|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-220 |
9.10e-76 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 231.11 E-value: 9.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYS 82
Cdd:COG1131 1 IEVRGLTKRyGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ENYFNERWTTKQLEKMIAPFY---RKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTS 157
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYglpRKEARERIDELLELFGLTdaADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 158 GLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRY 220
Cdd:COG1131 161 GLDPEARRELWELL-RELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-244 |
7.87e-64 |
|
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: 201.24 E-value: 7.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYS 82
Cdd:COG4555 2 IEVENLSKKyGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ENYFNERWTTKQLEKMIAPFYRKWDHQV---FEFYLEKFDL--PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTS 157
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELkkrIEELIELLGLeeFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 158 GLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQVvsgaiEDLDDELASL 237
Cdd:COG4555 162 GLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE-----ENLEDAFVAL 235
|
....*..
gi 577230680 238 LIYEEHK 244
Cdd:COG4555 236 IGSEEGE 242
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-207 |
7.51e-60 |
|
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: 188.38 E-value: 7.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYS 82
Cdd:cd03230 1 IEVRNLSKRYGKKTaLDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ENYFNERWTtkqlekmiapfyrkwdhqVFEfYLEkfdlpinksiktFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPL 162
Cdd:cd03230 81 EPSLYENLT------------------VRE-NLK------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 577230680 163 ARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:cd03230 130 SRREFWELL-RELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-264 |
1.57e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 158.35 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIelkNRIGFVY 81
Cdd:COG4152 1 MLELKGLTKRFGDKTaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR---RRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 SE-------------NYFNERwttKQLEKMIApfyRKWdhqvFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHH 146
Cdd:COG4152 78 EErglypkmkvgeqlVYLARL---KGLSKAEA---KRR----ADEWLERLGLGdrANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 147 AELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRY-----Q 221
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVI-RELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFgrntlR 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 577230680 222 VVSGAIEDLDDELASLLIYEEHKRTGFIGLTEHA---QVFKEILGH 264
Cdd:COG4152 227 LEADGDAGWLRALPGVTVVEEDGDGAELKLEDGAdaqELLRALLAR 272
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-237 |
2.26e-42 |
|
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: 147.54 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENYFNERWTTKQLEK 97
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 MIAPFY---RKWDHQVFEFYLEKFDL--PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIq 172
Cdd:TIGR01188 89 MMGRLYglpKDEAEERAEELLELFELgeAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI- 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 173 QELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQR-----YQVVSGAIEDLDDELASL 237
Cdd:TIGR01188 168 RALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRlgkdtLESRPRDIQSLKVEVSML 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-216 |
4.73e-42 |
|
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: 144.43 E-value: 4.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYS 82
Cdd:cd03265 1 IEVENLVKKYGDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ENYFNERWTTKQLEKMIAPFY----RKWDHQVFEFyLEKFDL--PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYgvpgAERRERIDEL-LDFVGLleAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 157 SGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-211 |
3.74e-41 |
|
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: 141.59 E-value: 3.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMaLNPIELKNRIGFVYSENYFNERWTTKQLEK 97
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPGFYPNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 MIAPFYRKWD---HQVFEFYLEKFDLpiNKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIqQE 174
Cdd:cd03268 95 LLARLLGIRKkriDEVLDVVGLKDSA--KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELI-LS 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 577230680 175 LIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03268 172 LRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
7.49e-41 |
|
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: 141.32 E-value: 7.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS-SDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIGFV 80
Cdd:COG1122 1 IELENLSFSyPGGTPaLDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 --YSENYF--------------NERWTTKQLEKMIapfyrkwdhqvfEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVA 142
Cdd:COG1122 81 fqNPDDQLfaptveedvafgpeNLGLPREEIRERV------------EEALELVGLEhlADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQ 221
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-206 |
1.16e-40 |
|
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: 140.29 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIGFV 80
Cdd:cd03225 1 ELKNLSFSypdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 --YSENYFNErwTTKQLEKMIAPFYRKWDH----QVFEFYLEKFDLPI--NKSIKTFSTGMKMKLSLAVAFSHHAELYIF 152
Cdd:cd03225 81 fqNPDDQFFG--PTVEEEVAFGLENLGLPEeeieERVEEALELVGLEGlrDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577230680 153 DEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGE 206
Cdd:cd03225 159 DEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-211 |
2.22e-40 |
|
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: 139.81 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENYFNERWTTKQLEK 97
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 MIAPFY---RKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQ 172
Cdd:cd03266 101 YFAGLYglkGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 577230680 173 QeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03266 181 Q-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-216 |
4.28e-40 |
|
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: 139.18 E-value: 4.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFV 80
Cdd:cd03263 1 LQIRNLTktYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YSENYFNERWTTKQLEKMIAPFYRKWDHQVF---EFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEP 155
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKeevELLLRVLGLTdkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 156 TSGLDPLARNELLEIIQQELidENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR--KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-211 |
4.66e-39 |
|
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: 136.26 E-value: 4.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAlnpIELKNRIGFVYSE-------------N 84
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPEErglypkmkvidqlV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 85 YFnerwttKQLEKMIAPFYRKWdhqvFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPL 162
Cdd:cd03269 93 YL------AQLKGLKKEEARRR----IDEWLERLELSeyANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577230680 163 ARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03269 163 NVELLKDVI-RELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-206 |
6.54e-38 |
|
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: 131.60 E-value: 6.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNYSS-DQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGFVys 82
Cdd:cd00267 1 EIENLSFRYgGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAkLPLEELRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 enyfnerwttKQLekmiapfyrkwdhqvfefylekfdlpinksiktfSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPL 162
Cdd:cd00267 79 ----------PQL----------------------------------SGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 577230680 163 ARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGE 206
Cdd:cd00267 115 SRERLLELL-RELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-211 |
2.45e-37 |
|
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: 131.93 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGfVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYS 82
Cdd:cd03264 1 LQLENLTKRyGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ENYFNERWTTKQLEKMIAPFY----RKWDHQVFEFyLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKgipsKEVKARVDEV-LELVNLGdrAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 157 SGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03264 159 AGLDPEERIRFRNLLSE--LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-218 |
2.29e-35 |
|
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: 127.23 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELK---NRIG 78
Cdd:cd03261 1 IELRGLTKSfGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISgLSEAELYrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVY-----------SENY-FNERWTTKQLEKMIApfyrkwdhQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFS 144
Cdd:cd03261 81 MLFqsgalfdsltvFENVaFPLREHTRLSEEEIR--------EIVLEKLEAVGLRgaEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEII---QQELideNKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIrslKKEL---GLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-206 |
4.30e-34 |
|
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: 122.11 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGF 79
Cdd:cd03228 1 IEFKNVSFSypgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VysenyfnerwttkqlekmiapfyrkwdHQvfEFYLekFDLPINKSIktFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:cd03228 81 V---------------------------PQ--DPFL--FSGTIRENI--LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577230680 160 DPLARNELLEIIQQelIDENKTIFMSTHIISDLEKiADYIIHLSDGE 206
Cdd:cd03228 128 DPETEALILEALRA--LAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
1.34e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDmalnPIELKNRIGF 79
Cdd:COG1121 4 MPAIELENLTVSYGGRPvLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 V--YSEnyFNE-------------RWTTKQLEKmiapFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVA 142
Cdd:COG1121 80 VpqRAE--VDWdfpitvrdvvlmgRYGRRGLFR----RPSRADREAVDEALERVGLEdlADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLsDGEVILNGSKEQLLQ 218
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLT 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-218 |
3.35e-33 |
|
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: 121.63 E-value: 3.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNYSsdqFN----LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELK-- 74
Cdd:COG1127 4 PMIEVRNLTKS---FGdrvvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItGLSEKELYel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 -NRIGFVY-------S----ENY-FNERWTTKQLEKMIapfyrkwdHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSL 139
Cdd:COG1127 81 rRRIGMLFqggalfdSltvfENVaFPLREHTDLSEAEI--------RELVLEKLELVGLPgaADKMPSELSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 140 AVAFSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENK-TIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELI-RELRDELGlTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-211 |
1.05e-32 |
|
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: 119.95 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLeedmALNPIELKNRIGFVYSE 83
Cdd:cd03235 1 EVEDLTVSYGGHPvLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF----GKPLEKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 NYFNerW----TTKQLEKM-------IAPFYRKWDHQVFEFYLEK---FDLpINKSIKTFSTGMKMKLSLAVAFSHHAEL 149
Cdd:cd03235 77 RSID--RdfpiSVRDVVLMglyghkgLFRRLSKADKAKVDEALERvglSEL-ADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 150 YIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLsDGEVILNG 211
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-219 |
1.48e-31 |
|
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: 123.79 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIG 78
Cdd:COG2274 473 DIELENVSFRypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSENY------------FNERWTTKQLEK--MIApfyrkwdhQVFEFYLE---KFDLPINKSIKTFSTGMKMKLSLAV 141
Cdd:COG2274 553 VVLQDVFlfsgtirenitlGDPDATDEEIIEaaRLA--------GLHDFIEAlpmGYDTVVGEGGSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 142 AFSHHAELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLeKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRR--LLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-211 |
5.30e-31 |
|
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: 114.45 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGFVys 82
Cdd:cd03214 1 EVENLSVGyGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAsLSPKELARKIAYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 enyfnerwttkqlekmiapfyrkwdHQVfefyLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLD 160
Cdd:cd03214 79 -------------------------PQA----LELLGLAhlADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577230680 161 PLARNELLEIIQQELIDENKTIFMSTHiisDLE---KIADYIIHLSDGEVILNG 211
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLH---DLNlaaRYADRVILLKDGRIVAQG 180
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-221 |
2.63e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 114.41 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV-------LEEDMALNPiELKNRigfvysEN-YFNER 89
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVngrvsalLELGAGFHP-ELTGR------ENiYLNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 ---WTTKQLEKMIApfyrkwdhQVFEFY-LEKF-DLPinksIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLAR 164
Cdd:COG1134 115 llgLSRKEIDEKFD--------EIVEFAeLGDFiDQP----VKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 165 NELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQ 221
Cdd:COG1134 183 KKCLARI-RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYE 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-217 |
3.51e-30 |
|
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: 114.37 E-value: 3.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGFV 80
Cdd:COG1120 1 MLEAENLSVGYGGRPvLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAsLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YSENYFNERWTTKQLekmIA----PFYRKW------DHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAE 148
Cdd:COG1120 81 PQEPPAPFGLTVREL---VAlgryPHLGLFgrpsaeDREAVEEALERTGLEhlADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 149 LYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLE---KIADYIIHLSDGEVILNGSKEQLL 217
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH---DLNlaaRYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
18-204 |
2.41e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 110.65 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENYFNERWTTKQLEK 97
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVRENLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 MIAPFY-RKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQE 174
Cdd:COG4133 98 FWAALYgLRADREAIDEALEAVGLAglADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAH 177
|
170 180 190
....*....|....*....|....*....|
gi 577230680 175 LiDENKTIFMSTHIisDLEKIADYIIHLSD 204
Cdd:COG4133 178 L-ARGGAVLLTTHQ--PLELAAARVLDLGD 204
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-211 |
5.29e-29 |
|
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: 110.88 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENyfNERWttkqlek 97
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQK--TQLW------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 miapfyrkWDHQVFE-FYLEK--FDLP--------------------INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDE 154
Cdd:cd03267 108 --------WDLPVIDsFYLLAaiYDLPparfkkrldelselldleelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 155 PTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-206 |
7.58e-28 |
|
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: 106.12 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA---LNPIELKNRIGF 79
Cdd:cd03229 1 LELKNVSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSenyfnerwttkqlekmiapfyrkwDHQVFeFYLEKFD---LPInksiktfSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:cd03229 81 VFQ------------------------DFALF-PHLTVLEniaLGL-------SGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577230680 157 SGLDPLARNELLEIIQQeLIDE-NKTIFMSTHIISDLEKIADYIIHLSDGE 206
Cdd:cd03229 129 SALDPITRREVRALLKS-LQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-219 |
8.82e-28 |
|
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: 107.77 E-value: 8.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEED-MALNPIELKNRIGFV 80
Cdd:cd03295 1 IEFENVTkrYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YSENYFNERWTtkqLEKMIA--PFYRKW-----DHQVFEFyLEKFDLPINKSIKTF----STGMKMKLSLAVAFSHHAEL 149
Cdd:cd03295 81 IQQIGLFPHMT---VEENIAlvPKLLKWpkekiRERADEL-LALVGLDPAEFADRYphelSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 150 YIFDEPTSGLDPLARNELLEI---IQQELideNKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEfkrLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-208 |
9.23e-28 |
|
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: 107.21 E-value: 9.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFN---LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELK---- 74
Cdd:cd03257 2 LEVKNLSvsFPTGGGSvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYSENY--FNERWTT-KQLEKMIAPFYRKWDHQ----VFEFYLEKFDLP---INKSIKTFSTGMKMKLSLAVAFS 144
Cdd:cd03257 82 KEIQMVFQDPMssLNPRMTIgEQIAEPLRIHGKLSKKEarkeAVLLLLVGVGLPeevLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIqQELIDE-NKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLL-KKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
18-219 |
1.07e-27 |
|
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: 111.92 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKN---RIGFVY--SENYFNERWT 91
Cdd:COG1123 281 VDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTkLSRRSLRElrrRVQMVFqdPYSSLNPRMT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 92 tkqLEKMIA-PF-------YRKWDHQVFEfYLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLD 160
Cdd:COG1123 361 ---VGDIIAePLrlhgllsRAERRERVAE-LLERVGLPpdlADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 161 PLARNELLEII---QQELideNKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:COG1123 437 VSVQAQILNLLrdlQREL---GLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-157 |
1.08e-27 |
|
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: 104.65 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIE-LKNRIGFVYSENYFNERWTTKQ-- 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVREnl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 -LEKMIAPFYRKWDHQVFEFYLEKFDL------PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTS 157
Cdd:pfam00005 81 rLGLLLKGLSKREKDARAEEALEKLGLgdladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-217 |
2.17e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.76 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIG--- 78
Cdd:PRK13536 41 AIDLAGVSKSyGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGvvp 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 --------FVYSEN------YFneRWTTKQLEKMIAPfyrkwdhqVFEFylEKFDLPINKSIKTFSTGMKMKLSLAVAFS 144
Cdd:PRK13536 121 qfdnldleFTVRENllvfgrYF--GMSTREIEAVIPS--------LLEF--ARLESKADARVSDLSGGMKRRLTLARALI 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRS-LLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-219 |
2.40e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.41 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVN--YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGF 79
Cdd:COG1132 339 EIEFENVSfsYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdLTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 V------YS----EN--YFNERWTTKQLEK-----MIAPFYRKWDhqvfefylEKFDLPINKSIKTFSTGMKMKLSLAVA 142
Cdd:COG1132 419 VpqdtflFSgtirENirYGRPDATDEEVEEaakaaQAHEFIEALP--------DGYDTVVGERGVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 143 FSHHAELYIFDEPTSGLDPlaRNELLeiIQQEL--IDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:COG1132 491 LLKDPPILILDEATSALDT--ETEAL--IQEALerLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-208 |
3.12e-27 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 105.03 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 8 NVNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPIELKNRIGFV------- 80
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSG--SILLNGKPIKAKERRKSIGYVmqdvdyq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 -YSENYFNE-RWTTKQLEKmiapfyrkwDHQVFEFYLEKFDLPINKSI--KTFSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:cd03226 84 lFTDSVREElLLGLKELDA---------GNEQAETVLKDLDLYALKERhpLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 157 SGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:cd03226 155 SGLDYKNMERVGELI-RELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-217 |
4.65e-27 |
|
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: 105.94 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIM-DLYQPQTGVIRVLEEDM-ALNPIELKNRI 77
Cdd:COG1119 1 DPLLELRNVTVRrGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRLFGERRgGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 78 GFVYSE--NYFNERWTtkqLEKMIA----------PFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAF 143
Cdd:COG1119 81 GLVSPAlqLRFPRDET---VLDVVLsgffdsiglyREPTDEQRERARELLELLGLAhlADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 144 SHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLEKIADYIIH---LSDGEVILNGSKEQLL 217
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH---HVEEIPPGITHvllLKDGRVVAAGPKEEVL 231
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-282 |
7.16e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.10 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFV----------------- 80
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfgqrsqlwwdlpaidsf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 ------Y--SENYFNERwttkqLEKMIapfyrkwdhQVFEfyLEKFdlpINKSIKTFSTGMKMKLSLAVAFSHHAELYIF 152
Cdd:COG4586 118 rllkaiYriPDAEYKKR-----LDELV---------ELLD--LGEL---LDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 153 DEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQ-------VVSG 225
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGpyktivlELAE 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 226 AIEDLD-DELASLLIYEEHK-RTGFIGLTEHAQVFKEILGHK----VNITTPSIENLM--VYLEK 282
Cdd:COG4586 259 PVPPLElPRGGEVIEREGNRvRLEVDPRESLAEVLARLLARYpvrdLTIEEPPIEEVIrrIYKEG 323
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-219 |
1.16e-26 |
|
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: 109.08 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSDQ--FNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGF 79
Cdd:COG4988 336 SIELEDVSFSYPGgrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYF------------NERWTTKQLEKMIApfyrkwDHQVFEF--YLEK-FDLPINKSIKTFSTGMKMKLSLAVAFS 144
Cdd:COG4988 416 VPQNPYLfagtirenlrlgRPDASDEELEAALE------AAGLDEFvaALPDgLDTPLGEGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLeKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRR--LAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
15-212 |
2.36e-26 |
|
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: 103.25 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 15 QFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNpiELKNrIGFVYSENYFNERWTTKQ 94
Cdd:TIGR03740 13 QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRK--DLHK-IGSLIESPPLYENLTARE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 LEKMIAPFYRKWDHQVFEFyLEKFDLPIN--KSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQ 172
Cdd:TIGR03740 90 NLKVHTTLLGLPDSRIDEV-LNIVDLTNTgkKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQELRELIR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 577230680 173 QeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGS 212
Cdd:TIGR03740 169 S-FPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
5.97e-26 |
|
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: 106.91 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQ---TGVIRVLEEDM-ALNPIELKN 75
Cdd:COG1123 4 LLEVRDLSVRypgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 RIGFVYSE--NYFN----ERWTTKQLEKMIAPfyRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHA 147
Cdd:COG1123 84 RIGMVFQDpmTQLNpvtvGDQIAEALENLGLS--RAEARARVLELLEAVGLErrLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 148 ELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQ 221
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-211 |
6.21e-26 |
|
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: 102.23 E-value: 6.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV-------LEEDMALNPiELKNRigfvysEN-YFNER 89
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvsslLGLGGGFNP-ELTGR------ENiYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 W---TTKQLEKMIapfyrkwdHQVFEFY-LEKFdlpINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARN 165
Cdd:cd03220 111 LlglSRKEIDEKI--------DEIIEFSeLGDF---IDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 577230680 166 ELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03220 180 KCQRRL-RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-221 |
1.02e-25 |
|
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: 102.91 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNY-----SSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA----LNPIEL 73
Cdd:TIGR04521 1 IKLKNVSYiyqpgTPFEKKaLDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 74 KNRIGFV--YSENyfnerwttkQL-----EKMIA--PFYRKWDHQ-----VFEfYLEKFDLP---INKSIKTFSTGMKMK 136
Cdd:TIGR04521 81 RKKVGLVfqFPEH---------QLfeetvYKDIAfgPKNLGLSEEeaeerVKE-ALELVGLDeeyLERSPFELSGGQMRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 137 LSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:TIGR04521 151 VAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
....*
gi 577230680 217 LQRYQ 221
Cdd:TIGR04521 231 FSDVD 235
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-207 |
1.20e-25 |
|
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: 101.41 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFN---LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIEL---- 73
Cdd:cd03255 1 IELKNLSktYGGGGEKvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 74 KNRIGFVYSENYFNERWTTKQ---LEKMIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAE 148
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALEnveLPLLLAGVPKKERRERAEELLERVGLGdrLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 149 LYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIIsDLEKIADYIIHLSDGEV 207
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-219 |
2.68e-25 |
|
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: 100.76 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN--LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIGFV 80
Cdd:cd03254 3 IEFENVNFSYDEKKpvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YSENY-FNE---------RWTTKQlEKMIAPFYRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:cd03254 83 LQDTFlFSGtimenirlgRPNATD-EEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 151 IFDEPTSGLDPlarnELLEIIQQ--ELIDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:cd03254 162 ILDEATSNIDT----ETEKLIQEalEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-262 |
3.38e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.19 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIG--- 78
Cdd:PRK13537 7 PIDFRNVEKRyGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 --------FVYSEN------YFNerWTTKQLEKMIAPfyrkwdhqVFEFylEKFDLPINKSIKTFSTGMKMKLSLAVAFS 144
Cdd:PRK13537 87 qfdnldpdFTVRENllvfgrYFG--LSAAAARALVPP--------LLEF--AKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRyQVVS 224
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRS-LLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES-EIGC 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 577230680 225 GAIEDLDDELASLliyeehkRTGFIGLTEHAQVFKEIL 262
Cdd:PRK13537 233 DVIEIYGPDPVAL-------RDELAPLAERTEISGETL 263
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-208 |
7.69e-25 |
|
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: 97.50 E-value: 7.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIE-LKNRIGFVYsenyfnerwttkQL 95
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDaRRAGIAMVY------------QL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 96 ekmiapfyrkwdhqvfefylekfdlpinksiktfSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeL 175
Cdd:cd03216 84 ----------------------------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRR-L 128
|
170 180 190
....*....|....*....|....*....|...
