LWE-ALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVD--VRT---DSLIQrtI 1414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 174 HKEFETTTILV-SHDPSEIYKlSNRVIVLKDGKIVDDGTAKSvLLKTSGSAKF 225
Cdd:PLN03232 1415 REEFKSCTMLViAHRLNTIID-CDKILVLSSGQVLEYDSPQE-LLSRDTSAFF 1465
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-206 |
1.48e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEIwqdekeflpvqkrKIGFVFQdyalfpnmtvlENLFFVNKDKELAN 109
Cdd:PRK10636 341 IGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGI-------------KLGYFAQ-----------HQLEFLRADESPLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 110 HLLEITELwELKNRLPNSL-----------------SGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILq 172
Cdd:PRK10636 397 HLARLAPQ-ELEQKLRDYLggfgfqgdkvteetrrfSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI- 474
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 173 lhkEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PRK10636 475 ---DFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-221 |
1.73e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLA-GLEKAQGIIKVDNEIWQDEKefLPVQKRKIGFVFQDYALFPNmTVLENL 98
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQrHFDVSEGDIRFHDIPLTKLQ--LDSWRSRLAVVSQTPFLFSD-TVANNI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFVNKDKELAnhllEITELWELKN------RLPNS-----------LSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPt 161
Cdd:PRK10789 410 ALGRPDATQQ----EIEHVARLASvhddilRLPQGydtevgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDG- 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1441214933 162 mriKLQDEILQLHKEF--ETTTILVSHDPSEIYKLSNrVIVLKDGKIVDDGTAKSvLLKTSG 221
Cdd:PRK10789 485 ---RTEHQILHNLRQWgeGRTVIISAHRLSALTEASE-ILVMQHGHIAQRGNHDQ-LAQQSG 541
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
20-189 |
2.23e-09 |
|
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: 57.84 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQG---IIKVDNEIWqdekeFLPvQKRKIGF-VFQDYALFPnMTVL 95
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGgrlTKPAKGKLF-----YVP-QRPYMTLgTLRDQIIYP-DSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 96 EnlfFVNK---DKELA--------NHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMri 164
Cdd:TIGR00954 543 D---MKRRglsDKDLEqildnvqlTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV-- 617
|
170 180
....*....|....*....|....*
gi 1441214933 165 klQDEILQLHKEFETTTILVSHDPS 189
Cdd:TIGR00954 618 --EGYMYRLCREFGITLFSVSHRKS 640
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-159 |
3.13e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 32 ALTGLSGSGKTTLLRSLAGlEKAQGIIKVDNEIwqdeKEFLPVQK---RKIGFVFQDYALFPNMTVLENLFF-------- 100
Cdd:TIGR00956 793 ALMGASGAGKTTLLNVLAE-RVTTGVITGGDRL----VNGRPLDSsfqRSIGYVQQQDLHLPTSTVRESLRFsaylrqpk 867
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 101 -VNKdKELANHLLEITELWELKNR------LPNS-LSGGQKQRVSLCRALMNRPKLLL-MDEPLSALD 159
Cdd:TIGR00956 868 sVSK-SEKMEYVEEVIKLLEMESYadavvgVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLD 934
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-204 |
3.78e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKvdneiwqdekeflpvQKRKIGFVFQDYALFPNmTVLENL 98
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIK---------------HSGRISFSPQTSWIMPG-TIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FF-VNKDKELANHLLEITELWELKNRLPN-----------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptmrIKL 166
Cdd:TIGR01271 508 IFgLSYDEYRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD----VVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1441214933 167 QDEILQ--LHKEFETTTILVSHDPSEIYKLSNRVIVLKDG 204
Cdd:TIGR01271 584 EKEIFEscLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-200 |
3.85e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 25 IRSKDFVALTGLSGSGKTTLLRSLAGLEKAqgiikvdneiwqDEKEFLPVQK--RKIGFVFQDYalfpNMTVLENLFFVN 102
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKP------------DEGEVDPELKisYKPQYIKPDY----DGTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 103 KD-------KELANHLleitELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHK 175
Cdd:PRK13409 426 DDlgssyykSEIIKPL----QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAE 501
|
170 180
....*....|....*....|....*
gi 1441214933 176 EFETTTILVSHDPSEIYKLSNRVIV 200
Cdd:PRK13409 502 EREATALVVDHDIYMIDYISDRLMV 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-200 |
1.05e-08 |
|
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: 55.56 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGLEKAqgiikvdneiwqDEKEFLPVQK--RKIGFVFQDYalfpNMTVLENLFFVNKDK--- 105
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKP------------DEGEVDEDLKisYKPQYISPDY----DGTVEEFLRSANTDDfgs 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 106 -----ELANHLleitELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFETT 180
Cdd:COG1245 433 syyktEIIKPL----GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
