|
Name |
Accession |
Description |
Interval |
E-value |
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-223 |
3.10e-48 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 167.34 E-value: 3.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 2 VIQAIGLTSASRGeePPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPA-GAVGV 79
Cdd:COG4555 1 MIEVENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAgLLKPDSGSILIDGEDVRKEPREArRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 LLGDVPGHPSRTARGHLRMLAA----AAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDD 155
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAElyglFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 156 PAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRRRLRP 223
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-221 |
4.81e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 4.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRG-ITLFGGRPLHRHTHPAGAVGVLLGDVPGHPSRTARGH 95
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLlRPTSGeVRVLGEDVARDPAEVRRRIGYVPQEPALYPDLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 96 LRMLAA----AAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGL 171
Cdd:COG1131 94 LRFFARlyglPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517388152 172 LKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRRRL 221
Cdd:COG1131 174 LRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-210 |
2.59e-40 |
|
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: 145.05 E-value: 2.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRG--ITLFGGRPLHRHThPAGAVGVLLgDVPG-HPSRTARG 94
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSgeITFDGKSYQKNIE-ALRRIGALI-EAPGfYPNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 95 HLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKA 174
Cdd:cd03268 92 NLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILS 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 517388152 175 YAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03268 172 LRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-206 |
1.93e-31 |
|
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: 120.66 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 1 MVIQAIGLtSASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHT-HPAGAVG 78
Cdd:COG4133 1 MMLEAENL-SCRRGERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLlPPSAGEVLWNGEPIRDAReDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 VLLGDVPGHPSRTARGHLRMLAAA--AGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALygLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAgrLGDRVVTLDKGR 206
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-207 |
9.64e-30 |
|
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: 114.80 E-value: 9.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRG-ITLFGGRPLHRHTHPAGAVGVLLGDVPGHPSRTARGH 95
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLlKPDSGeIKVLGKDIKKEPEEVKRRIGYLPEEPSLYENLTVREN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 96 LRmlaaaagapaeradqvleivglretagrrlstFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAY 175
Cdd:cd03230 94 LK--------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL 141
|
170 180 190
....*....|....*....|....*....|..
gi 517388152 176 AARGGAVVVTCADPKAAGRLGDRVVTLDKGRL 207
Cdd:cd03230 142 KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-209 |
7.30e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 113.75 E-value: 7.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRlML--ELEPGRGITLFGGRPLHRHTHpagAVGVL 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLK-MLtgELRPTSGTAYINGYSIRTDRK---AARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 LGDVPGH----PSRTARGHLRMLA----AAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALL 152
Cdd:cd03263 77 LGYCPQFdalfDELTVREHLRFYArlkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 153 LDDPAQGLSPHDTAWLYGLLKAYaARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVA 209
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-210 |
5.47e-26 |
|
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: 104.44 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPAGA--VGVLLgdvpghpsrtarg 94
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAgLLKPSSGEILLDGKDLASLSPKELArkIAYVP------------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 95 hlrmlaaaagapaeradQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKA 174
Cdd:cd03214 80 -----------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
|
170 180 190
....*....|....*....|....*....|....*..