gi 577230680 176 IDENKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:cd03216 129 RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-216 |
9.28e-25 |
|
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: 99.18 E-value: 9.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLI---MDLY--QPQTGVIRVLEED---MALNPIELK 74
Cdd:cd03260 1 IELRDLNVYYGDKHaLKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlNDLIpgAPDEGEVLLDGKDiydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYSE-NYFNerwttKQLEKMIA---PFYRKWDHQVF----EFYLEKFDLPINKSIKT----FSTGMKMKLSLAVA 142
Cdd:cd03260 81 RRVGMVFQKpNPFP-----GSIYDNVAyglRLHGIKLKEELdervEEALRKAALWDEVKDRLhalgLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAE--LKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-216 |
1.57e-24 |
|
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: 98.79 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNV--NYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKN---RI 77
Cdd:cd03256 1 IEVENLskTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 78 GFVYS-----------ENYFNERWTTKQLEKMIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFS 144
Cdd:cd03256 81 GMIFQqfnlierlsvlENVLSGRLGRRSTWRSLFGLFPKEEKQRALAALERVGLLdkAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-211 |
9.70e-24 |
|
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: 96.12 E-value: 9.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIG 78
Cdd:cd03245 2 RIEFRNVSFSypnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSE------------NYFNERWTTKQLEKM-----IAPFYRKWDHqvfefyleKFDLPINKSIKTFSTGMKMKLSLAV 141
Cdd:cd03245 82 YVPQDvtlfygtlrdniTLGAPLADDERILRAaelagVTDFVNKHPN--------GLDLQIGERGRGLSGGQRQAVALAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 142 AFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDenKTIFMSTHIISDLEkIADYIIHLSDGEVILNG 211
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-211 |
1.30e-23 |
|
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: 94.69 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFV 80
Cdd:cd03247 1 LSINNVSFSypeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YSENYFnerwttkqlekmiapfyrkwdhqvfefylekFDLPINKSI-KTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:cd03247 81 NQRPYL-------------------------------FDTTLRNNLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 160 DPLARNELLEIIQQELidENKTIFMSTHIISDLEKiADYIIHLSDGEVILNG 211
Cdd:cd03247 130 DPITERQLLSLIFEVL--KDKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-216 |
3.31e-23 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 95.51 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVN--YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKN---R 76
Cdd:COG3638 2 MLELRNLSkrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtALRGRALRRlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 IGFVYSEnyFN----------------ERWTTkqLEKMIAPFYRKWDHQVFEfYLEKFDLP--INKSIKTFSTGMKMKLS 138
Cdd:COG3638 82 IGMIFQQ--FNlvprlsvltnvlagrlGRTST--WRSLLGLFPPEDRERALE-ALERVGLAdkAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 139 LAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLE---KIADYIIHLSDGEVILNGSKEQ 215
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLH---QVDlarRYADRIIGLRDGRVVFDGPPAE 233
|
.
gi 577230680 216 L 216
Cdd:COG3638 234 L 234
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-219 |
5.06e-23 |
|
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: 98.68 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIG 78
Cdd:COG4987 333 SLELEDVSFRypgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSENY-FNerwTT-----------------------KQLEKMIAPFYRKWDHQVFEfylekfdlpinkSIKTFSTGMK 134
Cdd:COG4987 413 VVPQRPHlFD---TTlrenlrlarpdatdeelwaalerVGLGDWLAALPDGLDTWLGE------------GGRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 135 MKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELidENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKE 214
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL--AGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHE 554
|
....*
gi 577230680 215 QLLQR 219
Cdd:COG4987 555 ELLAQ 559
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-207 |
1.52e-22 |
|
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: 92.98 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN-YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKN---RIGF 79
Cdd:cd03262 1 IEIKNLHkSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VY-SENYFNERWTTKQLekMIAPFY-RKWD-HQVFEF---YLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYI 151
Cdd:cd03262 81 VFqQFNLFPHLTVLENI--TLAPIKvKGMSkAEAEERaleLLEKVGLAdkADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 152 FDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-211 |
1.80e-22 |
|
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: 92.58 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNV--NYSSDQFnLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNrIGFVY 81
Cdd:cd03259 1 LELKGLskTYGSVRA-LDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-IGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 sENYFNerWTTKQLEKMIA-PFYRK------WDHQVFEfYLEKFDLPI--NKSIKTFSTGMKMKLSLAVAFSHHAELYIF 152
Cdd:cd03259 79 -QDYAL--FPHLTVAENIAfGLKLRgvpkaeIRARVRE-LLELVGLEGllNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 153 DEPTSGLDPLARNELLEIIqQELIDENK-TIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03259 155 DEPLSALDAKLREELREEL-KELQRELGiTTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-217 |
4.50e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.13 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIG 78
Cdd:PRK13632 7 MIKVENVSFSypnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYS--ENYF--------------NERWTTKQLEKMIAPFYRKWDhqvFEFYLEKfdLPINksiktFSTGMKMKLSLAVA 142
Cdd:PRK13632 87 IIFQnpDNQFigatveddiafgleNKKVPPKKMKDIIDDLAKKVG---MEDYLDK--EPQN-----LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLEKI--ADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITH---DMDEAilADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-219 |
6.07e-22 |
|
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: 91.78 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL-NPIELKNRIGFVYSENYFNERW------ 90
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFNRSirdnia 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 91 ---TTKQLEKMIAPFYRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDplarNEL 167
Cdd:cd03252 98 ladPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD----YES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577230680 168 LEIIQQEL--IDENKTIFMSTHIISDLeKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:cd03252 174 EHAIMRNMhdICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-219 |
1.58e-21 |
|
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: 90.75 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNV--NYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA---LNpiELKNRI 77
Cdd:cd03251 1 VEFKNVtfRYPGDGPPvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdytLA--SLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 78 GFVYSENY-FNErwttkQLEKMIApfYRKWD---------------HQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAV 141
Cdd:cd03251 79 GLVSQDVFlFND-----TVAENIA--YGRPGatreeveeaaraanaHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 142 AFSHHAELYIFDEPTSGLDplarNELLEIIQQEL--IDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:cd03251 152 ALLKDPPILILDEATSALD----TESERLVQAALerLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-212 |
3.57e-21 |
|
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: 93.92 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 20 NISFKVPQgfVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENYFNERWTTKqlEKMI 99
Cdd:TIGR01257 950 NITFYENQ--ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVA--EHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 100 apFY-----RKWDHQVFEF--YLEKFDL--PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEI 170
Cdd:TIGR01257 1026 --FYaqlkgRSWEEAQLEMeaMLEDTGLhhKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577230680 171 IQQelIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGS 212
Cdd:TIGR01257 1104 LLK--YRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
6.48e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.81 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVN--YSSDQ-FNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNP---IELKN 75
Cdd:PRK13648 6 SIIVFKNVSfqYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAITDdnfEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 RIGFVYS--ENYFNERwTTK-----QLEKMIAPfYRKWDHQVFEfYLEKFDL--PINKSIKTFSTGMKMKLSLAVAFSHH 146
Cdd:PRK13648 84 HIGIVFQnpDNQFVGS-IVKydvafGLENHAVP-YDEMHRRVSE-ALKQVDMleRADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 147 AELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-218 |
9.36e-21 |
|
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: 88.26 E-value: 9.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFnLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVY 81
Cdd:cd03224 1 LEVENLNagYGKSQI-LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 S-------------EN-----YFNERWTTK-QLEKMIAPF---YRKWDHQVfefylekfdlpinksiKTFSTGMKMKLSL 139
Cdd:cd03224 80 VpegrrifpeltveENlllgaYARRRAKRKaRLERVYELFprlKERRKQLA----------------GTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 140 AVAFSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGLAPKIVEEIFEAI-RELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-221 |
1.01e-20 |
|
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: 88.41 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFN---LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKN-- 75
Cdd:cd03258 2 IELKNVSkvFGDTGGKvtaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 -RIGFVYseNYFNERWTTKQLEKMIAPF------YRKWDHQVFEFyLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHH 146
Cdd:cd03258 82 rRIGMIF--QHFNLLSSRTVFENVALPLeiagvpKAEIEERVLEL-LELVGLEdkADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 147 AELYIFDEPTSGLDPLARNELLEI---IQQELideNKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQ 221
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALlrdINREL---GLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
8-216 |
4.68e-20 |
|
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: 86.97 E-value: 4.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 8 NVNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA------LNpiELKNRIGFVY 81
Cdd:TIGR02315 8 SKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITklrgkkLR--KLRRRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 S-----------ENYFNERWTTKQLEKMIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAE 148
Cdd:TIGR02315 86 QhynlierltvlENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLAdkAYQRADQLSGGQQQRVAIARALAQQPD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 149 LYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:TIGR02315 166 LILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-219 |
6.09e-20 |
|
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: 86.52 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIE-LKNRIGFV 80
Cdd:cd03253 1 IEFENVTfaYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDsLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 ------------YSENYFNERWTTKQLEK---------MIAPFYRKWDHQVFEFYLEkfdlpinksiktFSTGMKMKLSL 139
Cdd:cd03253 81 pqdtvlfndtigYNIRYGRPDATDEEVIEaakaaqihdKIMRFPDGYDTIVGERGLK------------LSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 140 AVAFSHHAELYIFDEPTSGLDPLARNElleiIQQELID--ENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLL 217
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTERE----IQAALRDvsKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
..
gi 577230680 218 QR 219
Cdd:cd03253 224 AK 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-239 |
7.12e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL-NPIE-LKNRIGFVY-----------SEN 84
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrSPRDaQAAGIAIIHqelnlvpnlsvAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 85 YFNERWTTKqlekmiAPFYRkWD--HQVFEFYLEKFDLPIN--KSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLD 160
Cdd:COG1129 100 IFLGREPRR------GGLID-WRamRRRARELLARLGLDIDpdTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 161 PLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVilngskeqllqryqVVSGAIEDLD-DELASLLI 239
Cdd:COG1129 173 EREVERLFRII-RRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL--------------VGTGPVAELTeDELVRLMV 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
18-215 |
2.28e-19 |
|
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: 84.80 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYS-------------EN 84
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTfqiprlfpeltvlEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 85 -----------YFNERWTTKQLEKMIApfyrkwdhQVFEfYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYI 151
Cdd:cd03219 96 vmvaaqartgsGLLLARARREEREARE--------RAEE-LLERVGLAdlADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 152 FDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQ 215
Cdd:cd03219 167 LDEPAAGLNPEETEELAELI-RELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-217 |
2.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN--LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDM-ALNPIEL---KNRI 77
Cdd:PRK13644 2 IRLENVSYSYPDGTpaLENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKG--KVLVSGIdTGDFSKLqgiRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 78 GFVYS--ENYFNERWTTKQL----EKMIAP---FYRKWDHQVFEFYLEKFDlpiNKSIKTFSTGMKMKLSLAVAFSHHAE 148
Cdd:PRK13644 80 GIVFQnpETQFVGRTVEEDLafgpENLCLPpieIRKRVDRALAEIGLEKYR---HRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 149 LYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEkIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVL 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-208 |
3.26e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.95 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFNLKNISFKVPQG-FVtgFI-GRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAlnpiELKN---- 75
Cdd:COG2884 2 IRFENVSkrYPGGREALSDVSLEIEKGeFV--FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS----RLKRreip 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 ----RIGFVYSENYFNERWTTKQ-----LEkmIAPFYRK-WDHQVFEfYLEKFDLP--INKSIKTFSTGMKMKLSLAVAF 143
Cdd:COG2884 76 ylrrRIGVVFQDFRLLPDRTVYEnvalpLR--VTGKSRKeIRRRVRE-VLDLVGLSdkAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 144 SHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHiisDLEKIADY---IIHLSDGEVI 208
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELL-EEINRRGTTVLIATH---DLELVDRMpkrVLELEDGRLV 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-217 |
3.77e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 84.28 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKN---RIGF 79
Cdd:COG1126 2 IEIENLHKSFGDLEvLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrrKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VY-SENYFNERwTTkqLEK-MIAPFY-RKWD----HQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:COG1126 82 VFqQFNLFPHL-TV--LENvTLAPIKvKKMSkaeaEERAMELLERVGLAdkADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 151 IFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVM-RDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFF 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
18-187 |
5.54e-19 |
|
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: 82.86 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNP---IELKNRIGFVYSEnyfnerwTTKQ 94
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkglLERRQRVGLVFQD-------PDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 LekmiapFYRKWD-----------------HQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEP 155
Cdd:TIGR01166 81 L------FAADVDqdvafgplnlglseaevERRVREALTAVGASglRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 577230680 156 TSGLDPLARNELLEIIQQeLIDENKTIFMSTH 187
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRR-LRAEGMTVVISTH 185
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
5.83e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVN--YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVL-EEDMALNPIELKNRIG 78
Cdd:PRK13647 3 NIIEVEDLHfrYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSE---NYF-------------NERWTTKQLEKMIAPFYRKWDHQVFEfylekfdlpiNKSIKTFSTGMKMKLSLAVA 142
Cdd:PRK13647 83 LVFQDpddQVFsstvwddvafgpvNMGLDKDEVERRVEEALKAVRMWDFR----------DKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEqLLQRYQV 222
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDEDI 230
|
....
gi 577230680 223 VSGA 226
Cdd:PRK13647 231 VEQA 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-222 |
8.02e-19 |
|
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: 82.90 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFN---LKNISFKVPQG-FVTgFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAlnpiELKNRI 77
Cdd:cd03293 1 LEVRNVSktYGGGGGAvtaLEDISLSVEEGeFVA-LVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 78 GFVYSENY-FNerWTTKQ------LEkmIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAE 148
Cdd:cd03293 76 GYVFQQDAlLP--WLTVLdnvalgLE--LQGVPKAEARERAEELLELVGLSgfENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 149 LYIFDEPTSGLDPLARNELleiiQQELID----ENKTIFMSTHiisDLEKiAdyiIHLSDGEVILNGSKEQLLQRYQV 222
Cdd:cd03293 152 VLLLDEPFSALDALTREQL----QEELLDiwreTGKTVLLVTH---DIDE-A---VFLADRVVVLSARPGRIVAEVEV 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-187 |
1.17e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.95 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 20 NISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGF------VYSEnyfnerWTTK 93
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYmsqafsLYGE------LTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 94 Q-LEkMIAPFYR----KWDHQVFEFyLEKFDL-----------PInksiktfstGMKMKLSLAVAFSHHAELYIFDEPTS 157
Cdd:NF033858 358 QnLE-LHARLFHlpaaEIAARVAEM-LERFDLadvadalpdslPL---------GIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190
....*....|....*....|....*....|....