170 180
....*....|....*....|
gi 1441214933 181 TILVSHDPSEIYKLSNRVIV 200
Cdd:COG1245 509 AMVVDHDIYLIDYISDRLMV 528
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-206 |
1.23e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.56 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKaqgiiKVDNEIWQDEKEFLPVQ-----KRKIGFVFQ---DYALFPN 91
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDK-----RAGGEIRLNGKDISPRSpldavKKGMAYITEsrrDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 MTVLENLFFVNKDKE--------LANHLLEIT------ELWELK----NRLPNSLSGGQKQRVSLCRALMNRPKLLLMDE 153
Cdd:PRK09700 356 FSIAQNMAISRSLKDggykgamgLFHEVDEQRtaenqrELLALKchsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 154 PLSALDptmrIKLQDEILQLHKEFE---TTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PRK09700 436 PTRGID----VGAKAEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
15-201 |
2.30e-08 |
|
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: 52.57 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 15 GVMNLDVNL-DIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGiikvDNEIWqdekeflpvqkrkigfvfqdyalfPNMT 93
Cdd:cd03222 11 GVFFLLVELgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG----DNDEW------------------------DGIT 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFFVnkdkelanhlleitelwelknrlpnSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQL 173
Cdd:cd03222 63 PVYKPQYI-------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*...
gi 1441214933 174 HKEFETTTILVSHDPSEIYKLSNRVIVL 201
Cdd:cd03222 118 SEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-186 |
9.20e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 35 GLSGSGKTTLLrSLAGLEKAQGIikvDNE-------------IWQdekeflpvQKRKIGFV----FQDYALFPNM-TVLE 96
Cdd:PRK10938 293 GPNGAGKSTLL-SLITGDHPQGY---SNDltlfgrrrgsgetIWD--------IKKHIGYVssslHLDYRVSTSVrNVIL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 97 NLFF---------VNKDKELANHLLEITELWELKNRLP-NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKL 166
Cdd:PRK10938 361 SGFFdsigiyqavSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLV 440
|
170 180
....*....|....*....|
gi 1441214933 167 QDEILQLHKEFETTTILVSH 186
Cdd:PRK10938 441 RRFVDVLISEGETQLLFVSH 460
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-185 |
9.72e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 8 KELHGSNGVMNlDVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQDEKefLPVQKRKIGFVFQDYA 87
Cdd:TIGR01271 1226 KYTEAGRAVLQ-DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVT--LQTWRKAFGVIPQKVF 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 88 LFPNmTVLENL--FFVNKDKELanhlLEITELWELKN---RLPNSL-----------SGGQKQRVSLCRALMNRPKLLLM 151
Cdd:TIGR01271 1303 IFSG-TFRKNLdpYEQWSDEEI----WKVAEEVGLKSvieQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|....
gi 1441214933 152 DEPLSALDPtmrIKLQDEILQLHKEFETTTILVS 185
Cdd:TIGR01271 1378 DEPSAHLDP---VTLQIIRKTLKQSFSNCTVILS 1408
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-206 |
1.16e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGL-EKAQGIIKVDNEIWQDEKEFLPVQKrkiGFVF-----QDYALFPNMT 93
Cdd:PRK10982 266 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIrEKSAGTITLHGKKINNHNANEAINH---GFALvteerRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 94 VLENLFFVNKDKE------LANHLLEITELW---ELKNRLPN------SLSGGQKQRVSLCRALMNRPKLLLMDEPLSAL 158
Cdd:PRK10982 343 IGFNSLISNIRNYknkvglLDNSRMKSDTQWvidSMRVKTPGhrtqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1441214933 159 DPTMRIKLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PRK10982 423 DVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
31-187 |
1.60e-07 |
|
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: 52.24 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIwqdekeflpvqkrKIGFVFQDY-ALFPNMTVLEnlffvnkdkELA 108
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPdSGTIEIGETV-------------KLAYVDQSRdALDPNKTVWE---------EIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 109 NHLLEItelwELKNRLPNS--------------------LSGGQKQRVSLCRALMNRPKLLLMDEPLSALD-PTMRiKLQ 167
Cdd:TIGR03719 409 GGLDII----KLGKREIPSrayvgrfnfkgsdqqkkvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDvETLR-ALE 483
|
170 180
....*....|....*....|
gi 1441214933 168 DEILqlhkEFETTTILVSHD 187
Cdd:TIGR03719 484 EALL----NFAGCAVVISHD 499
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-199 |
1.71e-07 |
|
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: 50.01 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 18 NLDVNLDIRSkdFVALTGLSGSGKTTLLrsLAGLEKAQGIIKVDneiwqdekeFLPvqkrkigfvfqdyALFPNMTVlen 97
Cdd:cd03238 13 NLDVSIPLNV--LVVVTGVSGSGKSTLV--NEGLYASGKARLIS---------FLP-------------KFSRNKLI--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 98 lfFVNKDKELANHLLEITELwelkNRLPNSLSGGQKQRVSLCRALMNRPK--LLLMDEPLSALDPTMRIKLQDEILQLHK 175
Cdd:cd03238 64 --FIDQLQFLIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLID 137
|
170 180
....*....|....*....|....