gi 517388152 175 YAA-RGGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03214 143 LAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
19-215 |
3.44e-25 |
|
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: 103.60 E-value: 3.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEP---GRGiTLFGGRPLHRHTHPAGAVGVLLGDVPGHPSRTARGH 95
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsGRA-TVAGHDVVREPREVRRRIGIVFQDLSVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 96 L----RMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGL 171
Cdd:cd03265 94 LyihaRLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517388152 172 LKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:cd03265 174 IEKLKEEFGmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-210 |
4.26e-24 |
|
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: 100.52 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEEPP--AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGrpLHRHTHPAGA--- 76
Cdd:cd03266 2 ITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlEPDAGFATVDG--FDVVKEPAEArrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 77 VGVLLGDVPGHPSRTARGHL----RMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALL 152
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLeyfaGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 153 LDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
18-209 |
5.36e-24 |
|
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: 99.92 E-value: 5.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRG-ITLFGGrplhrhthPAGAVGVLLGDVPGHPS------ 89
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLlKPTSGsIRVFGK--------PLEKERKRIGYVPQRRSidrdfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 90 -------RTAR-GHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS 161
Cdd:cd03235 85 isvrdvvLMGLyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517388152 162 PHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKgRLVA 209
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNR-TVVA 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-272 |
9.75e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.64 E-value: 9.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRGITLFGGRPLHRHTH----------------PAGAVGVLL 81
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGiLAPDSGEVLWDGEPLDPEDRrrigylpeerglypkmKVGEQLVYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 82 GDVPGHPSRTARghlrmlaaaagapaERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS 161
Cdd:COG4152 96 ARLKGLSKAEAK--------------RRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 162 PHDTAWLYGLLKAYAARGGAVV--------VTcadpkaagRLGDRVVTLDKGRLVADQSAHE----FGRRRLRpyvaVHS 229
Cdd:COG4152 162 PVNVELLKDVIRELAAKGTTVIfsshqmelVE--------ELCDRIVIINKGRKVLSGSVDEirrqFGRNTLR----LEA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 517388152 230 PQAerLGLLLTDDGTEITHESGSRIRV---HGATTAQVGEAAFRNG 272
Cdd:COG4152 230 DGD--AGWLRALPGVTVVEEDGDGAELkleDGADAQELLRALLARG 273
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-215 |
3.61e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.59 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 1 MVIQAIGLTSASRGEepPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPAGA-VG 78
Cdd:PRK13536 40 VAIDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMtSPDAGKITVLGVPVPARARLARArIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 VLLGDVPGHPSRTARGHL----RMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLD 154
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLlvfgRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517388152 155 DPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHA 258
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-215 |
9.72e-22 |
|
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: 94.04 E-value: 9.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHT-HPAGAVGV--------LLGD----- 83
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISgFLRPTSGSVLFDGEDITGLPpHEIARLGIgrtfqiprLFPEltvle 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 84 ---VPGHPSRTARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGL 160
Cdd:cd03219 95 nvmVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 161 SPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:cd03219 175 NPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-206 |
3.12e-21 |
|
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: 92.14 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLM-LELEPGRGITLFGGRPLHRHTHP--AGAVGVLLGDvpghPSR 90
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLnGLLGPTSGEVLVDGKDLTKLSLKelRRKVGLVFQN----PDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 91 -----TARG----HLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS 161
Cdd:cd03225 87 qffgpTVEEevafGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517388152 162 PHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGR 206
Cdd:cd03225 167 PAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-215 |
3.88e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.10 E-value: 3.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPAGA-VGVllgdVPG----HPSRTAR 93
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLtHPDAGSISLCGEPVPSRARHARQrVGV----VPQfdnlDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 94 GHL----RMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLY 169
Cdd:PRK13537 99 ENLlvfgRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 517388152 170 GLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13537 179 ERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHA 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-216 |
5.78e-21 |
|
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: 91.63 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLtSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLM--LeLEPGRGITLFGGRPLHRHTHPAGA--VG 78
Cdd:COG1122 1 IELENL-SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngL-LKPTSGEVLVDGKDITKKNLRELRrkVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 VL-------------LGDV---P---GHPSRTARghlrmlaaaagapaERADQVLEIVGLRETAGRRLSTFSLGMDRRLG 139
Cdd:COG1122 79 LVfqnpddqlfaptvEEDVafgPenlGLPREEIR--------------ERVEEALELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 140 VAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
19-209 |
6.28e-21 |
|
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: 91.19 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRGITLFGGRPL---HRHT----------HPAGAVG---VLL 81
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDGKPLdiaARNRigylpeerglYPKMKVIdqlVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 82 GDVPGHPSRTARghlrmlaaaagapaERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS 161
Cdd:cd03269 95 AQLKGLKKEEAR--------------RRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517388152 162 PHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVA 209
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
18-216 |
6.65e-21 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRhthPAGAVG------------------ 78
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILgLLPPTSGTVRLFGKPPRR---ARRRIGyvpqraevdwdfpitvrd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 -VLLGdvpghpsrtARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPA 157
Cdd:COG1121 97 vVLMG---------RYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPF 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 158 QGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKgRLVADQSAHEF 216
Cdd:COG1121 168 AGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-209 |
8.93e-21 |
|
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: 90.66 E-value: 8.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGAVGVLLGDVPGHPSRTARGH- 95
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLErPDSGEILIDGRDVTGVPPERRNIGMVFQDYALFPHLTVAENi 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 96 ---LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLL 172
Cdd:cd03259 94 afgLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREEL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 517388152 173 KAYAARGG--AVVVTcADPKAAGRLGDRVVTLDKGRLVA 209
Cdd:cd03259 174 KELQRELGitTIYVT-HDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-206 |
1.05e-20 |
|
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: 88.84 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 16 EPPAVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLHRHTHPagavgvllgdvpghpsrtarg 94
Cdd:cd00267 11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRaIAGLLKPTSGEILIDGKDIAKLPLE--------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 95 hlrmlaaaagapaeradQVLEIVGLretagrrLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKA 174
Cdd:cd00267 70 -----------------ELRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|..