gi 577230680 158 GLDPLARNELLEIiqqeLID----ENKTIFMSTH 187
Cdd:NF033858 427 GVDPVARDMFWRL----LIElsreDGVTIFISTH 456
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-223 |
1.29e-18 |
|
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: 82.72 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGF 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHvLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYS-------------ENyfnerwttkqLEkmIAPFYRKWD---HQVFEFYLEKFdlPINKSIK-----TFSTG---Mkm 135
Cdd:COG0410 81 GYVpegrrifpsltveEN----------LL--LGAYARRDRaevRADLERVYELF--PRLKERRrqragTLSGGeqqM-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 136 kLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQ 215
Cdd:COG0410 145 -LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEII-RRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAE 222
|
....*...
gi 577230680 216 LLQRYQVV 223
Cdd:COG0410 223 LLADPEVR 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-211 |
2.04e-18 |
|
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: 81.06 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-------LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDL--YQPQTGVIRVleEDMALNPIELK 74
Cdd:cd03213 4 LSFRNLTVTVKSSPsksgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLI--NGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYSENYFNERWTtkqlekmiapfyrkwdhqVFEFylekfdLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDE 154
Cdd:cd03213 82 KIIGYVPQDDILHPTLT------------------VRET------LMFAAKLRGLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 155 PTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIIS-DLEKIADYIIHLSDGEVILNG 211
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRR-LADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-206 |
4.06e-18 |
|
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: 79.03 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEedmalnpielKNRIGfvys 82
Cdd:cd03221 1 IELENLSKTyGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 enyfnerwttkqlekmiapfyrkwdhqvfefYLEKFdlpinksiktfSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPL 162
Cdd:cd03221 67 -------------------------------YFEQL-----------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLE 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 577230680 163 ARnellEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGE 206
Cdd:cd03221 105 SI----EALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-219 |
4.21e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.16 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQT---GVIRVLEEDMALNPI-ELK 74
Cdd:PRK13640 4 NIVEFKHVSFTypdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVwDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYsENYFNErWTTKQLEKMIApfyrkwdhqvfeFYLEKFDLPINKSIK--------------------TFSTGMK 134
Cdd:PRK13640 84 EKVGIVF-QNPDNQ-FVGATVGDDVA------------FGLENRAVPRPEMIKivrdvladvgmldyidsepaNLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 135 MKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEkIADYIIHLSDGEVILNGS-- 212
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSpv 228
|
250
....*....|.
gi 577230680 213 ----KEQLLQR 219
Cdd:PRK13640 229 eifsKVEMLKE 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-217 |
6.82e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.95 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVnysSDQFN----LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV----LEEDMALNPI- 71
Cdd:PRK11264 1 MSAIEVKNL---VKKFHgqtvLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditIDTARSLSQQk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 72 ----ELKNRIGFVY-SENYFNERwttKQLEKMI-APFYRKWD-----HQVFEFYLEKFDLPINKSI--KTFSTGMKMKLS 138
Cdd:PRK11264 78 glirQLRQHVGFVFqNFNLFPHR---TVLENIIeGPVIVKGEpkeeaTARARELLAKVGLAGKETSypRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 139 LAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQ-LAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
18-215 |
8.54e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.63 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA---LNPIELKNRIGFV--YSENYFNERWTT 92
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkVKLSDIRKKVGLVfqYPEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 93 KQL----------EKMIAPFYRKWDHQV---FEFYLEK--FDLpinksiktfSTGMKMKLSLAVAFSHHAELYIFDEPTS 157
Cdd:PRK13637 103 KDIafgpinlglsEEEIENRVKRAMNIVgldYEDYKDKspFEL---------SGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 158 GLDPLARNELLEIIqQELIDENK-TIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQ 215
Cdd:PRK13637 174 GLDPKGRDEILNKI-KELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-219 |
1.09e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.83 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNY---SSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVleEDMALNP---IELKN 75
Cdd:PRK13635 4 EIIRVEHISFrypDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV--GGMVLSEetvWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 RIGFVYS-------------------ENYFNERwttkqlEKMIapfyRKWDHQVFEFYLEKFdlpINKSIKTFSTGMKMK 136
Cdd:PRK13635 82 QVGMVFQnpdnqfvgatvqddvafglENIGVPR------EEMV----ERVDQALRQVGMEDF---LNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 137 LSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLEKIA--DYIIHLSDGEVILNGSKE 214
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITH---DLDEAAqaDRVIVMNKGEILEEGTPE 225
|
....*
gi 577230680 215 QLLQR 219
Cdd:PRK13635 226 EIFKS 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-205 |
1.13e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 80.52 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVN--YSSDQFN---LKNISFKVPQG-FVTgFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDmalnPIELK 74
Cdd:COG1116 5 APALELRGVSkrFPTGGGGvtaLDDVSLTVAAGeFVA-LVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP----VTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVysenyFNER----W-TTKQ-----LEKMIAPfyRKWDHQVFEFYLEKFDL-------PinksiKTFSTGMKMKL 137
Cdd:COG1116 80 PDRGVV-----FQEPallpWlTVLDnvalgLELRGVP--KAERRERARELLELVGLagfedayP-----HQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 138 SLAVAFSHHAELYIFDEPTSGLDPLARNELleiiQQELID----ENKTIFMSTHiisDLE---KIADYIIHLSDG 205
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERL----QDELLRlwqeTGKTVLFVTH---DVDeavFLADRVVVLSAR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-208 |
1.56e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFNL-KNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEedmalnpielKNRIGFVYS 82
Cdd:COG0488 316 LELEGLSKSYGDKTLlDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE----------TVKIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 EN-YFNERWTtkqLEKMIAPFYRKWDHQVFEFYLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:COG0488 386 HQeELDPDKT---VLDELRDGAPGGTEQEVRGYLGRFLFSgddAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577230680 159 LDPlarnELLEIIQQELIDENKTIFMSTHiisD---LEKIADYIIHLSDGEVI 208
Cdd:COG0488 463 LDI----ETLEALEEALDDFPGTVLLVSH---DryfLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-212 |
2.18e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVleEDMALNP-------------------IELKNRIG 78
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDkknnhelitnpyskkiknfKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSENYFNERWTTKQLEKMIAPF---YRKWD-HQVFEFYLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSHHAELYI 151
Cdd:PRK13631 120 MVFQFPEYQLFKDTIEKDIMFGPValgVKKSEaKKLAKFYLNKMGLDdsyLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 152 FDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGS 212
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-211 |
2.26e-17 |
|
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: 79.24 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLyQPQTGVI--RVLEEDMALNPIELKNRIGFVYSENYF------NER 89
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR-VEGGGTTsgQILFNGQPRKPDQFQKCVAYVRQDDILlpgltvRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 WTTKQLEKMIAPFYRKWDHQVFEFYLEKF--DLPI-NKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNE 166
Cdd:cd03234 102 LTYTAILRLPRKSSDAIRKKRVEDVLLRDlaLTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 577230680 167 LLEIIQQeLIDENKTIFMSTHII-SDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03234 182 LVSTLSQ-LARRNRIVILTIHQPrSDLFRLFDRILLLSSGEIVYSG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-208 |
4.82e-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: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVnysSDQFN----LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL-NPIE-LKNR 76
Cdd:COG3845 5 ALELRGI---TKRFGgvvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrSPRDaIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 IGFVY------------------SENYFNERWTTKQLEKMIApfyrkwdhqvfEFyLEKFDLPIN--KSIKTFSTGMKMK 136
Cdd:COG3845 82 IGMVHqhfmlvpnltvaenivlgLEPTKGGRLDRKAARARIR-----------EL-SERYGLDVDpdAKVEDLSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 137 LSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-222 |
5.62e-17 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 78.47 E-value: 5.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVY--SENYFNERWTTKQL 95
Cdd:TIGR04406 17 VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYlpQEASIFRKLTVEEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 96 EKMIAPFYRKWDHQVFEFYLEKF--DLPI----NKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLE 169
Cdd:TIGR04406 97 IMAVLEIRKDLDRAEREERLEALleEFQIshlrDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 170 IIQQeLIDENKTIFMSTHIISDLEKIAD--YIIHlsDGEVILNGSKEQLLQRYQV 222
Cdd:TIGR04406 177 IIKH-LKERGIGVLITDHNVRETLDICDraYIIS--DGKVLAEGTPAEIVANEKV 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-218 |
6.24e-17 |
|
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: 77.97 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVY--SENYFNERWTTKQ- 94
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYlpQEASIFRKLTVEEn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 ----LEkmIAPFYRKWDHQVFEFYLEKFDL-PINKSI-KTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELL 168
Cdd:cd03218 96 ilavLE--IRGLSKKEREEKLEELLEEFHItHLRKSKaSSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 169 EIIQQeLIDENKTIFMSTHIISDLEKIAD--YIIHlsDGEVILNGSKEQLLQ 218
Cdd:cd03218 174 KIIKI-LKDRGIGVLITDHNVRETLSITDraYIIY--EGKVLAEGTPEEIAA 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-228 |
6.95e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.47 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL-------------NPIE-LKNRIGFVYse 83
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvadkNQLRlLRTRLTMVF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 NYFNERWTTKQLEK-MIAP-----FYRKWDHQVFEFYLEKFDLPINKSIK---TFSTGMKMKLSLAVAFSHHAELYIFDE 154
Cdd:PRK10619 99 QHFNLWSHMTVLENvMEAPiqvlgLSKQEARERAVKYLAKVGIDERAQGKypvHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 155 PTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL------QRYQVVSGAIE 228
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQ-LAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFgnpqspRLQQFLKGSLK 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
4-218 |
8.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.62 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN------LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV-------LEEDMALNP 70
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 71 IELKNRIGFVYSENYFNERWTTKQLEKMIAPF--YRKWDHQVFEFYLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSH 145
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNFgiPKEKAEKIAAEKLEMVGLAdefWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 146 HAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-218 |
2.52e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 76.98 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGFVYSENYFNERWTTKQL- 95
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmLSSRQLARRLALLPQHHLTPEGITVRELv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 96 EKMIAPFYRKW------DHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNEL 167
Cdd:PRK11231 98 AYGRSPWLSLWgrlsaeDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577230680 168 LEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:PRK11231 178 MRLM-RELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-218 |
2.76e-16 |
|
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: 76.91 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIEL----KNRIGFVYS---------- 82
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAaMSRKELrelrRKKISMVFQsfallphrtv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 -ENyfnerwTTKQLEkmIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:cd03294 120 lEN------VAFGLE--VQGVPRAEREERAAEALELVGLEgwEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 160 DPLARNELleiiQQELID----ENKTIFMSTHiisDLE---KIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:cd03294 192 DPLIRREM----QDELLRlqaeLQKTIVFITH---DLDealRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-202 |
3.98e-16 |
|
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: 78.10 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSDQFN--LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGF 79
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpaLRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFnerwttkqLEKMIAP---FYRKW--DHQVFE----FYLEKF--------DLPINKSIKTFSTGMKMKLSLAVA 142
Cdd:TIGR02857 401 VPQHPFL--------FAGTIAEnirLARPDasDAEIREalerAGLDEFvaalpqglDTPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLEKiADYIIHL 202
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRA--LAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-221 |
5.66e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.94 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIG 78
Cdd:PRK11160 338 SLTLNNVSFTypdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIaDYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FV------YS----ENYF--NERWTTKQLEKMIapfyrkwdHQVFEFYLEKFDLPINKSI----KTFSTGMKMKLSLAVA 142
Cdd:PRK11160 418 VVsqrvhlFSatlrDNLLlaAPNASDEALIEVL--------QQVGLEKLLEDDKGLNAWLgeggRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIQQELidENKTIFMSTHIISDLEKIaDYIIHLSDGEVILNGSKEQLLQ---R 219
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAqqgR 566
|
..
gi 577230680 220 YQ 221
Cdd:PRK11160 567 YY 568
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-209 |
6.27e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV--------LEEDMALNP---------------IELK 74
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrigyLPQEPPLDDdltvldtvldgdaelRALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYSENYFNERwTTKQLEKMIAPFYRK----WDHQVfEFYLEKFDLPI---NKSIKTFSTGMKMKLSLAVAFSHHA 147
Cdd:COG0488 94 AELEELEAKLAEPDE-DLERLAELQEEFEALggweAEARA-EEILSGLGFPEedlDRPVSELSGGWRRRVALARALLSEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 148 ELYIFDEPTSGLDplarnelLEIIQ---QELIDENKTIFMSTHiisD---LEKIADYIIHLSDGEVIL 209
Cdd:COG0488 172 DLLLLDEPTNHLD-------LESIEwleEFLKNYPGTVLVVSH---DryfLDRVATRILELDRGKLTL 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-219 |
6.85e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.92 E-value: 6.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNV--NYSSDQ--FNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV----LEEDmalNPIE 72
Cdd:PRK13650 2 SNIIEVKNLtfKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdgdlLTEE---NVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 73 LKNRIGFVYS--ENYF--------------NERWTTKQLEKMIapfyrkwdHQVFEFY-LEKFDlpiNKSIKTFSTGMKM 135
Cdd:PRK13650 79 IRHKIGMVFQnpDNQFvgatveddvafgleNKGIPHEEMKERV--------NEALELVgMQDFK---EREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 136 KLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLEKIA--DYIIHLSDGEVILNGSK 213
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITH---DLDEVAlsDRVLVMKNGQVESTSTP 224
|
....*.
gi 577230680 214 EQLLQR 219
Cdd:PRK13650 225 RELFSR 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-211 |
1.00e-15 |
|
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: 74.45 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFNLkNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIElKNRIGFVYSE 83
Cdd:cd03298 1 VRLDKIRFSYGEQPM-HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-DRPVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 NYFNERWTTKQ---LEKMIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:cd03298 79 NNLFAHLTVEQnvgLGLSPGLKLTAEDRQAIEVALARVGLAglEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 577230680 159 LDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:cd03298 159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-219 |
1.01e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.98 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIrVLE----EDMALNpiELKNR 76
Cdd:PRK11176 342 IEFRNVTFTypgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI-LLDghdlRDYTLA--SLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 IGFVySEN--YFN------------ERWTTKQLEK-------MiaPFYRKWDHqvfefyleKFDLPINKSIKTFSTGMKM 135
Cdd:PRK11176 419 VALV-SQNvhLFNdtianniayartEQYSREQIEEaarmayaM--DFINKMDN--------GLDTVIGENGVLLSGGQRQ 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 136 KLSLAVAFSHHAELYIFDEPTSGLDPLArnellEIIQQELIDE---NKTIFMSTHIISDLEKiADYIIHLSDGEVILNGS 212
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTES-----ERAIQAALDElqkNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
....*..
gi 577230680 213 KEQLLQR 219
Cdd:PRK11176 562 HAELLAQ 568
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-219 |
1.43e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.17 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNY---SSDQFN---LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVleedmalNPIELKNR 76
Cdd:PRK13649 2 GINLQNVSYtyqAGTPFEgraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV-------DDTLITST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 igfvySENYfnerwTTKQLEKMIAPFYRKWDHQVFE-----------------------FYLEKFDLP------INKSIK 127
Cdd:PRK13649 75 -----SKNK-----DIKQIRKKVGLVFQFPESQLFEetvlkdvafgpqnfgvsqeeaeaLAREKLALVgiseslFEKNPF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 128 TFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:PRK13649 145 ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
250
....*....|..
gi 577230680 208 ILNGSKEQLLQR 219
Cdd:PRK13649 224 VLSGKPKDIFQD 235
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
16-208 |
1.49e-15 |
|
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: 73.87 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 16 FNLKnISFKVPQGFvTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV-------LEEDMALNPieLKNRIGFVYSENYFNE 88
Cdd:cd03297 13 FTLK-IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdSRKKINLPP--QQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 RWTTKQ-LEKMIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARN 165
Cdd:cd03297 89 HLNVREnLAFGLKRKRNREDRISVDELLDLLGLDhlLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577230680 166 ELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-219 |
1.67e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFNLkNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIElknR-IGFVY 81
Cdd:COG3840 2 LRLDDLTYRYGDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtALPPAE---RpVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 SE-NYFN---------------------ERwttKQLEKMIApfyrkwdhQV-FEFYLEKfdLPinksiKTFSTGMKMKLS 138
Cdd:COG3840 78 QEnNLFPhltvaqniglglrpglkltaeQR---AQVEQALE--------RVgLAGLLDR--LP-----GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 139 LAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
.
gi 577230680 219 R 219
Cdd:COG3840 220 G 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-233 |
1.68e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 74.73 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS--SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNP---IELKNRIG 78
Cdd:PRK13639 2 LETRDLKYSypDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYS---ENYF-------------NERWTTKQLEKMIAPFYRKWDHQVFEfylekfdlpiNKSIKTFSTGMKMKLSLAVA 142
Cdd:PRK13639 82 IVFQnpdDQLFaptveedvafgplNLGLSKEEVEKRVKEALKAVGMEGFE----------NKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQV 222
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLL-YDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
250 260
....*....|....*....|.