gi 1441214933 176 EfETTTILVSHDPSEIyKLSNRVI 199
Cdd:cd03238 138 L-GNTVILIEHNLDVL-SSADWII 159
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
21-221 |
1.75e-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: 51.06 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 21 VNLDIRSKDFVALTGLSGSGKTTLlrSLAGLEKA---QGIIKVDN-EIWQdekefLPVQ--KRKIGFVFQDYALFPNMTV 94
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVdifDGKIVIDGiDISK-----LPLHtlRSRLSIILQDPILFSGSIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 95 LenlffvNKDKELA---NHLLEITELWELKN---RLPNSL-----------SGGQKQRVSLCRALMNRPKLLLMDEPLSA 157
Cdd:cd03288 113 F------NLDPECKctdDRLWEALEIAQLKNmvkSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 158 LDPTMRIKLQDEILQLHKefETTTILVSHDPSEIYKlSNRVIVLKDGKIVDDGTAKSVLLKTSG 221
Cdd:cd03288 187 IDMATENILQKVVMTAFA--DRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDG 247
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-206 |
2.61e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 18 NLDVNLDIRSKdfVALTGLSGSGKTTLLRSLAG-LEKAQGII----KVDNEIW-QDEKEFLPVQKRKIGFVFQDYALFPn 91
Cdd:PLN03073 527 NLNFGIDLDSR--IAMVGPNGIGKSTILKLISGeLQPSSGTVfrsaKVRMAVFsQHHVDGLDLSSNPLLYMMRCFPGVP- 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 92 mtvlenlffvnkDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDptmrIKLQDEIL 171
Cdd:PLN03073 604 ------------EQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALI 667
|
170 180 190
....*....|....*....|....*....|....*
gi 1441214933 172 QLHKEFETTTILVSHDPSEIYKLSNRVIVLKDGKI 206
Cdd:PLN03073 668 QGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-201 |
3.58e-07 |
|
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: 50.06 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 26 RSKDFVALTGLSGSGKTTLLRSLAGLEKAQGIIKVDNEIWQD------------------EKEFLPVQKRkigfvfQDYA 87
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEildefrgselqnyftkllEGDVKVIVKP------QYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 88 LFPNM---TVLENLFFVNkDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRI 164
Cdd:cd03236 98 LIPKAvkgKVGELLKKKD-ERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1441214933 165 KLQDEILQLHKEfETTTILVSHDPSEIYKLSNRVIVL 201
Cdd:cd03236 177 NAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
76-163 |
3.96e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 76 KRKIGFVFQDYALFPNMTVLENL------FFVNKDK--ELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPK 147
Cdd:NF033858 338 RRRVGYMSQAFSLYGELTVRQNLelharlFHLPAAEiaARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPE 417
|
90
....*....|....*.
gi 1441214933 148 LLLMDEPLSALDPTMR 163
Cdd:NF033858 418 LLILDEPTSGVDPVAR 433
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-187 |
4.11e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 29 DFVALTGLSGSGKTTLLRSLAGLEKAQ-GIIKVDNeiwqdekeflpvqKRKIGFvFQDY--ALFPNMTVLENL------F 99
Cdd:PRK11147 346 DKIALIGPNGCGKTTLLKLMLGQLQADsGRIHCGT-------------KLEVAY-FDQHraELDPEKTVMDNLaegkqeV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 FVN-KDKELANHLLEIteLWELKN-RLP-NSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDpTMRIKLQDEILQlhkE 176
Cdd:PRK11147 412 MVNgRPRHVLGYLQDF--LFHPKRaMTPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD-VETLELLEELLD---S 485
|
170
....*....|.