gi 517388152 175 YAARGGAVVVTCADPKAAGRLGDRVVTLDKGR 206
Cdd:cd00267 126 LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
19-162 |
1.13e-20 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 90.33 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGeITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPA-GAVGVLLGDVPGHPSRTARGHL 96
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILAtLTPPSSGTIRIDGQDVLKQPQKLrRRIGYLPQEFGVYPNFTVREFL 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 97 RMLAA----AAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:cd03264 94 DYIAWlkgiPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDP 163
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
19-210 |
1.87e-20 |
|
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: 90.87 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHR----------------HTHPAGAVGVL- 80
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITgFYRPTSGRILFDGRDITGlpphriarlgiartfqNPRLFPELTVLe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 ---LGDVPGHPSRTARGHLRMLAAAAGAPAERA--DQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDD 155
Cdd:COG0411 99 nvlVAAHARLGRGLLAALLRLPRARREEREAREraEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 156 PAQGLSPHDTAWLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-156 |
8.39e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 86.16 E-value: 8.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHR--HTHPAGAVGVLLGDVPGHPSRTARGHL 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAgLLSPTEGTILLDGQDLTDdeRKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 97 RMLAAAAGAPAERADQ----VLEIVGLRETAGRRL----STFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:pfam00005 81 RLGLLLKGLSKREKDAraeeALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-215 |
1.17e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 88.63 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPAGA--------------------Vg 78
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTgELTPSSGEVRLNGRPLAAWSPWELArrravlpqhsslafpftveeV- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 VLLGDVPGHPSRTARGHLrmlaaaagapaerADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALL-------GDPPAL 151
Cdd:COG4559 96 VALGRAPHGSSAAQDRQI-------------VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517388152 152 LLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:COG4559 163 FLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-208 |
2.07e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 86.54 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHpAGAVGVLLGDVPGHP 88
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLiKESSGSILLNGKPIKAKER-RKSIGYVMQDVDYQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 -SRTARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAW 167
Cdd:cd03226 85 fTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517388152 168 LYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
2.33e-19 |
|
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: 91.12 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 2 VIQAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPG----RGITLFGGRPLHRHTHP--AG 75
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggriSGEVLLDGRDLLELSEAlrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 76 AVGVLLGD-----VPGHPSRTARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPA 150
Cdd:COG1123 84 RIGMVFQDpmtqlNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 151 LLLDDPAQGLSPHDTAWLYGLLKA-YAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRR 219
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-213 |
2.50e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.64 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPAGA-----VGV------LL 81
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYgEERPTSGQVLVNGQDLSRLKRREIPylrrrIGVvfqdfrLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 82 GD------------VPGHPSRTARGHLRmlaaaagapaeradQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPP 149
Cdd:COG2884 92 PDrtvyenvalplrVTGKSRKEIRRRVR--------------EVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 150 ALLLDDPAQGLSPhDTAW-LYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSA 213
Cdd:COG2884 158 LLLADEPTGNLDP-ETSWeIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
10-226 |
3.68e-19 |
|
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: 86.97 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRP--------LHRHthpagaVGVL 80
Cdd:cd03295 7 TKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEIFIDGEDireqdpveLRRK------IGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 LGDVPGHPSRTARGH----LRMLAAAAGAPAERADQVLEIVGL--RETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLD 154
Cdd:cd03295 81 IQQIGLFPHMTVEENialvPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517388152 155 DPAQGLSPHDTAWLYG-LLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRRRLRPYVA 226
Cdd:cd03295 161 EPFGALDPITRDQLQEeFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVA 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-208 |
3.68e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.47 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 22 DLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGIT----LFGGRPLHRHTHPAgAVGVLLGDVPGHPSRTARGHLR 97
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTsgqiLFNGQPRKPDQFQK-CVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 98 ---MLAAAAGAPAERADQVLEIVGLRETA-----GRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLY 169