gi 577230680 223 VSGA----------IEDLDDE 233
Cdd:PRK13639 231 IRKAnlrlprvahlIEILNKE 251
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-219 |
1.72e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 74.11 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS----SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIG 78
Cdd:cd03249 1 IEFKNVSFRypsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FV----------YSEN--YFNERWTTKQLEKM-----IAPFYRKWDHqvfefyleKFDLPINKSIKTFSTGMKMKLSLAV 141
Cdd:cd03249 81 LVsqepvlfdgtIAENirYGKPDATDEEVEEAakkanIHDFIMSLPD--------GYDTLVGERGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 142 AFSHHAELYIFDEPTSGLDplARNEllEIIQQEL--IDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:cd03249 153 ALLRNPKILLLDEATSALD--AESE--KLVQEALdrAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
1.77e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIG 78
Cdd:PRK09536 1 MPMIDVSDLSVEfGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSENYFNERWTTKQLEKMIAPFYR----KW---DHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAEL 149
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPHRsrfdTWtetDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 150 YIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHiisDLEKIADY---IIHLSDGEVILNGSKEQLL 217
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELV-RRLVDDGKTAVAAIH---DLDLAARYcdeLVLLADGRVRAAGPPADVL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
18-215 |
2.24e-15 |
|
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: 73.92 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELkNRIGFVYS-------------E 83
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITgLPPHRI-ARLGIARTfqnprlfpeltvlE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 N-------YFNERWTTKQLEkmiAPFYRKWDHQVFEF---YLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYI 151
Cdd:COG0411 99 NvlvaahaRLGRGLLAALLR---LPRARREEREARERaeeLLERVGLAdrADEPAGNLSYGQQRRLEIARALATEPKLLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 152 FDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQ 215
Cdd:COG0411 176 LDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-226 |
2.43e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 74.27 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 14 DQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVirVLEEDMALN-----PIELKNRIGFVYSEN---- 84
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGA--VLWQGKPLDyskrgLLALRQQVATVFQDPeqqi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 85 YFNE-----RWTTKQLEKMIAPFYRKWDHQVFEFYLEKFDlpiNKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:PRK13638 91 FYTDidsdiAFSLRNLGVPEAEITRRVDEALTLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 160 DPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQVVSGA 226
Cdd:PRK13638 168 DPAGRTQMIAIIRR-IVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAMEQA 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-207 |
3.14e-15 |
|
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: 71.86 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNY---SSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIGF 79
Cdd:cd03246 1 LEVENVSFrypGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIsQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSEnyfnerwttkqlekmiapfyrkwdhqvfefyLEKFDLPINKSIktFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:cd03246 81 LPQD-------------------------------DELFSGSIAENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 577230680 160 DPLARNELLEIIQQeLIDENKTIFMSTHIISDLEkIADYIIHLSDGEV 207
Cdd:cd03246 128 DVEGERALNQAIAA-LKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-207 |
3.60e-15 |
|
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: 72.83 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIE----LKNRI 77
Cdd:cd03292 1 IEFINVTktYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 78 GFVYSENYFNERWTTKQ-----LEKMIAPfYRKWDHQVFEFyLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:cd03292 81 GVVFQDFRLLPDRNVYEnvafaLEVTGVP-PREIRKRVPAA-LELVGLShkHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 151 IFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
9-214 |
5.76e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 9 VNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEedMALNPIELKNRIGFVYSENYFNe 88
Cdd:PRK15056 14 VTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG--QPTRQALQKNLVAYVPQSEEVD- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 rWTTKQLEKMIAPFYR-----------KWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEP 155
Cdd:PRK15056 91 -WSFPVLVEDVVMMGRyghmgwlrrakKRDRQIVTAALARVDMVefRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 156 TSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIhLSDGEVILNGSKE 214
Cdd:PRK15056 170 FTGVDVKTEARIISLL-RELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTE 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-211 |
6.42e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.58 E-value: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALN---PIELKNRIGFVYSENYFNERWTTKQ 94
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktKEKEKVLEKLVIQKTRFKKIKKIKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 LEKMIAPFYRKWDHQVFE--------F------------------YLEKFDLPIN---KSIKTFSTGMKMKLSLAVAFSH 145
Cdd:PRK13651 103 IRRRVGVVFQFAEYQLFEqtiekdiiFgpvsmgvskeeakkraakYIELVGLDESylqRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 146 HAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNG 211
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIF-DNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-207 |
6.73e-15 |
|
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: 71.31 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIE--LKNRIGFVySENyfnerwttkql 95
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYV-PED----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 96 ekmiapfyRKwDHQVFEfylekfDLPI--NKSIKTF-STGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIq 172
Cdd:cd03215 84 --------RK-REGLVL------DLSVaeNIALSSLlSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI- 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 577230680 173 QELIDENKTIFMsthIISDLEKI---ADYIIHLSDGEV 207
Cdd:cd03215 148 RELADAGKAVLL---ISSELDELlglCDRILVMYEGRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
8.07e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 8.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNV--NYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEdmalnPIELKNrig 78
Cdd:PRK13652 1 MHLIETRDLcySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE-----PITKEN--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 fvysenyfnerwtTKQLEKMIAPFYRKWDHQVFEFYLEKfDL---PINKSIKT--------------------------F 129
Cdd:PRK13652 73 -------------IREVRKFVGLVFQNPDDQIFSPTVEQ-DIafgPINLGLDEetvahrvssalhmlgleelrdrvphhL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 130 STGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVIL 209
Cdd:PRK13652 139 SGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
250 260
....*....|....*....|.
gi 577230680 210 NGSKEQLLQRYQVVSGAIEDL 230
Cdd:PRK13652 219 YGTVEEIFLQPDLLARVHLDL 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-216 |
1.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.50 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLE-------EDMALNPIELKNRIGFVYSENYFNERW 90
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 91 TTKQLE------KMIAPFYRKWDHQVfefyLEKFDLPIN---KSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDP 161
Cdd:PRK13646 103 VEREIIfgpknfKMNLDEVKNYAHRL----LMDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 162 LARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-222 |
1.59e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.46 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNR--IGFVYSE-------NYFNE 88
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYLPQEasifrrlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 RWTTKQLEKMIAPFYRK--WDHQVFEFYLEKFDLPINKSIktfSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNE 166
Cdd:PRK10895 99 LMAVLQIRDDLSAEQREdrANELMEEFHIEHLRDSMGQSL---SGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 167 LLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQV 222
Cdd:PRK10895 176 IKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-247 |
1.71e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 73.62 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-------LNPielk 74
Cdd:NF033858 1 VARLEGVSHRyGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdarhrraVCP---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 nRIGF--------------VYsEN--YF--------NERwttkqlEKMIAPFYRKWDhqvfefyLEKF-DLPINKsiktF 129
Cdd:NF033858 77 -RIAYmpqglgknlyptlsVF-ENldFFgrlfgqdaAER------RRRIDELLRATG-------LAPFaDRPAGK----L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 130 STGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARnelleiiQQ--ELIDE------NKTIFMSTHIISDLEKIaDYIIH 201
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSR-------RQfwELIDRiraerpGMSVLVATAYMEEAERF-DWLVA 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 577230680 202 LSDGEVILNGSKEQLLQRyqvvSGAiEDLDDELASLLiyEEHKRTG 247
Cdd:NF033858 210 MDAGRVLATGTPAELLAR----TGA-DTLEAAFIALL--PEEKRRG 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-262 |
1.75e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.96 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN------LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALN------PI 71
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikeVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 72 ELKNRIGFVYSenyFNE-RWTTKQLEKMIA--PFYRKWDHQvfEFY------LEKFDLP---INKSIKTFSTGMKMKLSL 139
Cdd:PRK13645 87 RLRKEIGLVFQ---FPEyQLFQETIEKDIAfgPVNLGENKQ--EAYkkvpelLKLVQLPedyVKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 140 AVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 577230680 220 YQVVSgAIEDLDDELASLLIYEEHKRTGFIG-----LTEHAQVFKEIL 262
Cdd:PRK13645 242 QELLT-KIEIDPPKLYQLMYKLKNKGIDLLNknirtIEEFAKELAKVL 288
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
8-226 |
1.91e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 8 NVNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALN-----PIELKNRIGFVYS 82
Cdd:PRK13636 12 NYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSG--RILFDGKPIDysrkgLMKLRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 EN---------YFNERWTTKQLEKMIAPFYRKWDHQVFEFYLEKFDlpiNKSIKTFSTGMKMKLSLAVAFSHHAELYIFD 153
Cdd:PRK13636 90 DPdnqlfsasvYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLK---DKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 154 EPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQVVSGA 226
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKV 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-218 |
3.24e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL-NPIE-LKNRIGFVySENyfneRwttKQL 95
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrSPRDaIRAGIAYV-PED----R---KGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 96 ---------EKMIAPFY----------RKWDHQVFEFYLEKFDL---PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFD 153
Cdd:COG1129 340 glvldlsirENITLASLdrlsrgglldRRRERALAEEYIKRLRIktpSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 154 EPTSGLDPLARNELLEIIqQELIDENKTIFMsthIISDLE---KIADYIIHLSDGEV--ILNG---SKEQLLQ 218
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLI-RELAAEGKAVIV---ISSELPellGLSDRILVMREGRIvgELDReeaTEEAIMA 488
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-205 |
3.82e-14 |
|
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: 70.16 E-value: 3.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEE----DMA-LNPIEL----KNRIGFVySEnYFNE 88
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAqASPREIlalrRRTIGYV-SQ-FLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 --RWTTkqLEKMIAPFYRK-WDHQVFEF----YLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:COG4778 105 ipRVSA--LDVVAEPLLERgVDREEARArareLLARLNLPerlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577230680 159 LDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDG 205
Cdd:COG4778 183 LDAANRAVVVELI-EEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-219 |
4.41e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVleEDMALNPIELKNRI----- 77
Cdd:PRK09493 2 IEFKNVSKHFGPTQvLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIV--DGLKVNDPKVDERLirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 78 GFVYSENYFNERWTTkqLEK-MIAPFY-----RKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAEL 149
Cdd:PRK09493 80 GMVFQQFYLFPHLTA--LENvMFGPLRvrgasKEEAEKQARELLAKVGLAerAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 150 YIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-219 |
4.64e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 71.26 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSDQFN---LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKN-- 75
Cdd:COG1135 2 IELENLSktFPTKGGPvtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 -RIGFVY-SENYFNERwTTKQ-----LEkmIApfyrKWDHQ-----VFEfYLEKFDLP--INKSIKTFSTGMKMKLSLAV 141
Cdd:COG1135 82 rKIGMIFqHFNLLSSR-TVAEnvalpLE--IA----GVPKAeirkrVAE-LLELVGLSdkADAYPSQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 142 AFSHHAELYIFDEPTSGLDP------LarnELLEIIQQELideNKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQ 215
Cdd:COG1135 154 ALANNPKVLLCDEATSALDPettrsiL---DLLKDINREL---GLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
....
gi 577230680 216 LLQR 219
Cdd:COG1135 228 VFAN 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-219 |
4.96e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.82 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-------LNPieLKNRIGFVYSenyFNErw 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkkLKP--LRKKVGIVFQ---FPE-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 91 ttkqlekmiapfyrkwdHQVFEFYLEKfDL---PIN---------------------------KSIKTFSTGMKMKLSLA 140
Cdd:PRK13634 96 -----------------HQLFEETVEK-DIcfgPMNfgvseedakqkaremielvglpeellaRSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 141 VAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
7.24e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELsNVNYSsDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFV 80
Cdd:PRK13540 2 LDVIEL-DFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YSENYFNERWTTKQ---LEKMIAPFYRKWDHQVFEFYLEKF-DLPINksikTFSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:PRK13540 80 GHRSGINPYLTLREnclYDIHFSPGAVGITELCRLFSLEHLiDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 577230680 157 SGLDPLARNELLEIIQQELiDENKTIFMSTHIISDLEKiADY 198
Cdd:PRK13540 156 VALDELSLLTIITKIQEHR-AKGGAVLLTSHQDLPLNK-ADY 195
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-205 |
8.83e-14 |
|
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: 69.03 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRvleedMALNPIELKNRIGFVYSENYFNERWTTKQ--- 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI-----LEGKQITEPGPDRMVVFQNYSLLPWLTVReni 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 ---LEKMIAPFYRKWDHQVFEFYLEKFDL--PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLE 169
Cdd:TIGR01184 76 alaVDRVLPDLSKSERRAIVEEHIALVGLteAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 577230680 170 IIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDG 205
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
3-216 |
9.63e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.86 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNY------SSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNP-----I 71
Cdd:PRK13641 2 SIKFENVDYiyspgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 72 ELKNRIGFVY--SENYFNERWTTKQLE---KMIAPFYRKWDHQVFEfYLEKFDLP---INKSIKTFSTGMKMKLSLAVAF 143
Cdd:PRK13641 82 KLRKKVSLVFqfPEAQLFENTVLKDVEfgpKNFGFSEDEAKEKALK-WLKKVGLSedlISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 144 SHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLF-KDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-216 |
9.93e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.79 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIEL---KN 75
Cdd:PRK11831 5 ANLVDMRGVSFTrGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 RIGFVYSE-------NYF-NERWTTKQLEKMIAPFYrkwdHQVFEFYLEKFDLPINKSIK--TFSTGMKMKLSLAVAFSH 145
Cdd:PRK11831 85 RMSMLFQSgalftdmNVFdNVAYPLREHTQLPAPLL----HSTVMMKLEAVGLRGAAKLMpsELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 146 HAELYIFDEPTSGLDPLARNELLeiiqqELIDE-NK----TIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLV-----KLISElNSalgvTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-209 |
1.29e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.45 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLY--QPQTGVIRVLE----------EDMA 67
Cdd:COG2401 28 AIVLEAFGVELRVVERYvLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDnqfgreasliDAIG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 68 LNP-----IELKNRIGfvYSENYFnerwttkqlekmiapFYRKWDHqvfefylekfdlpinksiktFSTGMKMKLSLAVA 142
Cdd:COG2401 108 RKGdfkdaVELLNAVG--LSDAVL---------------WLRRFKE--------------------LSTGQKFRFRLALL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTH---IISDLekIADYIIHLSDGEVIL 209
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHhydVIDDL--QPDLLIFVGYGGVPE 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-208 |
1.38e-13 |
|
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: 68.21 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSN--VNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIE-LKNRIGF 79
Cdd:cd03369 7 IEVENlsVRYAPDLPPvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEdLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFnerwTTKQLEKMIAPFYRKWDHQVFEfylekfDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:cd03369 87 IPQDPTL----FSGTIRSNLDPFDEYSDEEIYG------ALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577230680 160 DPLARNELLEIIQQELidENKTIFMSTHiisDLEKIADY--IIHLSDGEVI 208
Cdd:cd03369 157 DYATDALIQKTIREEF--TNSTILTIAH---RLRTIIDYdkILVMDAGEVK 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-269 |
1.71e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNP-IELKNRIGFVYS-----------EN 84
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkLDHkLAAQLGIGIIYQelsvideltvlEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 85 YFNERWTTKQLEKMIAPFYRKWdHQVFEFYLEKFDLPINKSIKT--FSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPL 162
Cdd:PRK09700 101 LYIGRHLTKKVCGVNIIDWREM-RVRAAMMLLRVGLKVDLDEKVanLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 163 ARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEvilngskeqllqryQVVSGAIEDL-DDELASLLIYE 241
Cdd:PRK09700 180 EVDYLFLIMNQ-LRKEGTAIVYISHKLAEIRRICDRYTVMKDGS--------------SVCSGMVSDVsNDDIVRLMVGR 244
|
250 260
....*....|....*....|....*....
gi 577230680 242 EHKrTGFIGLTE-HAQVFKEILGHKVNIT 269
Cdd:PRK09700 245 ELQ-NRFNAMKEnVSNLAHETVFEVRNVT 272
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-208 |
1.78e-13 |
|
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: 68.29 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YSSD-QFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGF 79
Cdd:cd03244 3 IEFKNVSlrYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENY-------FNerwttkqlekmIAPFYRKWDHQVFEfYLE-------------KFDLPINKSIKTFSTGMKMKLSL 139
Cdd:cd03244 83 IPQDPVlfsgtirSN-----------LDPFGEYSDEELWQ-ALErvglkefveslpgGLDTVVEEGGENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 140 AVAFSHHAELYIFDEPTSGLDPlarnELLEIIQQELIDE--NKTIFMSTHiisDLEKIADY--IIHLSDGEVI 208
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDP----ETDALIQKTIREAfkDCTVLTIAH---RLDTIIDSdrILVLDKGRVV 216
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-219 |
2.32e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.99 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSD--QFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGF 79
Cdd:PRK13657 334 AVEFDDVSFSYDnsRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtVTRASLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFNERWTTKQL---------EKMIAPFYRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:PRK13657 414 VFQDAGLFNRSIEDNIrvgrpdatdEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 151 IFDEPTSGLDPLARNELleiiqQELIDE---NKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:PRK13657 494 ILDEATSALDVETEAKV-----KAALDElmkGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR 559
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-225 |
3.23e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN-YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRL---IMDLYQPQTGVIRVLEEDMALN-----PIELK 74
Cdd:PRK14243 11 LRTENLNvYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGFRVEGKVTFHGKNLYapdvdPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYSE-NYFnerwtTKQLEKMIAPFYR----KWD-HQVFEFYLEKFDL------PINKSIKTFSTGMKMKLSLAVA 142
Cdd:PRK14243 91 RRIGMVFQKpNPF-----PKSIYDNIAYGARingyKGDmDELVERSLRQAALwdevkdKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLEKIAD-----------------YIIHLSDG 205
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHE--LKEQYTIIIVTHNMQQAARVSDmtaffnveltegggrygYLVEFDRT 243
|
250 260
....*....|....*....|
gi 577230680 206 EVILNGSKEQLLQRYqvVSG 225
Cdd:PRK14243 244 EKIFNSPQQQATRDY--VSG 261
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-220 |
3.63e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLI--MDLYQPQTGviRVLEEdMALNP----IELKNR 76
Cdd:TIGR03269 1 IEVKNLTKKFDGKEvLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSG--RIIYH-VALCEkcgyVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 IGFVYS--ENYFNER----WT-----TKQLEKMIAPFYRKwdhqVFEFY------------LEKFDLPINKSIKT----- 128
Cdd:TIGR03269 78 VGEPCPvcGGTLEPEevdfWNlsdklRRRIRKRIAIMLQR----TFALYgddtvldnvleaLEEIGYEGKEAVGRavdli 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 129 ---------------FSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLE 193
Cdd:TIGR03269 154 emvqlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*..