gi 1441214933 177 FETTTILVSHD 187
Cdd:PRK11147 486 YQGTVLLVSHD 496
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-191 |
8.45e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.75 E-value: 8.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 27 SKDFVALTGLSGSGKTTLLRSLAGLEKAQGiikvdneiwqdekeflpvqkrkigfvfqdyalfpnmtvlENLFFVNKDKE 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPG---------------------------------------GGVIYIDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 107 LANHLLEITElwELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI-----LQLHKEFETTT 181
Cdd:smart00382 42 LEEVLDQLLL--IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllLLLKSEKNLTV 119
|
170
....*....|
gi 1441214933 182 ILVSHDPSEI 191
Cdd:smart00382 120 ILTTNDEKDL 129
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-218 |
9.13e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 49.04 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAG-LEKAQGIIKVDNEIwqdekeflpvqkrkiGFVFQDYALFPNMTVLENL 98
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGsLSPTVGKVDRNGEV---------------SVIAISAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 99 FFV--------NKDKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEI 170
Cdd:PRK13546 107 EFKmlcmgfkrKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1441214933 171 LQLhKEFETTTILVSHDPSEIYKLSNRVIVLKDGKIVDDGTAKSVLLK 218
Cdd:PRK13546 187 YEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-186 |
3.54e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 33 LTGLSGSGKTTLLRSLA-----GLEKAQGIIKVDNEIWQD--------------------EKEFLPVQKRKIGF--VFQD 85
Cdd:PLN03073 208 LVGRNGTGKTTFLRYMAmhaidGIPKNCQILHVEQEVVGDdttalqcvlntdiertqlleEEAQLVAQQRELEFetETGK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 86 YALFPNMTVLENLffVNKDKELANHLLEITELW-----------------ELKNRLPNSLSGGQKQRVSLCRALMNRPKL 148
Cdd:PLN03073 288 GKGANKDGVDKDA--VSQRLEEIYKRLELIDAYtaearaasilaglsftpEMQVKATKTFSGGWRMRIALARALFIEPDL 365
|
170 180 190
....*....|....*....|....*....|....*...
gi 1441214933 149 LLMDEPLSALDPTMRIKLQDEILQLHKEFetttILVSH 186
Cdd:PLN03073 366 LLLDEPTNHLDLHAVLWLETYLLKWPKTF----IVVSH 399
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
33-216 |
4.52e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 33 LTGLSGSGKTTLLRSLAGleKAQGIIKVDNEIWQDE---KEFLPvqKRKIGFVFQDYALFPNMTVLENLFF------VNK 103
Cdd:PLN03140 196 LLGPPSSGKTTLLLALAG--KLDPSLKVSGEITYNGyrlNEFVP--RKTSAYISQNDVHVGVMTVKETLDFsarcqgVGT 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 104 DKELANHL-----------------------------------------LEITELWELKNRLPNSLSGGQKQRVSLCRAL 142
Cdd:PLN03140 272 RYDLLSELarrekdagifpeaevdlfmkatamegvksslitdytlkilgLDICKDTIVGDEMIRGISGGQKKRVTTGEMI 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1441214933 143 MNRPKLLLMDEPLSALDP--TMRI-KLQDEILQLHKefetTTILVS--HDPSEIYKLSNRVIVLKDGKIVDDGTAKSVL 216
Cdd:PLN03140 352 VGPTKTLFMDEISTGLDSstTYQIvKCLQQIVHLTE----ATVLMSllQPAPETFDLFDDIILLSEGQIVYQGPRDHIL 426
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-191 |
7.79e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 20 DVNLDIRSKDFVALTGLSGSGKTTLLRSLAGLEKAQgiikvDNEIWQDEKEFLPVQKRKIGFVFQDYALFPNMTVLENLF 99
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPS-----SGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 100 FVNK---DKELANHLLEITELWELKNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRiKLQDEILQLHKE 176
Cdd:PRK13541 93 FWSEiynSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLNNLIVMKAN 171
|
170
....*....|....*
gi 1441214933 177 FETTTILVSHDPSEI 191
Cdd:PRK13541 172 SGGIVLLSSHLESSI 186
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
127-187 |
2.65e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 2.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1441214933 127 SLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEIlqlhKEFETTTILVSHD 187
Cdd:PRK10636 149 DFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHD 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
31-187 |
3.69e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 31 VALTGLSGSGKTTLLRSLAGLEKA-QGIIKVDNEIwqdekeflpvqkrKIGFVFQDY-ALFPNMTVLEnlffvnkdkela 108
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPdSGTIKIGETV-------------KLAYVDQSRdALDPNKTVWE------------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 109 nhllEIT---ELWELKNRLPNS--------------------LSGGQKQRVSLCRALMNRPKLLLMDEPLSALD-PTMRi 164
Cdd:PRK11819 408 ----EISgglDIIKVGNREIPSrayvgrfnfkggdqqkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDvETLR- 482
|
170 180
....*....|....*....|...