Cdd:cd03234 104 ytaILRLPRKSSDAIRKKRVEDVLLRDLAltrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517388152 170 GLLKAYAARGGAVVVTCADPKA-AGRLGDRVVTLDKGRLV 208
Cdd:cd03234 184 STLSQLARRNRIVILTIHQPRSdLFRLFDRILLLSSGEIV 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-210 |
9.29e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 83.28 E-value: 9.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 1 MVIQAIGLtSASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPAGA--V 77
Cdd:PRK13548 1 AMLEARNL-SVRLGGRT-LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSPDSGEVRLNGRPLADWSPAELArrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 GVLlgdvPGHPSR----TARGHLRM----LAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALL---- 145
Cdd:PRK13548 79 AVL----PQHSSLsfpfTVEEVVAMgrapHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 146 --GDPPALLLDDPAQGLSPHDTAWLYGLLKAYA-ARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-210 |
1.71e-17 |
|
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: 81.36 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGAV---G 78
Cdd:cd03293 3 VRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLErPTSGEVLVDGEPVTGPGPDRGYVfqqD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 VLLgdvpghPSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLD 154
Cdd:cd03293 83 ALL------PWLTVLDNvalgLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 155 DPAQGLSPHDTAWLYG-LLKAYAARGGAVV-VTcADPKAAGRLGDRVVTLDK--GRLVAD 210
Cdd:cd03293 157 EPFSALDALTREQLQEeLLDIWRETGKTVLlVT-HDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-210 |
2.08e-17 |
|
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: 81.61 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 15 EEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRG-ITLFGGRPLHRHTHPAGAVGVLLG-------DVP 85
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTSGeVRVAGLVPWKRRKKFLRRIGVVFGqktqlwwDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 86 ghPSRTARGHLRMLAAAAGAPAERADQV---LEIVGLRETAGRRLstfSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:cd03267 112 --VIDSFYLLAAIYDLPPARFKKRLDELselLDLEELLDTPVRQL---SLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517388152 163 HDTAWLYGLLKAYAA-RGGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03267 187 VAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-208 |
2.12e-17 |
|
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: 82.31 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPAgavgvlLGDVPGH--------- 87
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLiEPTSGKVLIDGQDIAAMSRKE------LRELRRKkismvfqsf 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 88 ---PSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGL 160
Cdd:cd03294 112 allPHRTVLENvafgLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517388152 161 SP------HDTawlygLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:cd03294 192 DPlirremQDE-----LLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-216 |
8.46e-17 |
|
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: 79.40 E-value: 8.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLHRH-THPAGAVGVLLgdVP-GH---PSRT 91
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGY--VPeGRrifPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGHLRM--LAAAAGAPAERADQVLEIV-GLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWL 168
Cdd:cd03224 92 VEENLLLgaYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 517388152 169 YGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:cd03224 172 FEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
10-185 |
1.33e-16 |
|
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: 78.17 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPAGAVGVLLGDVPG-H 87
Cdd:TIGR01189 7 ACSRGERM-LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLlRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGlK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 88 PSRTARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAW 167
Cdd:TIGR01189 86 PELSALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170
....*....|....*...
gi 517388152 168 LYGLLKAYAARGGAVVVT 185
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLT 183
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-207 |
3.49e-16 |
|
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: 77.53 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLH----------RHTHpagaVGV------L 80
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDrPTSGEVRVDGTDISklsekelaafRRRH----IGFvfqsfnL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 LgdvpghPSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:cd03255 94 L------PDLTALENvelpLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAA-RGGAVVVTCADPKAAgRLGDRVVTLDKGRL 207
Cdd:cd03255 168 TGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-207 |
4.39e-16 |
|
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: 81.98 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHpagAVGVLLGDVPGHP----SRTA 92
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLlPPTSGTVLVGGKDIETNLD---AVRQSLGMCPQHNilfhHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 93 RGHL----RMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWL 168
Cdd:TIGR01257 1021 AEHIlfyaQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|....*....