gi 577230680 194 KIADYIIHLSDGEVILNGSKEQLLQRY 220
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-207 |
4.75e-13 |
|
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: 67.11 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS----SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPIE---LKNR 76
Cdd:cd03248 12 VKFQNVTFAyptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGG--QVLLDGKPISQYEhkyLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 IGFVYSENYFNER---------WTTKQLEKMIAPFYRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHA 147
Cdd:cd03248 90 VSLVGQEPVLFARslqdniaygLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 148 ELYIFDEPTSGLDPlarnELLEIIQQELID--ENKTIFMSTHIISDLEKiADYIIHLSDGEV 207
Cdd:cd03248 170 QVLILDEATSALDA----ESEQQVQQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-217 |
5.42e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.81 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAI-ELSNVNY----SSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELK 74
Cdd:PRK13642 1 MNKIlEVENLVFkyekESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYS--ENYF----NERWTTKQLEKMIAP---FYRKWDHQVFEFYLEKFDlpiNKSIKTFSTGMKMKLSLAVAFSH 145
Cdd:PRK13642 81 RKIGMVFQnpDNQFvgatVEDDVAFGMENQGIPreeMIKRVDEALLAVNMLDFK---TREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 146 HAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLEKIA--DYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITH---DLDEAAssDRILVMKAGEIIKEAAPSELF 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-216 |
8.59e-13 |
|
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: 68.78 E-value: 8.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIR------VLEEDMALNPIELKNRI--GFVYSENYFNER 89
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhsgrisFSPQTSWIMPGTIKDNIifGLSYDEYRYTSV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 WTTKQLEKMIAPFyrkwdhqvfefyLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLE 169
Cdd:TIGR01271 522 IKACQLEEDIALF------------PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFE 589
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577230680 170 IIQQELIdENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQL 216
Cdd:TIGR01271 590 SCLCKLM-SNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-214 |
8.96e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNySSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL-NPIE-LKNRIGFVYS 82
Cdd:PRK09700 267 EVRNVT-SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrSPLDaVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ---ENYFNERWTTKQ------------LEKMIAPFYRKWDHQVFEFYLEKFDL---PINKSIKTFSTGMKMKLSLAVAFS 144
Cdd:PRK09700 346 srrDNGFFPNFSIAQnmaisrslkdggYKGAMGLFHEVDEQRTAENQRELLALkchSVNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEV--ILNGSKE 214
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLtqILTNRDD 496
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-206 |
1.04e-12 |
|
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: 65.57 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 16 FNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVlEEDMALNPIE-------LKNRIGFVYSenyFNE 88
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-PGSIAYVSQEpwiqngtIRENILFGKP---FDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 RWTTK-----QLEKmiapfyrkwDhqvfefyLEKFDLPIN-----KSIkTFSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:cd03250 95 ERYEKvikacALEP---------D-------LEILPDGDLteigeKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577230680 159 LDPLARNELLE-IIQQELIDeNKTIFMSTHIISDLEKiADYIIHLSDGE 206
Cdd:cd03250 158 VDAHVGRHIFEnCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
1.53e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.02 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVN-YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRL---IMDLYQPQ--TGVIRVLEEDM---ALNPI 71
Cdd:PRK14267 2 KFAIETVNLRvYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrLLELNEEArvEGEVRLFGRNIyspDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 72 ELKNRIGFVYS--------ENYFNERWTTKqLEKMIAPfyRKWDHQVFEFYLEKFDL------PINKSIKTFSTGMKMKL 137
Cdd:PRK14267 82 EVRREVGMVFQypnpfphlTIYDNVAIGVK-LNGLVKS--KKELDERVEWALKKAALwdevkdRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 138 SLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFE--LKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
.
gi 577230680 218 Q 218
Cdd:PRK14267 237 E 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-207 |
1.71e-12 |
|
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: 65.35 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMalNPIELKNR-IGFVY 81
Cdd:cd03301 1 VELENVTKRFGNVTaLDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--TDLPPKDRdIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 sENYfnerwttkqlekMIAPFYRKWDHQVFEFYLEKFD--------------LPI----NKSIKTFSTGMKMKLSLAVAF 143
Cdd:cd03301 79 -QNY------------ALYPHMTVYDNIAFGLKLRKVPkdeidervrevaelLQIehllDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 144 SHHAELYIFDEPTSGLDPLARNEL-LEI--IQQELideNKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMrAELkrLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-216 |
1.94e-12 |
|
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: 66.03 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIR------VLEEDMALNPIELKNRI--GFVYSENYFNER 89
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhsgrisFSSQFSWIMPGTIKENIifGVSYDEYRYKSV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 WTTKQLEKMIAPFyrkwdhqvfefyLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLE 169
Cdd:cd03291 133 VKACQLEEDITKF------------PEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577230680 170 IIQQELIdENKTIFMSTHIISDLeKIADYIIHLSDGEVILNGSKEQL 216
Cdd:cd03291 201 SCVCKLM-ANKTRILVTSKMEHL-KKADKILILHEGSSYFYGTFSEL 245
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-212 |
1.99e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 66.75 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVN--YS--SDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEED-MALNPIEL---K 74
Cdd:PRK11153 2 IELKNISkvFPqgGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDlTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 NRIGFVYseNYFN-----------------ERWTTKQLEKMIAPFyrkwdhqvfefyLEKFDL-------PINksiktFS 130
Cdd:PRK11153 82 RQIGMIF--QHFNllssrtvfdnvalplelAGTPKAEIKARVTEL------------LELVGLsdkadryPAQ-----LS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 131 TGMKMKLSLAVAFSHHAELYIFDEPTSGLDP------LarnELLEIIQQELideNKTIFMSTHIISDLEKIADYIIHLSD 204
Cdd:PRK11153 143 GGQKQRVAIARALASNPKVLLCDEATSALDPattrsiL---ELLKDINREL---GLTIVLITHEMDVVKRICDRVAVIDA 216
|
....*...
gi 577230680 205 GEVILNGS 212
Cdd:PRK11153 217 GRLVEQGT 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-218 |
3.03e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.03 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVN--YSSDQFnLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEE--DMALNP-----IEL 73
Cdd:COG4161 2 SIQLKNINcfYGSHQA-LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPsekaiRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 74 KNRIGFVYSEnyfnerwttkqlekmiapfYRKWDH-QVFEFYLE---KFdLPINKSIKTF-------------------- 129
Cdd:COG4161 81 RQKVGMVFQQ-------------------YNLWPHlTVMENLIEapcKV-LGLSKEQAREkamkllarlrltdkadrfpl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 130 --STGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:COG4161 141 hlSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
250
....*....|.
gi 577230680 208 ILNGSKEQLLQ 218
Cdd:COG4161 220 IEQGDASHFTQ 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-219 |
3.93e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.67 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYS----SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIG 78
Cdd:TIGR00958 479 IEFQDVSFSypnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSENYFNER---------WTTKQLEKMIAPFYRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAEL 149
Cdd:TIGR00958 559 LVGQEPVLFSGsvreniaygLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 150 YIFDEPTSGLDplARNELLeiIQQELIDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:TIGR00958 639 LILDEATSALD--AECEQL--LQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-208 |
4.02e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNYS------SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEdmalnPIELKN 75
Cdd:COG4615 326 QTLELRGVTYRypgedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ-----PVTADN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 RIGF------VYSENY-FNERWttkQLEKMIAPfyrkwdhQVFEFYLEKFDLpINK-SIKT-------FSTGMKMKLSLA 140
Cdd:COG4615 401 REAYrqlfsaVFSDFHlFDRLL---GLDGEADP-------ARARELLERLEL-DHKvSVEDgrfsttdLSQGQRKRLALL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 141 VAFSHHAELYIFDEPTSGLDPLAR----NELLeiiqQELIDENKTIFMSTHiisDlEK---IADYIIHLSDGEVI 208
Cdd:COG4615 470 VALLEDRPILVFDEWAADQDPEFRrvfyTELL----PELKARGKTVIAISH---D-DRyfdLADRVLKMDYGKLV 536
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-216 |
4.37e-12 |
|
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: 64.67 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNrIGFVY 81
Cdd:cd03296 2 SIEVRNVSKRFGDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 sENYFNERWTT------------KQLEKMIAPFYRKWDHQVFEFY-LEKFDlpiNKSIKTFSTGMKMKLSLAVAFSHHAE 148
Cdd:cd03296 81 -QHYALFRHMTvfdnvafglrvkPRSERPPEAEIRAKVHELLKLVqLDWLA---DRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 149 LYIFDEPTSGLDPLARNELLEIIqQELIDE--NKTIFMsTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWL-RRLHDElhVTTVFV-THDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-217 |
4.79e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.01 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 19 KNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGFVySENYFNERWTTKQleK 97
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhYASKEVARRIGLL-AQNATTPGDITVQ--E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 MIA-------PFYRKW---DHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARN 165
Cdd:PRK10253 101 LVArgryphqPLFTRWrkeDEEAVTKAMQATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 166 ELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK10253 181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-217 |
6.22e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNYSSDQFNLK---NISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTG--VIRVLEE--DMALNPIELKNR- 76
Cdd:TIGR03269 284 NVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEwvDMTKPGPDGRGRa 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 ---IGFVYSE-NYFNERWTTKQLEKMIA---PF---YRKWDH--QVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFS 144
Cdd:TIGR03269 364 kryIGILHQEyDLYPHRTVLDNLTEAIGlelPDelaRMKAVItlKMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-219 |
7.56e-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: 65.74 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNYS---SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDlyqpqtgvirvlEEDMALNPIELKNRIG 78
Cdd:TIGR00957 635 NSITVHNATFTwarDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA------------EMDKVEGHVHMKGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYSENYFNERWTT------KQLEKmiaPFYRkwdhQVFEFYLEKFDLPI----------NKSIkTFSTGMKMKLSLAVA 142
Cdd:TIGR00957 703 YVPQQAWIQNDSLRenilfgKALNE---KYYQ----QVLEACALLPDLEIlpsgdrteigEKGV-NLSGGQKQRVSLARA 774
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLE-IIQQELIDENKTIFMSTHIISDLEKIaDYIIHLSDGEVILNGSKEQLLQR 219
Cdd:TIGR00957 775 VYSNADIYLFDDPLSAVDAHVGKHIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQR 851
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-216 |
7.72e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 20 NISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYS-EN--YFNERWTTKQLe 96
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTfQHvrLFREMTVIENL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 97 kMIA----------------PFYRKWDHQVFE---FYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEP 155
Cdd:PRK11300 102 -LVAqhqqlktglfsgllktPAFRRAESEALDraaTWLERVGLLehANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 156 TSGLDPLARNELleiiqQELIDE-----NKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK11300 181 AAGLNPKETKEL-----DELIAElrnehNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-220 |
8.09e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.30 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 16 FNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV------------LEEDMA-LNPIELKnriGFVYS 82
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkgsaaliaissgLNGQLTgIENIELK---GLMMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 enyfnerwTTKQLEKMIAPfyrkwdhQVFEFY-LEKFdlpINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDP 161
Cdd:PRK13545 115 --------LTKEKIKEIIP-------EIIEFAdIGKF---IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 162 LARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRY 220
Cdd:PRK13545 177 TFTKKCLDKM-NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHY 234
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-224 |
8.48e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.74 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLI---------------MDLYQPQTGviRVLEEDMALNPIELKNRIGFVYS 82
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdpratsgrivfdgKDITDWQTA--KIMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 EN-----YFNERwttKQLEKMIApfyrkwdhQVFEFYLEKFDLPINKSiKTFSTGMKMKLSLAVAFSHHAELYIFDEPTS 157
Cdd:PRK11614 99 ENlamggFFAER---DQFQERIK--------WVYELFPRLHERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 158 GLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQVVS 224
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRS 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-218 |
9.56e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 9.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 16 FNLKNISFKV-------------PQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPIELK---NRIGF 79
Cdd:PRK10575 12 FALRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEG--EILLDAQPLESWSSKafaRKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFNERWTTKQLEKM-IAPF------YRKWDHQVFEFYLEKFDL-PI-NKSIKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIgRYPWhgalgrFGAADREKVEEAISLVGLkPLaHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 151 IFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-212 |
1.23e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 63.95 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNY-------SSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL--NPIE 72
Cdd:PRK13633 3 EMIKCKNVSYkyesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeeNLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 73 LKNRIGFVYsENYFNERWTTKqLEKMIApfyrkwdhqvfeFYLEKFDLP-------INKSIKT-------------FSTG 132
Cdd:PRK13633 83 IRNKAGMVF-QNPDNQIVATI-VEEDVA------------FGPENLGIPpeeirerVDESLKKvgmyeyrrhaphlLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 133 MKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGS 212
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-206 |
1.34e-11 |
|
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: 64.81 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 25 VPQ-GFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVI-------RVLEEdmalnpielknrigFVYSE--NYFnERWTTKQ 94
Cdd:COG1245 95 VPKkGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdEVLKR--------------FRGTElqDYF-KKLANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 LEKMIAPFY----------------RKWD-HQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEP 155
Cdd:COG1245 160 IKVAHKPQYvdlipkvfkgtvrellEKVDeRGKLDELAEKLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577230680 156 TSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYiIHLSDGE 206
Cdd:COG1245 240 SSYLDIYQRLNVARLI-RELAEEGKYVLVVEHDLAILDYLADY-VHILYGE 288
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-188 |
1.45e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAL-NPIELKNRIG--------FVYSENYfnE 88
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACHYLGhrnamkpaLTVAENL--E 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 RWttkqlekmiAPFYRKWDHQVFEfYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNE 166
Cdd:PRK13539 96 FW---------AAFLGGEELDIAA-ALEAVGLAplAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|..
gi 577230680 167 LLEIIQQELiDENKTIFMSTHI 188
Cdd:PRK13539 166 FAELIRAHL-AQGGIVIAATHI 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-213 |
1.46e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 19 KNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPIELKNRI--GFVY------SENYFNE-- 88
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGG--RIMLNGKEINALSTAQRLarGLVYlpedrqSSGLYLDap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 -RWTTKQLEKMIAPFY--RKWDHQVFEFYLE----KFDLPiNKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDP 161
Cdd:PRK15439 358 lAWNVCALTHNRRGFWikPARENAVLERYRRalniKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 162 LARNELLEIIqQELIDENKTIFMsthIISDLEKI---ADYIIHLSDGEviLNGSK 213
Cdd:PRK15439 437 SARNDIYQLI-RSIAAQNVAVLF---ISSDLEEIeqmADRVLVMHQGE--ISGAL 485
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-220 |
2.20e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVN--YSSDQFNLKNISFKVP-QGFVtGFIGRNGAGKTTIIRLIMDLYQPQTGVIR------------VLEEDMA 67
Cdd:PRK10790 340 RIDIDNVSfaYRDDNLVLQNINLSVPsRGFV-ALVGHTGSGKSTLASLLMGYYPLTEGEIRldgrplsslshsVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 68 L---NPIELKN------RIGFVYSENYFNERWTTKQLekmiAPFYRKWDhqvfefylEKFDLPINKSIKTFSTGMKMKLS 138
Cdd:PRK10790 419 MvqqDPVVLADtflanvTLGRDISEEQVWQALETVQL----AELARSLP--------DGLYTPLGEQGNNLSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 139 LAVAFSHHAELYIFDEPTSGLDplARNEllEIIQQEL--IDENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID--SGTE--QAIQQALaaVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
....*..
gi 577230680 217 LQ---RY 220
Cdd:PRK10790 562 LAaqgRY 568
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-218 |
2.38e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.29 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFNLKnISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIElKNRIGFVYSE 83
Cdd:PRK10771 2 LKLTDITWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 -NYFNE---------------RWTTKQLEKM--IApfyrkwdHQVF-EFYLEKfdLPinksiKTFSTGMKMKLSLAVAFS 144
Cdd:PRK10771 80 nNLFSHltvaqniglglnpglKLNAAQREKLhaIA-------RQMGiEDLLAR--LP-----GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-205 |
2.66e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-------ALNP----I--------------- 71
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaALAAgvaiIyqelhlvpemtvaen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 72 ----ELKNRIGFVYSENYfnERWTTKQLEKMiapfyrkwdhqvfefyleKFDLPINKSIKTFSTGMKMKLSLAVAFSHHA 147
Cdd:PRK11288 100 lylgQLPHKGGIVNRRLL--NYEAREQLEHL------------------GVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 148 ELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDG 205
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVI-RELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-217 |
3.46e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 62.37 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 11 YSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVL-------EEDMALNPIELKNRIGFVYSE 83
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfgKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 N--------YFNERWTTK--------QLEKMIAPFYRKwdhqvFEFYLEKFDlPINKSIKTFSTGMKMKLSLAVAFSHHA 147
Cdd:PRK14246 99 PnpfphlsiYDNIAYPLKshgikekrEIKKIVEECLRK-----VGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 148 ELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITE--LKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-198 |
4.18e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSD-QFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQpqtgvirvLEEDmalnpIELKNRIGFvY 81
Cdd:PRK14258 7 AIKVNNLSFYYDtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE--------LESE-----VRVEGRVEF-F 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 SENYFNERWTTKQLEKMIAPFYRK--------------------WDHQV-----FEFYLEKFDL------PINKSIKTFS 130
Cdd:PRK14258 73 NQNIYERRVNLNRLRRQVSMVHPKpnlfpmsvydnvaygvkivgWRPKLeiddiVESALKDADLwdeikhKIHKSALDLS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 131 TGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADY 198
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDF 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
6.52e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRL---IMDLYQPQ--TGVIRVLEEDM-ALNPIEL 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEvLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIfKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 74 KNRIGFVYS-----------ENY-----FNERWTTK-QLEKMIAPFYRKwdHQVFEFYLEKFDLPINKsiktFSTGMKMK 136
Cdd:PRK14247 81 RRRVQMVFQipnpipnlsifENValglkLNRLVKSKkELQERVRWALEK--AQLWDEVKDRLDAPAGK----LSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 137 LSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQelIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGS---- 212
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLE--LKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPtrev 232
|
250
....*....|....*....