gi 1441214933 165 KLQDEILqlhkEFETTTILVSHD 187
Cdd:PRK11819 483 ALEEALL----EFPGCAVVISHD 501
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-199 |
5.53e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 18 NL-DVNLDIRSKDFVALTGLSGSGKTTL-------------LRSLA--------GLEKAQgiikVDN------EIWQDEK 69
Cdd:cd03270 10 NLkNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSayarqflgQMDKPD----VDSieglspAIAIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 70 EFLPVQKRKIGFVFQ--DY--ALFPNMTVLENLFFvnkdkelanhLLEITELWELKNRLPNSLSGGQKQRVSLCRAL-MN 144
Cdd:cd03270 86 TTSRNPRSTVGTVTEiyDYlrLLFARVGIRERLGF----------LVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIgSG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1441214933 145 RPKLL-LMDEPLSALDPTMRIKLQdEILQLHKEFETTTILVSHDPsEIYKLSNRVI 199
Cdd:cd03270 156 LTGVLyVLDEPSIGLHPRDNDRLI-ETLKRLRDLGNTVLVVEHDE-DTIRAADHVI 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
128-188 |
3.73e-04 |
|
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: 40.04 E-value: 3.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1441214933 128 LSGGQKQRVSLCRAL----MNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEFeTTTILVSHDP 188
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG-AQVIVITHLP 141
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
2-45 |
6.50e-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: 6.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1441214933 2 IKIEIKKELHGSNGVM---------NL-DVNLDIRSKDFVALTGLSGSGKTTLL 45
Cdd:TIGR00630 598 KKIEVPAERRPGNGKFltlkgarenNLkNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
131-187 |
1.15e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 1.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1441214933 131 GQKQRVSLCRALMNRPKLLLMDEPLSALD-PTMRIkLQDEIlqlhKEFETTTILVSHD 187
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDiNTIRW-LEDVL----NERNSTMIIISHD 211
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
3-45 |
1.93e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.93e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1441214933 3 KIEIKKELHGSNGVM---------NL-DVNLDIRSKDFVALTGLSGSGKTTLL 45
Cdd:PRK00349 600 KIEVPKERRKGNGKFlklkgarenNLkNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
30-49 |
4.03e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.84 E-value: 4.03e-03
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-44 |
4.40e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 4.40e-03
10 20
....*....|....*....|....*....
gi 1441214933 18 NL-DVNLDI-RSKdFVALTGLSGSGKTTL 44
Cdd:COG0178 15 NLkNIDVDIpRNK-LVVITGLSGSGKSSL 42
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
3-44 |
5.56e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.13 E-value: 5.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1441214933 3 KIEIK--KElHgsngvmNL-DVNLDI-RSKdFVALTGLSGSGKTTL 44
Cdd:PRK00349 5 KIIIRgaRE-H------NLkNIDLDIpRDK-LVVFTGLSGSGKSSL 42
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|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
111-187 |
6.06e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 37.84 E-value: 6.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1441214933 111 LLEITELWelkNRLPNSLSGGQKQRVSLCRALMNRPKLLLMDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHD 187
Cdd:COG1245 199 KLGLENIL---DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHD 271
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
31-49 |
6.49e-03 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 36.43 E-value: 6.49e-03
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
33-57 |
9.76e-03 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 36.22 E-value: 9.76e-03
10 20
....*....|....*....|....*
gi 1441214933 33 LTGLSGSGKTTLLRSLAGLEKAQGI 57
Cdd:COG0529 21 FTGLSGSGKSTLANALERRLFERGR 45
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
122-225 |
9.95e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1441214933 122 NRLPNSLSGGQKQRVSLCRALMNRPK--LLLMDEPLSALDPTMRIKLQDEILQLHKEfETTTILVSHDPSEIyKLSNRVI 199
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMI-SLADRII 548
|
90 100 110
....*....|....*....|....*....|...
gi 1441214933 200 VLK------DGKIVDDGTAKSVLLKT-SGSAKF 225
Cdd:PRK00635 549 DIGpgagifGGEVLFNGSPREFLAKSdSLTAKY 581
|
|
|