gi 577230680 213 ----KEQLLQRYqvVSGAI 227
Cdd:PRK14247 233 ftnpRHELTEKY--VTGRL 249
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
20-200 |
7.71e-11 |
|
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: 61.61 E-value: 7.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 20 NISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQ---TGVIRVLEEDM-ALNPIELK----NRIGFVYSE--NYFNER 89
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLlKLSEKELRkirgREIQMIFQDpmTSLNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 WTT-KQLEKMIApFYRKWDHQ-----VFEfYLEKFDLPINKSIKT-----FSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:COG0444 103 MTVgDQIAEPLR-IHGGLSKAearerAIE-LLERVGLPDPERRLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577230680 159 LDPLARNELLEIIqQELIDE-NKTIFMSTHIISDLEKIADYII 200
Cdd:COG0444 181 LDVTIQAQILNLL-KDLQRElGLAILFITHDLGVVAEIADRVA 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-210 |
8.39e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 61.23 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGV--------------IRVLEEDMALNPIE-LKNRIGFVYS 82
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtaplaearedTRLMFQDARLLPWKkVIDNVGLGLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ENyfnerWTTKQLEKM----IAPFYRKWdhqvfefylekfdlPinksiKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:PRK11247 108 GQ-----WRDAALQALaavgLADRANEW--------------P-----AALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 159 LDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILN 210
Cdd:PRK11247 164 LDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-289 |
1.37e-10 |
|
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: 61.95 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSEN 84
Cdd:TIGR01257 1942 ELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFD 2021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 85 YFNERWTTKQ---LEKMIAPFYRKWDHQVFEFYLEKFDLPI--NKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:TIGR01257 2022 AIDDLLTGREhlyLYARLRGVPAEEIEKVANWSIQSLGLSLyaDRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 160 DPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRY---QVVSGAIED-LDDELA 235
Cdd:TIGR01257 2102 DPQARRMLWNTIVS-IIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFgdgYIVTMKIKSpKDDLLP 2180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 236 SLLIYEEHKRTGFIGLTEH----------------AQVFKEILGHK-------VNITTPSIENLMVYLEKRKPKYHE 289
Cdd:TIGR01257 2181 DLNPVEQFFQGNFPGSVQRerhynmlqfqvsssslARIFQLLISHKdsllieeYSVTQTTLDQVFVNFAKQQTETYD 2257
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-187 |
2.29e-10 |
|
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: 60.84 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 9 VNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGFV------- 80
Cdd:TIGR02868 342 AGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSsLDQDEVRRRVSVCaqdahlf 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 ---YSENYF--NERWTTKQLEKMIApfyRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEP 155
Cdd:TIGR02868 422 dttVRENLRlaRPDATDEELWAALE---RVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|..
gi 577230680 156 TSGLDPLARNELLEIIQQelIDENKTIFMSTH 187
Cdd:TIGR02868 499 TEHLDAETADELLEDLLA--ALSGRTVVLITH 528
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-187 |
2.34e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 59.74 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNAIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIrvlEEDMALnpielknRIGF 79
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRvLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI---KRNGKL-------RIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFNerwTTKQLE----KMIAPFYRKWD-----HQVFEFYLekFDLPINKsiktFSTGMKMKLSLAVAFSHHAELY 150
Cdd:PRK09544 72 VPQKLYLD---TTLPLTvnrfLRLRPGTKKEDilpalKRVQAGHL--IDAPMQK----LSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 577230680 151 IFDEPTSGLD---PLARNELLEIIQQELideNKTIFMSTH 187
Cdd:PRK09544 143 VLDEPTQGVDvngQVALYDLIDQLRREL---DCAVLMVSH 179
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-218 |
3.19e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 59.27 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVY-----SenYFnERWTT 92
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGYlpqeaS--IF-RKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 93 KQ-----LEkmIAPFYRKWDHQVFEFYLEKFDL-PINKSI-KTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARN 165
Cdd:COG1137 96 EDnilavLE--LRKLSKKEREERLEELLEEFGItHLRKSKaYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 166 ELLEIIQQeLIDENKTIFMSTHIISDLEKIAD--YIIHlsDGEVILNGSKEQLLQ 218
Cdd:COG1137 174 DIQKIIRH-LKERGIGVLITDHNVRETLGICDraYIIS--EGKVLAEGTPEEILN 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-203 |
5.96e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSD-QFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELKNRIGF-- 79
Cdd:PRK10247 8 LQLQNVGYLAGdAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStLKPEIYRQQVSYca 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 ---------VYSENYFNerWTTKQlekmIAPfyrkwDHQVFEFYLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSHHA 147
Cdd:PRK10247 88 qtptlfgdtVYDNLIFP--WQIRN----QQP-----DPAIFLDDLERFALPdtiLTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 148 ELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLEKI--ADYIIHLS 203
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTH---DKDEInhADKVITLQ 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-214 |
7.60e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.10 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVN--YSSDQFnLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEE--DMALNP-----IEL 73
Cdd:PRK11124 2 SIQLNGINcfYGAHQA-LFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPsdkaiREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 74 KNRIGFVYSENYFNERWTTkqLEKMI-AP-----FYRKWDHQVFEFYLEKFDL-------PINksiktFSTGMKMKLSLA 140
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTV--QQNLIeAPcrvlgLSKDQALARAEKLLERLRLkpyadrfPLH-----LSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 141 VAFSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKE 214
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSII-RELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-211 |
8.53e-10 |
|
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: 56.95 E-value: 8.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 17 NLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMdlyqpQTGVIRVLEEDMALNPielKNRIGFVysenyfnerwttKQLE 96
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-----YASGKARLISFLPKFS---RNKLIFI------------DQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 97 KMIApfyrkwdhqVFEFYLekfdlPINKSIKTFSTGMKMKLSLA--VAFSHHAELYIFDEPTSGLDPLARNELLEIIqQE 174
Cdd:cd03238 70 FLID---------VGLGYL-----TLGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVI-KG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577230680 175 LIDENKTIFMSTHIIsDLEKIADYIIHL------SDGEVILNG 211
Cdd:cd03238 135 LIDLGNTVILIEHNL-DVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-219 |
8.57e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNV--NYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDM-ALNPIELKNRIGFV 80
Cdd:PRK10522 323 LELRNVtfAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YSENYFNERWTTKQLEKMIAPFYRKWDHQvfefyLE---KFDLPINKSIKT-FSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANPALVEKWLER-----LKmahKLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDEWA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 157 SGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKiADYIIHLSDGEVI-LNGSKEQLLQR 219
Cdd:PRK10522 478 ADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSeLTGEERDAASR 540
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
18-173 |
1.13e-09 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 57.40 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEE----DMA-LNPIEL----KNRIGFVYSENYFNE 88
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEgawvDLAqASPREVlevrRKTIGYVSQFLRVIP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 RWTT-----KQLEKMIAPfyRKWDHQVFEFYLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLD 160
Cdd:TIGR02324 104 RVSAlevvaEPLLERGVP--REAARARARELLARLNIPerlWHLPPATFSGGEQQRVNIARGFIADYPILLLDEPTASLD 181
|
170
....*....|...
gi 577230680 161 PLARNELLEIIQQ 173
Cdd:TIGR02324 182 AANRQVVVELIAE 194
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
115-216 |
1.16e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 115 LEKFDL--PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDL 192
Cdd:NF000106 129 LERFSLteAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS-MVRDGATVLLTTQYMEEA 207
|
90 100
....*....|....*....|....
gi 577230680 193 EKIADYIIHLSDGEVILNGSKEQL 216
Cdd:NF000106 208 EQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-199 |
1.41e-09 |
|
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: 57.38 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 22 SFK-----VPQ-GFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPIElknriGFVYSE--NYFnERWTTK 93
Cdd:cd03236 14 SFKlhrlpVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWDEILD-----EFRGSElqNYF-TKLLEG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 94 QLEKMIAPFY-----------------RKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDE 154
Cdd:cd03236 86 DVKVIVKPQYvdlipkavkgkvgellkKKDERGKLDELVDQLELRhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 577230680 155 PTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYI 199
Cdd:cd03236 166 PSSYLDIKQRLNAARLI-RELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-208 |
1.46e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.35 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVN--YSSDQfNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLI--M-DLYqPQ---TGVIRVLEEDM---ALNPI 71
Cdd:COG1117 11 KIEVRNLNvyYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMnDLI-PGarvEGEILLDGEDIydpDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 72 ELKNRIGFV-----------YsENyfnerwttkqlekmIApfY----------RKWDHQVfEFYLEKFDLP------INK 124
Cdd:COG1117 89 ELRRRVGMVfqkpnpfpksiY-DN--------------VA--YglrlhgikskSELDEIV-EESLRKAALWdevkdrLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 125 SIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLA--RNElleiiqqELIDENK---TIFMSTHIISDLEKIADYI 199
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStaKIE-------ELILELKkdyTIVIVTHNMQQAARVSDYT 223
|
....*....
gi 577230680 200 IHLSDGEVI 208
Cdd:COG1117 224 AFFYLGELV 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-206 |
1.58e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 27 QGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPIELknrigFVYSE--NYFnERWTTKQLEKMIAPFY- 103
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLG--DYEEEPSWDEVLKR-----FRGTElqNYF-KKLYNGEIKVVHKPQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 104 ---------------RKWD-HQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARN 165
Cdd:PRK13409 170 dlipkvfkgkvrellKKVDeRGKLDEVVERLGLEniLDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL 249
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 577230680 166 ELLEIIqQELIdENKTIFMSTHIISDLEKIADYiIHLSDGE 206
Cdd:PRK13409 250 NVARLI-RELA-EGKYVLVVEHDLAVLDYLADN-VHIAYGE 287
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-61 |
1.92e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 1.92e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV 61
Cdd:PRK11819 325 IEAENLSKSfGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-61 |
2.11e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 2.11e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 4 IELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV 61
Cdd:TIGR03719 323 IEAENLTKAfGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-216 |
2.52e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.40 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAlnPIELKNR-IGFV 80
Cdd:PRK10851 2 SIEIANIKKSFGRTQvLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRkVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 81 YsENYFNERWTT---------KQLEKMIAPFYRKWDHQVFEFyLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAEL 149
Cdd:PRK10851 80 F-QHYALFRHMTvfdniafglTVLPRRERPNAAAIKAKVTQL-LEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 150 YIFDEPTSGLDPLARNELLEIIQQeLIDENKtiFMSTHIISDLE---KIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQ-LHEELK--FTSVFVTHDQEeamEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-210 |
2.58e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 57.81 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 1 MNA-IELSNV--NYSSDQFN---LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIEL 73
Cdd:PRK10535 1 MTAlLELKDIrrSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 74 ----KNRIGFVYSENYFNERWTTKQ---LEKMIAPFYRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFS 144
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHLTAAQnveVPAVYAGLERKQRLLRAQELLQRLGLEdrVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 145 HHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHiISDLEKIADYIIHLSDGEVILN 210
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTH-DPQVAAQAERVIEIRDGEIVRN 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-216 |
3.65e-09 |
|
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: 56.09 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN-LKNISFKVPQG-FVTgFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIElKNRIGFVY 81
Cdd:cd03300 1 IELENVSKFYGGFVaLDGVSLDIKEGeFFT-LLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 sENY-------------FNERwtTKQLEKmiAPFYRKWDHQVFEFYLEKFDlpiNKSIKTFSTGMKMKLSLAVAFSHHAE 148
Cdd:cd03300 79 -QNYalfphltvfeniaFGLR--LKKLPK--AEIKERVAEALDLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 149 LYIFDEPTSGLDPLARNEL-LEI--IQQELideNKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMqLELkrLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-204 |
3.99e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.85 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSS--DQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEedmalnpielKNRIGFVY 81
Cdd:cd03223 1 IELENLSLATpdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE----------GEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 SENYFNeRWTTKQLekMIAPfyrkWDhqvfefylekfdlpinksiKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDP 161
Cdd:cd03223 71 QRPYLP-LGTLREQ--LIYP----WD-------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577230680 162 LARNELLEIIQQELIdenkTIFMSTHIISdLEKIADYIIHLSD 204
Cdd:cd03223 125 ESEDRLYQLLKELGI----TVISVGHRPS-LWKFHDRVLDLDG 162
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
18-208 |
4.04e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVL--EEDMALNPIELKNRIGFVYSE-----------N 84
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkEIDFKSSKEALENGISMVHQElnlvlqrsvmdN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 85 YFNERWTTKQL----EKMiapfYRKwDHQVFefylEKFDLPINKSIK--TFSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:PRK10982 94 MWLGRYPTKGMfvdqDKM----YRD-TKAIF----DELDIDIDPRAKvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 577230680 159 LDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:PRK10982 165 LTEKEVNHLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-217 |
4.50e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIELK----NRIGFVYSENYFNERWTT 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkISDAELRevrrKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 93 KQ-----LEKMIAPFYRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNEL 167
Cdd:PRK10070 124 LDntafgMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 577230680 168 LEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-218 |
4.70e-09 |
|
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: 55.23 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDL--YQPQTGVIRVLEEDMALNPIELKNRIG----FVYSEnyfnerwt 91
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGiflaFQYPP-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 92 tkqlekmiapfyrkwdhQVFEFYLEKFDLPINKSiktFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEII 171
Cdd:cd03217 88 -----------------EIPGVKNADFLRYVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 172 qQELIDENKTIFMSTHiisdLEKIADYI----IH-LSDGEVILNGSKEQLLQ 218
Cdd:cd03217 148 -NKLREEGKSVLIITH----YQRLLDYIkpdrVHvLYDGRIVKSGDKELALE 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-216 |
4.73e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYSSD----QFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNP-----IEL 73
Cdd:PLN03232 614 AISIKNGYFSWDsktsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPqvswiFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 74 KNRIGFVYSENYFNERwttkqlekmiapFYRKWDHQVFEFYLEKF---DLP-INKSIKTFSTGMKMKLSLAVAFSHHAEL 149
Cdd:PLN03232 694 TVRENILFGSDFESER------------YWRAIDVTALQHDLDLLpgrDLTeIGERGVNISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 150 YIFDEPTSGLDP-LARNELLEIIQQELidENKTIFMSTHIISDLEKIaDYIIHLSDGEVILNGSKEQL 216
Cdd:PLN03232 762 YIFDDPLSALDAhVAHQVFDSCMKDEL--KGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAEL 826
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-211 |
6.22e-09 |
|
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: 55.49 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 30 VTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNP--IE----------LKNRIGFVYSENYFN-ERWTTKQLE 96
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPqyIKadyegtvrdlLSSITKDFYTHPYFKtEIAKPLQIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 97 KMIapfyrkwDHQVfefylekfdlpinksiKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELI 176
Cdd:cd03237 107 QIL-------DREV----------------PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180 190
....*....|....*....|....*....|....*
gi 577230680 177 DENKTIFMSTHIISDLEKIADYIIhLSDGEVILNG 211
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLI-VFEGEPSVNG 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-215 |
7.60e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 30 VTGFIGRNGAGKTTIIRLIMDLYQPQTGVI----RVL---EEDMALnPIElKNRIGFVYSE-NYF-------NERWTTKq 94
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngRVLfdaEKGICL-PPE-KRRIGYVFQDaRLFphykvrgNLRYGMA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 lEKMIAPFyrkwDHQV----FEFYLEKFdlPInksikTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEI 170
Cdd:PRK11144 103 -KSMVAQF----DKIVallgIEPLLDRY--PG-----SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 577230680 171 IqQELIDENKT-IFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQ 215
Cdd:PRK11144 171 L-ERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
10-205 |
7.96e-09 |
|
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: 54.64 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 10 NYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVI---RVLEEDMALNPIELKNRigfvYSENYF 86
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNR----YSVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 87 NER-W-TTKQLEKMI---APFYRKWDHQVFEFYLEKFD---LPINKSIK------TFSTGMKMKLSLAVAFSHHAELYIF 152
Cdd:cd03290 85 AQKpWlLNATVEENItfgSPFNKQRYKAVTDACSLQPDidlLPFGDQTEigergiNLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 577230680 153 DEPTSGLDPLARNELL-EIIQQELIDENKTIFMSTHIISDLEKiADYIIHLSDG 205
Cdd:cd03290 165 DDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
18-217 |
1.14e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 54.81 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNP-------------IE-LKNRIGFVYSE 83
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpadrrqLQrIRTRLGMVFQS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 nyFNeRWTTKQ-LEKMI-APFY-----RKWDHQVFEFYLEKFDL-------PINksiktFSTGMKMKLSLAVAFSHHAEL 149
Cdd:COG4598 104 --FN-LWSHMTvLENVIeAPVHvlgrpKAEAIERAEALLAKVGLadkrdayPAH-----LSGGQQQRAAIARALAMEPEV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 150 YIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:COG4598 176 MLFDEPTSALDPELVGEVLKVMRD-LAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-218 |
1.44e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.44 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMdLYQPqTGVIR---VLEEDMALNPIELKNRIGFVYSENYFNERWTTKQ 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSP-KGVKGsgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 ------LEKMIAPFYRKWDHQVFEFYLEKFDLP--------INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLD 160
Cdd:TIGR00955 119 hlmfqaHLRMPRRVTKKEKRERVDEVLQALGLRkcantrigVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 161 PLARNELLEIIqQELIDENKTIFMSTH-IISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:TIGR00955 199 SFMAYSVVQVL-KGLAQKGKTIICTIHqPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-209 |
1.45e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 27 QGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENYFNERwttkqlekmiapfyrkw 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 107 dhqvfefylekfdlpinksiktfstGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQ-----QELIDENKT 181
Cdd:smart00382 64 -------------------------ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLT 118
|
170 180
....*....|....*....|....*...
gi 577230680 182 IFMSTHIISDLekIADYIIHLSDGEVIL 209
Cdd:smart00382 119 VILTTNDEKDL--GPALLRRRFDRRIVL 144
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-233 |
2.28e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS----SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPielknRIG 78
Cdd:PLN03130 614 AISIKNGYFSwdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVP-----QVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FVYS----EN-YFNERWTTKQLEKMIAPFYRKWDHQVfefyLEKFDLP-INKSIKTFSTGMKMKLSLAVAFSHHAELYIF 152
Cdd:PLN03130 689 WIFNatvrDNiLFGSPFDPERYERAIDVTALQHDLDL----LPGGDLTeIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 153 DEPTSGLDP-LARNELLEIIQQELidENKTIFMSTHIISDLEKIaDYIIHLSDGEVILNGSKEQL------LQRYQVVSG 225
Cdd:PLN03130 765 DDPLSALDAhVGRQVFDKCIKDEL--RGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELsnngplFQKLMENAG 841
|
....*...
gi 577230680 226 AIEDLDDE 233
Cdd:PLN03130 842 KMEEYVEE 849
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-178 |
2.48e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 5 ELSNVNYSSDQFNL-KNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV---LE------EDMALNPielk 74
Cdd:PRK11147 321 EMENVNYQIDGKQLvKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtkLEvayfdqHRAELDP---- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 75 nrigfvysenyfnERwTT-------KQlEKMIAPFYRkwdHQVfeFYLEKFDLPINKS---IKTFSTGMKMKLSLAVAFS 144
Cdd:PRK11147 397 -------------EK-TVmdnlaegKQ-EVMVNGRPR---HVL--GYLQDFLFHPKRAmtpVKALSGGERNRLLLARLFL 456
|
170 180 190
....*....|....*....|....*....|....
gi 577230680 145 HHAELYIFDEPTSGLDpLARNELLEiiqqELIDE 178
Cdd:PRK11147 457 KPSNLLILDEPTNDLD-VETLELLE----ELLDS 485
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-188 |
2.94e-08 |
|
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: 52.88 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPIELKNRIGFVYSENYFNERWTTKQLEK 97
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG--RVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 MiaPFYRKW--DHQVFEFY----LEKF-DLPINksikTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEI 170
Cdd:cd03231 94 L--RFWHADhsDEQVEEALarvgLNGFeDRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
170
....*....|....*...
gi 577230680 171 IQQELiDENKTIFMSTHI 188
Cdd:cd03231 168 MAGHC-ARGGMVVLTTHQ 184
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-218 |
3.13e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 53.62 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 3 AIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMAlnpielknrigfvy 81
Cdd:PRK13548 2 MLEARNLSVRlGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 senyfneRWTTKQLEKMIA----------PF---------------YRKWDHQVFEFYLEKFDLP--INKSIKTFSTGMK 134
Cdd:PRK13548 68 -------DWSPAELARRRAvlpqhsslsfPFtveevvamgraphglSRAEDDALVAAALAQVDLAhlAGRDYPQLSGGEQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 135 MKLSLA-----VAFSHHAELYIF-DEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHiisDLE---KIADYIIHLSDG 205
Cdd:PRK13548 141 QRVQLArvlaqLWEPDGPPRWLLlDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH---DLNlaaRYADRIVLLHQG 217
|
250
....*....|...
gi 577230680 206 EVILNGSKEQLLQ 218
Cdd:PRK13548 218 RLVADGTPAEVLT 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
120-216 |
3.27e-08 |
|
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: 54.63 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 120 LPINKSIKTFSTGMKMKLSLAVAFSH---HAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIIsDLEKIA 196
Cdd:TIGR00630 821 IRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQR-LVDKGNTVVVIEHNL-DVIKTA 898
|
90 100
....*....|....*....|....*.
gi 577230680 197 DYIIHL------SDGEVILNGSKEQL 216
Cdd:TIGR00630 899 DYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
18-188 |
4.59e-08 |
|
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: 52.36 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENYFNERWTTKQLEK 97
Cdd:TIGR01189 16 FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 98 MIAPFYRKWDHQVFEfYLEKF------DLPINksikTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPlARNELLEII 171
Cdd:TIGR01189 96 FWAAIHGGAQRTIED-ALAAVgltgfeDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTALDK-AGVALLAGL 169
|
170
....*....|....*..
gi 577230680 172 QQELIDENKTIFMSTHI 188
Cdd:TIGR01189 170 LRAHLARGGIVLLTTHQ 186
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-221 |
4.96e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 16 FNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIR------VLEEDMALNP-------IELKNR-IGFvy 81
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrngevsVIAISAGLSGqltgienIEFKMLcMGF-- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 82 senyfnerwTTKQLEKMIApfyrkwdhQVFEFY-LEKFdlpINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLD 160
Cdd:PRK13546 116 ---------KRKEIKAMTP--------KIIEFSeLGEF---IYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 161 PLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQRYQ 221
Cdd:PRK13546 176 QTFAQKCLDKI-YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-218 |
6.02e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.01 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVL-EEDMALNPIE-------LKNRIGFVYSENyfner 89
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG--RVWaERSIAYVPQQawimnatVRGNILFFDEED----- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 wtTKQLEKMIAPFYRKWDHQVFEFYLEKfdlPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPlarnELLE 169
Cdd:PTZ00243 749 --AARLADAVRVSQLEADLAQLGGGLET---EIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA----HVGE 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 170 IIQQELID---ENKTIFMSTHIISDLEKiADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:PTZ00243 820 RVVEECFLgalAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-216 |
6.34e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVnysSDQFN----LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA-LNPIeLKNRIG 78
Cdd:PRK15439 12 LCARSI---SKQYSgvevLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArLTPA-KAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 79 FvysenyfnerWTTKQlEKMIAPfyrkwDHQVFEFYLekFDLPIN----KSIKTFSTGMKMKLSLAVAFS---------- 144
Cdd:PRK15439 88 I----------YLVPQ-EPLLFP-----NLSVKENIL--FGLPKRqasmQKMKQLLAALGCQLDLDSSAGslevadrqiv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 145 -------HHAELYIFDEPTSGLDPLARNELLEIIQqELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK15439 150 eilrglmRDSRILILDEPTASLTPAETERLFSRIR-ELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-219 |
1.05e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.41 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIElkNR-IGF 79
Cdd:PRK11432 5 NFVVLKNITKRfGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VY-SENYFNERWTTKQLE---KMIAPFYRKWDHQVFEfYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFD 153
Cdd:PRK11432 83 VFqSYALFPHMSLGENVGyglKMLGVPKEERKQRVKE-ALELVDLAgfEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 154 EPTSGLDPLARNELLEII---QQELideNKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIrelQQQF---NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-217 |
1.42e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 51.64 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVirVLEEDMAL---------NPIELKNRIGFVYSE-NYFN 87
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY--RYSGDVLLggrsifnyrDVLEFRRRVGMLFQRpNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 88 ERWTTKQLEKMIAP--FYRKWDHQVFEFYLEKFDL------PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGL 159
Cdd:PRK14271 115 MSIMDNVLAGVRAHklVPRKEFRGVAQARLTEVGLwdavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 160 DPLARNELLEIIQQelIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK14271 195 DPTTTEKIEEFIRS--LADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
4-200 |
2.62e-07 |
|
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: 51.71 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRvLEEDMALNP--IE--------- 72
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKISYKPqyISpdydgtvee 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 73 -LKNRIGFVYSENYFNERWTTK-QLEKMIapfyrkwdhqvfefylekfdlpiNKSIKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:COG1245 421 fLRSANTDDFGSSYYKTEIIKPlGLEKLL-----------------------DKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577230680 151 IFDEPTSGLDPLARNELLEIIQQeLIDEN-KTIFMSTHIISDLEKIADYII 200
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRR-FAENRgKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
4-200 |
5.01e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIrVLEEDMALNPIELKN-------- 75
Cdd:PRK13409 341 VEYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKISYKPQYIKPdydgtved 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 76 ---RIGFVYSENYFNERWTTK-QLEKMiapfyrkwdhqvfefylekFDlpinKSIKTFSTGMKMKLSLAVAFSHHAELYI 151
Cdd:PRK13409 420 llrSITDDLGSSYYKSEIIKPlQLERL-------------------LD----KNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 577230680 152 FDEPTSGLDPLARNELLEIIQQeLIDEN-KTIFMSTHIISDLEKIADYII 200
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRR-IAEEReATALVVDHDIYMIDYISDRLM 525
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-217 |
5.63e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 20 NISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPI----ELKNRI------GFVYSE------ 83
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalsEAERRRllrtewGFVHQHprdglr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 -------------------NYFNERWTTKQ-LEKM-IAPfyRKWDhqvfefylekfDLPinksiKTFSTGMKMKLSLAVA 142
Cdd:PRK11701 104 mqvsaggnigerlmavgarHYGDIRATAGDwLERVeIDA--ARID-----------DLP-----TTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 577230680 143 FSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLL 217
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-192 |
9.31e-07 |
|
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: 50.29 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQtGVIRVleEDMALNPIELKN-RIGF-VYSENYF--------- 86
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQI--DGVSWNSVTLQTwRKAFgVIPQKVFifsgtfrkn 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 87 ---NERWTTKQLEKMIAPFYRKwdhQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLA 163
Cdd:TIGR01271 1312 ldpYEQWSDEEIWKVAEEVGLK---SVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
170 180
....*....|....*....|....*....
gi 577230680 164 RNELLEIIQQELidENKTIFMSTHIISDL 192
Cdd:TIGR01271 1389 LQIIRKTLKQSF--SNCTVILSEHRVEAL 1415
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
125-213 |
1.10e-06 |
|
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: 47.74 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 125 SIKTFSTGMKMKLSLAVAFSHHAE----LYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMsTHiISDLEKIADYII 200
Cdd:cd03227 74 TRLQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVI-TH-LPELAELADKLI 151
|
90
....*....|...
gi 577230680 201 HLsdGEVILNGSK 213
Cdd:cd03227 152 HI--KKVITGVYK 162
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-206 |
1.14e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFN----LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTG--------------------VI 59
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdiiindshnlkdinlkwwrsKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 60 RVLEEDMALNPIELKNRIGF-VYS-------ENYFNERWTTKQ----------------LEKMIAPF-----------YR 104
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYsLYSlkdlealSNYYNEDGNDSQenknkrnscrakcagdLNDMSNTTdsneliemrknYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 105 KWD-------------HQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEII 171
Cdd:PTZ00265 543 TIKdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270
....*....|....*....|....*....|....*
gi 577230680 172 QQELIDENKTIFMSTHIISDLeKIADYIIHLSDGE 206
Cdd:PTZ00265 623 NNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRE 656
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
130-221 |
1.15e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 130 STGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEII---QQELidENKTIFMsTHIISDLEKIADYIIHLSDGE 206
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvlQKEM--SMGVIFI-THDMGVVAEIADRVLVMYQGE 246
|
90
....*....|....*
gi 577230680 207 VILNGSKEQLLQRYQ 221
Cdd:PRK10261 247 AVETGSVEQIFHAPQ 261
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-211 |
1.91e-06 |
|
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: 47.64 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLI---MDLYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENYFNERWTTKQ 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 95 LekmiapfyrkwdhqvFEFYLEkfdLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQE 174
Cdd:cd03233 103 T---------------LDFALR---CKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTM 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 577230680 175 LIDENKTIFMSTHIISD-LEKIADYIIHLSDGEVILNG 211
Cdd:cd03233 165 ADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQIYYG 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-208 |
2.09e-06 |
|
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: 48.67 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQT--GVIRVLEEDMALNPIELKNRIGFV-------------YS 82
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIViihqeltlvpelsVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 83 ENYFNERWTTKQLEKMIAP-FYRKWDHQVFEFYLEkfDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDP 161
Cdd:TIGR02633 97 ENIFLGNEITLPGGRMAYNaMYLRAKNLLRELQLD--ADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 577230680 162 LARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:TIGR02633 175 KETEILLDII-RDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-187 |
2.77e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.50 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGviRVLEEDMALNPI------ELKNR-IGFVYSENYFNERW 90
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG--DVIFNGQPMSKLssaakaELRNQkLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 91 TTkqLEKMIAPFY--RKWDHQVFEFYLEK-----FDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLA 163
Cdd:PRK11629 103 TA--LENVAMPLLigKKKPAEINSRALEMlaavgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180
....*....|....*....|....*
gi 577230680 164 RNELLEIIqQELIDENKTIFM-STH 187
Cdd:PRK11629 181 ADSIFQLL-GELNRLQGTAFLvVTH 204
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-217 |
2.85e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 120 LPINKSIKTFSTGMKMKLSLAVAFShhAEL----YIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTH---IISdl 192
Cdd:PRK00635 468 LTPERALATLSGGEQERTALAKHLG--AELigitYILDEPSIGLHPQDTHKLINVIKK-LRDQGNTVLLVEHdeqMIS-- 542
|
90 100 110
....*....|....*....|....*....|.
gi 577230680 193 ekIADYIIHLS------DGEVILNGSKEQLL 217
Cdd:PRK00635 543 --LADRIIDIGpgagifGGEVLFNGSPREFL 571
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-207 |
4.70e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 14 DQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGvirvleedmalnPIELKNRIGFVYSENYFNE--RWT 91
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG------------EIGLAKGIKLGYFAQHQLEflRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 92 TKQLEKM--IAPfyrKWDHQVFEFYLEKFDL---PINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNE 166
Cdd:PRK10636 392 ESPLQHLarLAP---QELEQKLRDYLGGFGFqgdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 577230680 167 LLEiiqqELIDENKTIFMSTHIISDLEKIAD--YIIHlsDGEV 207
Cdd:PRK10636 469 LTE----ALIDFEGALVVVSHDRHLLRSTTDdlYLVH--DGKV 505
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
120-218 |
4.99e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 120 LPINKSIKTFSTGMKMKLSLA---VAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFM---STHIIsdle 193
Cdd:PRK00635 801 LPLGRPLSSLSGGEIQRLKLAyelLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQS-LTHQGHTVVIiehNMHVV---- 875
|
90 100 110
....*....|....*....|....*....|.
gi 577230680 194 KIADYIIHLS------DGEVILNGSKEQLLQ 218
Cdd:PRK00635 876 KVADYVLELGpeggnlGGYLLASCSPEELIH 906
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
17-206 |
7.00e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.92 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 17 NLKNISFKVPQGFVTgFIGRNGAGKTTIIRLImDLYQPQTGVIRVLEEDMALNP----------IELKNRIGFVYSENYF 86
Cdd:COG3593 13 SIKDLSIELSDDLTV-LVGENNSGKSSILEAL-RLLLGPSSSRKFDEEDFYLGDdpdlpeieieLTFGSLLSRLLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 87 NERWTT----------------KQLEKMIAPFYRKWDHQV---FEFYLEKFDLPINK-----------SIKTFSTGMK-- 134
Cdd:COG3593 91 EEDKEEleealeelneelkealKALNELLSEYLKELLDGLdleLELSLDELEDLLKSlslriedgkelPLDRLGSGFQrl 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 135 MKLSLAVAFSHHAE-----LYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTH--IISDLEKIADyIIHLSDGE 206
Cdd:COG3593 171 ILLALLSALAELKRapanpILLIEEPEAHLHPQAQRRLLKLL-KELSEKPNQVIITTHspHLLSEVPLEN-IRRLRRDS 247
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-216 |
7.44e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 20 NISFKVPQGFVTGFIGRNGAGKTTIIRLIMdlyqpqtGVI----RVLEEDMALNPIEL-----KNRIGFVYSE--NYFNE 88
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSVSSLAIM-------GLIdypgRVMAEKLEFNGQDLqriseKERRNLVGAEvaMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 RWTTkqlekmIAPFY-----------------RKWDHQVFEFYLEKFDLPINKS-----IKTFSTGMKMKLSLAVAFSHH 146
Cdd:PRK11022 98 PMTS------LNPCYtvgfqimeaikvhqggnKKTRRQRAIDLLNQVGIPDPASrldvyPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 147 AELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-219 |
8.90e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.28 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA---------------LNPIELKNRIGF--- 79
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfgltdlrrvlsiipQSPVLFSGTVRFnid 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFNERWttKQLEKM-------IAPFyrKWDHQVFEfylekfdlpinkSIKTFSTGMKMKLSLAVAFSHHAELYIF 152
Cdd:PLN03232 1332 PFSEHNDADLW--EALERAhikdvidRNPF--GLDAEVSE------------GGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 153 DEPTSGLDplARNELLeiIQQELIDENKTIFMSThIISDLEKI--ADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:PLN03232 1396 DEATASVD--VRTDSL--IQRTIREEFKSCTMLV-IAHRLNTIidCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-203 |
1.84e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 21 ISFKVPqgfVTGFIGRNGAGKTTIIRLI-MDLY--QPQTGVIRVLEEDMALN-------PIELKNRIGFVYS-ENYFNer 89
Cdd:cd03240 18 IEFFSP---LTLIVGQNGAGKTTIIEALkYALTgeLPPNSKGGAHDPKLIREgevraqvKLAFENANGKKYTiTRSLA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 wttkQLEKMIapfyrkWDHQvfefylEKFDLPINKSIKTFSTGMKMKLSLAV------AFSHHAELYIFDEPTSGLDPLA 163
Cdd:cd03240 93 ----ILENVI------FCHQ------GESNWPLLDMRGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEPTTNLDEEN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 577230680 164 RNE-LLEIIQQELIDENKTIFMSTHiISDLEKIADYIIHLS 203
Cdd:cd03240 157 IEEsLAEIIEERKSQKNFQLIVITH-DEELVDAADHIYRVE 196
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
120-202 |
2.77e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 120 LPINKSIKTFSTGMKMKLSLAVAFSHHAE---LYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIIsDLEKIA 196
Cdd:cd03271 161 IKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVL-QRLVDKGNTVVVIEHNL-DVIKCA 238
|
....*.
gi 577230680 197 DYIIHL 202
Cdd:cd03271 239 DWIIDL 244
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
127-219 |
3.09e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 127 KTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADYIIHLSDGE 206
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS-LHQSGITLVLVLNRFDEIPDFVQFAGVLADCT 212
|
90
....*....|...
gi 577230680 207 VILNGSKEQLLQR 219
Cdd:PRK10938 213 LAETGEREEILQQ 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-231 |
3.26e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 44.46 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQtGVIRVleEDMALNPIELKN-RIGF-VYSENYF--------- 86
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQI--DGVSWNSVPLQKwRKAFgVIPQKVFifsgtfrkn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 87 ---NERWTTKQLEKMIAPFYRKwdhQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLA 163
Cdd:cd03289 97 ldpYGKWSDEEIWKVAEEVGLK---SVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 164 RNELLEIIQQELIDenKTIFMSTHIISDLEKIADYIIhLSDGEVILNGSKEQLLQRYQVVSGAIEDLD 231
Cdd:cd03289 174 YQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLV-IEENKVRQYDSIQKLLNEKSHFKQAISPSD 238
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-223 |
4.62e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 44.87 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIELKnRIGFVYSENYFNERWT------ 91
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILK-RTGFVTQDDILYPHLTvretlv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 92 -----------TKQLEKMIApfyrkwDHQVFEFYLEKFDLPI--NKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSG 158
Cdd:PLN03211 163 fcsllrlpkslTKQEKILVA------ESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 159 LDPLARNELLEIIQQeLIDENKTIFMSTHIISD-LEKIADYIIHLSDGEVILNGSKEQLLQRYQVV 223
Cdd:PLN03211 237 LDATAAYRLVLTLGS-LAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-60 |
4.74e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 4.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNYSSDQFNL-KNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIR 60
Cdd:PRK15064 318 NALEVENLTKGFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-216 |
5.22e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.85 E-value: 5.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIR----LIMDLYQPQT-----GVIRVLEEDMALNPIELKNRIGFVYSENYFNE 88
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 89 RWTTkqLEKMI------APFYR---KWDHQVFEFY----LEKFDLP--INKSIKTFSTGMKMKLSLAVAFSHHAELYIFD 153
Cdd:PRK09984 100 RLSV--LENVLigalgsTPFWRtcfSWFTREQKQRalqaLTRVGMVhfAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577230680 154 EPTSGLDPlarnELLEIIQQELIDENK----TIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK09984 178 EPIASLDP----ESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-207 |
6.03e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 21 ISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRV-------------LEEDMALNP----------------- 70
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdgkpidirsprdaIRAGIMLCPedrkaegiipvhsvadn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 71 IELKNRIGFVYSENYFNERWTTKQLEKMIAPFYRKWDHqvfefylekfdlpINKSIKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:PRK11288 352 INISARRHHLRAGCLINNRWEAENADRFIRSLNIKTPS-------------REQLIMNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 151 IFDEPTSGLDPLARNELLEIIqQELIDENKTIFMsthIISDLEK---IADYIIHLSDGEV 207
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVI-YELAAQGVAVLF---VSSDLPEvlgVADRIVVMREGRI 474
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
35-188 |
7.56e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 35 GRNGAGKTTIIRLI-MDLYQPQTGVIRVLEEDMALNPIELKNRIGFvysenYFNERWTTKQLEKmiapfYRKWDHQVFE- 112
Cdd:cd03279 35 GPTGAGKSTILDAItYALYGKTPRYGRQENLRSVFAPGEDTAEVSF-----TFQLGGKKYRVER-----SRGLDYDQFTr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 113 -FYLE--KFDLPINKSIKTFSTGMKMKLSLAVAFSHHA----------ELYIFDEPTSGLDPLARNELLEIIQQeLIDEN 179
Cdd:cd03279 105 iVLLPqgEFDRFLARPVSTLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGFGTLDPEALEAVATALEL-IRTEN 183
|
....*....
gi 577230680 180 KTIFMSTHI 188
Cdd:cd03279 184 RMVGVISHV 192
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-207 |
9.11e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 9.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 12 SSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRvleedmaLNPIELKNRIGFVYSENYF----N 87
Cdd:PRK10982 258 SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTIT-------LHGKKINNHNANEAINHGFalvtE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 88 ERWTTKQLEKMIAPFYRKWDHqvFEFYLEKFDLPINKSIK----------------------TFSTGMKMKLSLAVAFSH 145
Cdd:PRK10982 331 ERRSTGIYAYLDIGFNSLISN--IRNYKNKVGLLDNSRMKsdtqwvidsmrvktpghrtqigSLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 146 HAELYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-205 |
1.07e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 42.76 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIR--------------VLEEDMALNP-------IELKNR 76
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvegpgaergVVFQNEGLLPwrnvqdnVAFGLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 77 IGFVYSEnyfnERWTTKQleKMIApfyrKWDhqvfefyLEKFDlpiNKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:PRK11248 97 LAGVEKM----QRLEIAH--QMLK----KVG-------LEGAE---KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 577230680 157 SGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDG 205
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-218 |
1.22e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 42.75 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIM--DLYQPQTGVIRVLEED---------------MAL-NPIELKNrigf 79
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDilelspderaragifLAFqYPVEIPG---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFNERWTTKQLEKMIAPFYRKwdhQVFEfYLEKFDLP---INKSI-KTFSTG---------MKM-KLSLAvafsh 145
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSAREFLK---LLKE-KMKELGLDedfLDRYVnEGFSGGekkrneilqMLLlEPKLA----- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 146 haelyIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHiisdLEKIADYI----IH-LSDGEVILNGSKEQLLQ 218
Cdd:COG0396 163 -----ILDETDSGLDIDALRIVAEGV-NKLRSPDRGILIITH----YQRILDYIkpdfVHvLVDGRIVKSGGKELALE 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
129-238 |
1.35e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.79 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 129 FSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIqQELIDE-NKTIFMSTHIISDLEKIADYIIHLSDGEV 207
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLL-NELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
90 100 110
....*....|....*....|....*....|....*.
gi 577230680 208 ILNGSKEQLLQR----YQV-VSGAIEDLDDELASLL 238
Cdd:PRK09473 241 MEYGNARDVFYQpshpYSIgLLNAVPRLDAEGESLL 276
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-208 |
1.95e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.68 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALN-P---------I---ELkNRIG-FVYSE 83
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgPkssqeagigIihqEL-NLIPqLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 NYF-----NERWTTKQLEKMiapfYRKWDHqvfefYLEKFDLPIN--KSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPT 156
Cdd:PRK10762 99 NIFlgrefVNRFGRIDWKKM----YAEADK-----LLARLNLRFSsdKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 577230680 157 SGLDPLARNELLEIIqQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVI 208
Cdd:PRK10762 170 DALTDTETESLFRVI-RELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-219 |
2.47e-04 |
|
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: 42.36 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLyQPQTGVIRVLEEDM------ALNPieLKNRIGFVYSENY--FNER 89
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglsrrALRP--LRRRMQVVFQDPFgsLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 90 WTTKQL--EKM----IAPFYRKWDHQVFEFyLEKFDLP---INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLD 160
Cdd:COG4172 379 MTVGQIiaEGLrvhgPGLSAAERRARVAEA-LEEVGLDpaaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577230680 161 PLARN---ELLEIIQQELideNKT-IFMStHiisDL---EKIADYIIHLSDGEVILNGSKEQLLQR 219
Cdd:COG4172 458 VSVQAqilDLLRDLQREH---GLAyLFIS-H---DLavvRALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
149-211 |
3.15e-04 |
|
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: 41.09 E-value: 3.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 149 LYIFDEPTSGLDPLARNELLEIIqQELIDENKTIFMSTHiisDLEKI--ADYIIHLS------DGEVILNG 211
Cdd:cd03270 160 LYVLDEPSIGLHPRDNDRLIETL-KRLRDLGNTVLVVEH---DEDTIraADHVIDIGpgagvhGGEIVAQG 226
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-60 |
3.22e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 41.26 E-value: 3.22e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 577230680 1 MNAI-ELSNVNYSSDQFN-LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIR 60
Cdd:COG4674 7 HGPIlYVEDLTVSFDGFKaLNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVL 68
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
149-218 |
3.45e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 3.45e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 149 LYIFDEPTSGL--DPLARneLLEIIqQELIDENKTIFMSTHIIsDLEKIADYIIHL------SDGEVILNGSKEQLLQ 218
Cdd:PRK00349 854 LYILDEPTTGLhfEDIRK--LLEVL-HRLVDKGNTVVVIEHNL-DVIKTADWIIDLgpeggdGGGEIVATGTPEEVAK 927
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-187 |
3.61e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 2 NAIELSNVNYS-SDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIM-DlyQPQTgvirvLEEDMAL--------NPI 71
Cdd:PRK10938 259 PRIVLNNGVVSyNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgD--HPQG-----YSNDLTLfgrrrgsgETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 72 -ELKNRIGFVYSENYFNERWTTKQLEKMIAPF------YRKWD---HQVFEFYLEKFDLP---INKSIKTFSTGMKMKLS 138
Cdd:PRK10938 332 wDIKKHIGYVSSSLHLDYRVSTSVRNVILSGFfdsigiYQAVSdrqQKLAQQWLDILGIDkrtADAPFHSLSWGQQRLAL 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 577230680 139 LAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKT--IFMSTH 187
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDV-LISEGETqlLFVSHH 461
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
128-205 |
5.33e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 128 TFSTGMKMKLSLAVAFSHHAE--LYIFDEPTSGLDPLARNELLEIIqQELIDENKTIfmsthIISD----LEKIADYIIH 201
Cdd:PRK00635 1387 TLSDGEHYRLHLAKKISSNLTdiIYLLEDPLSGLHPQDAPTLLQLI-KELVTNNNTV-----IATDrsgsLAEHADHLIH 1460
|
....
gi 577230680 202 LSDG 205
Cdd:PRK00635 1461 LGPG 1464
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-67 |
5.42e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 40.83 E-value: 5.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA 67
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLA 77
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
118-217 |
6.29e-04 |
|
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: 40.66 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 118 FDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDenKTIFMSTHIISDLEKiAD 197
Cdd:cd03288 146 LDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVSTILD-AD 222
|
90 100
....*....|....*....|
gi 577230680 198 YIIHLSDGEVILNGSKEQLL 217
Cdd:cd03288 223 LVLVLSRGILVECDTPENLL 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-220 |
7.22e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMD--LYQPQTGVIRVLEEDMALNPIELKNRIGFVYSENY---------- 85
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIFLAFQYpieipgvsna 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 86 ------FNERWTTKQLEKMIAPFYrkwdhqvFEFYLEKFDLP------INKSI-KTFSTGMKMK---LSLAVAFShhaEL 149
Cdd:CHL00131 103 dflrlaYNSKRKFQGLPELDPLEF-------LEIINEKLKLVgmdpsfLSRNVnEGFSGGEKKRneiLQMALLDS---EL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577230680 150 YIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIA-DYIIHLSDGEVILNGSKE--QLLQRY 220
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINK-LMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAElaKELEKK 245
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
136-217 |
7.29e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.56 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 136 KLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQ 215
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
..
gi 577230680 216 LL 217
Cdd:PRK15093 246 LV 247
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-171 |
7.33e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 4 IELSNVNYSSDQFNLKNISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVleEDMALNPIElKNRIGFVYSE 83
Cdd:PRK13541 2 LSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIA-KPYCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 84 NYFNERWTTKQLEKMIAPFYRKWDHQVFEFYLEKFDLPINKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLA 163
Cdd:PRK13541 79 LGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158
|
....*...
gi 577230680 164 RNELLEII 171
Cdd:PRK13541 159 RDLLNNLI 166
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
18-218 |
1.05e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 39.81 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTTIIR-LIMDLYQPQ-------TGVIRVLEEDMA-LNPIEL---------KNRIGF 79
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGaprgarvTGDVTLNGEPLAaIDAPRLarlravlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 80 VYSENYFNERWTTKQLEKMIAPFYRkwDHQVFEFYLEKFDLP--INKSIKTFSTGMKMKLSLAVAFSH----HAEL---- 149
Cdd:PRK13547 97 AFSAREIVLLGRYPHARRAGALTHR--DGEIAWQALALAGATalVGRDVTTLSGGELARVQFARVLAQlwppHDAAqppr 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 150 -YIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVILNGSKEQLLQ 218
Cdd:PRK13547 175 yLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
91-187 |
1.20e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 91 TTKQLEKMIAPFYRKWDHQVFEFYLEKFDLPINKSikTFSTGMKMKLSLAVAFS---HHAELYIFDEPTSGLDPLARNEL 167
Cdd:pfam13304 201 DLGEGIEKSLLVDDRLRERGLILLENGGGGELPAF--ELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRL 278
|
90 100
....*....|....*....|
gi 577230680 168 LEIIqQELIDENKTIFMSTH 187
Cdd:pfam13304 279 LELL-KELSRNGAQLILTTH 297
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-72 |
1.39e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.93 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 577230680 4 IELSNVNYSSD-QFNLKNISFKVPQG-FVTgFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMALNPIE 72
Cdd:PRK09452 15 VELRGISKSFDgKEVISNLDLTINNGeFLT-LLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
149-202 |
2.15e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 149 LYIFDEPTSGL--DPLARneLLEIIQQeLIDENKTIFMSTH---IIsdleKIADYIIHL 202
Cdd:COG0178 850 LYILDEPTTGLhfHDIRK--LLEVLHR-LVDKGNTVVVIEHnldVI----KTADWIIDL 901
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-216 |
2.18e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.30 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 18 LKNISFKVPQGFVTGFIGRNGAGKTT----IIRLImdlyqPQTGVIrvLEEDMALNP------IELKNRIGFVYSENY-- 85
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEI--WFDGQPLHNlnrrqlLPVRHRIQVVFQDPNss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 86 FNERWTTKQL--------EKMIAPFYRkwDHQVFEFYLE-------KFDLPinksiKTFSTGMKMKLSLAVAFSHHAELY 150
Cdd:PRK15134 375 LNPRLNVLQIieeglrvhQPTLSAAQR--EQQVIAVMEEvgldpetRHRYP-----AEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577230680 151 IFDEPTSGLDPLARNELLEIIQQeLIDENKT--IFMStHIISDLEKIADYIIHLSDGEVILNGSKEQL 216
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKS-LQQKHQLayLFIS-HDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
122-202 |
2.20e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 122 INKSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDplarneLLEIIQQE--LIDENKTIFMSTHIISDLEKIADYI 199
Cdd:PRK10636 143 LERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD------LDAVIWLEkwLKSYQGTLILISHDRDFLDPIVDKI 216
|
...
gi 577230680 200 IHL 202
Cdd:PRK10636 217 IHI 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-67 |
2.42e-03 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 38.25 E-value: 2.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 577230680 20 NISFKVPQGFVTGFIGRNGAGKTTIIRLIMDLYQPQTGVIRVLEEDMA 67
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR 66
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
130-219 |
2.54e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.53 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 130 STGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHLSDGEVIL 209
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
90
....*....|
gi 577230680 210 NGSKEQLLQR 219
Cdd:PRK10418 222 QGDVETLFNA 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
130-221 |
2.65e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.30 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 130 STGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEI---IQQELideNKTIFMSTHIISDLEKIADYIIHLSDGE 206
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLlreLQQEL---NMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
90
....*....|....*
gi 577230680 207 VILNGSKEQLLQRYQ 221
Cdd:PRK15134 235 CVEQNRAATLFSAPT 249
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
124-202 |
3.42e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 3.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577230680 124 KSIKTFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLArnelLEIIQQELIDENKTIFMSTHIISDLEKIADYIIHL 202
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA----VLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHL 414
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
149-226 |
4.03e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 149 LYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHiisDLEKI--ADYIIHLS------DGEVILNGSKEQLLQRY 220
Cdd:TIGR00630 511 LYVLDEPSIGLHQRDNRRLINTLKR-LRDLGNTLIVVEH---DEDTIraADYVIDIGpgagehGGEVVASGTPEEILANP 586
|
....*.
gi 577230680 221 QVVSGA 226
Cdd:TIGR00630 587 DSLTGQ 592
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
119-227 |
5.90e-03 |
|
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: 37.88 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577230680 119 DLPINKsiktFSTGMKMKLSLAVAFSHHAELYIFDEPTSGLDPLARNELLEIIQQeLIDENKTIFMSTHIISDLEKIADY 198
Cdd:TIGR02633 398 FLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQ-LAQEGVAIIVVSSELAEVLGLSDR 472
|
90 100
....*....|....*....|....*....
gi 577230680 199 IIHLSDGEVILNGSKEQLLQRyQVVSGAI 227
Cdd:TIGR02633 473 VLVIGEGKLKGDFVNHALTQE-QVLAAAL 500
|
|
| |