gi 517388152 169 YGLLKAYAArGGAVVVTCADPKAAGRLGDRVVTLDKGRL 207
Cdd:TIGR01257 1101 WDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-207 |
4.64e-16 |
|
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: 77.06 E-value: 4.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRP---LHRHTHP--AGAVGVLLGDVPGHPSRT 91
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYkEELPTSGTIRVNGQDvsdLRGRAIPylRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAW 167
Cdd:cd03292 95 VYENvafaLEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517388152 168 LYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRL 207
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
10-222 |
5.60e-16 |
|
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: 77.61 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRG-ITLFG-------GRPLHRHTHPAGAV--- 77
Cdd:cd03256 7 SKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLvEPTSGsVLIDGtdinklkGKALRQLRRQIGMIfqq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 -----------GVLLGDVPGHPsrTARGHLRMLAAAAGAPAEradQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLG 146
Cdd:cd03256 87 fnlierlsvleNVLSGRLGRRS--TWRSLFGLFPKEEKQRAL---AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 147 DPPALLLDDPAQGLSPHDTAWLYGLLKAYA-ARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRRRLR 222
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
21-216 |
7.28e-16 |
|
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: 77.16 E-value: 7.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 21 DDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHThPAGA------VGVL-----------LG 82
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVgLLRPDSGEVLIDGEDISGLS-EAELyrlrrrMGMLfqsgalfdsltVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 83 DVPGHPSRTargHLRMLAAAAGAPAEradQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:cd03261 96 ENVAFPLRE---HTRLSEEEIREIVL---EKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 163 HDTAWLYGLLKAYAARGGA--VVVTcADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:cd03261 170 IASGVIDDLIRSLKKELGLtsIMVT-HDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-224 |
7.34e-16 |
|
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: 80.33 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 2 VIQAIGLT---SASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHP---- 73
Cdd:COG1123 260 LLEVRNLSkryPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrPTSGSILFDGKDLTKLSRRslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 74 -AGAVGVLLGDvPGH---PSRT-----ARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRL-STFSLGMDRRLGVAAA 143
Cdd:COG1123 340 lRRRVQMVFQD-PYSslnPRMTvgdiiAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYpHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 144 LLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRRRLR 222
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGlTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
..
gi 517388152 223 PY 224
Cdd:COG1123 499 PY 500
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-208 |
9.81e-16 |
|
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: 76.39 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 12 SRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLH-----RHTHPAGAVGVLLGDVP 85
Cdd:cd03257 13 TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLklsrrLRKIRRKEIQMVFQDPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 86 G--HPSRTARGHLR-MLAAAAGAP-----AERADQVLEIVGLRETAGRRL-STFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:cd03257 93 SslNPRMTIGEQIAePLRIHGKLSkkearKEAVLLLLVGVGLPEEVLNRYpHELSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517388152 157 AQGLSPhDTAW--LYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:cd03257 173 TSALDV-SVQAqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
19-206 |
1.53e-15 |
|
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: 74.53 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGA----VGVLLGDVPGHPSRTar 93
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEePDSGSILIDGEDLTDLEDELPPlrrrIGMVFQDFALFPHLT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 94 ghlrmlaaaagapaeradqVLEIVGLRetagrrlstFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLK 173
Cdd:cd03229 93 -------------------VLENIALG---------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
170 180 190
....*....|....*....|....*....|....
gi 517388152 174 AYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGR 206
Cdd:cd03229 145 SLQAQLGiTVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
19-216 |
8.10e-15 |
|
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: 73.75 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRL---MLELEPGR---GITLFGGRPLhrhthPAGAVGVLL-----GDVPGH 87
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLlnrLNDLIPGApdeGEVLLDGKDI-----YDLDVDVLElrrrvGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 88 PS---RTARGHLRM-LAAAAGAPAERAD----QVLEIVGLRETAGRRLSTFSL--GMDRRLGVAAALLGDPPALLLDDPA 157
Cdd:cd03260 90 PNpfpGSIYDNVAYgLRLHGIKLKEELDerveEALRKAALWDEVKDRLHALGLsgGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 158 QGLSPHDTAWLYGLLKAYAARGGAVVVTcADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:cd03260 170 SALDPISTAKIEELIAELKKEYTIVIVT-HNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-210 |
1.60e-14 |
|
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: 73.58 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRG--ITLFGGRP------------------LH 68
Cdd:COG1119 10 TVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGndVRLFGERRggedvwelrkriglvspaLQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 69 rHTHPAGAVG---VLLG--DVPG---HPSRTARGHLRmlaaaagapaeradQVLEIVGLRETAGRRLSTFSLGMDRRLGV 140
Cdd:COG1119 89 -LRFPRDETVldvVLSGffDSIGlyrEPTDEQRERAR--------------ELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 141 AAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGA--VVVTcadpkaaGRLGD------RVVTLDKGRLVAD 210
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtlVLVT-------HHVEEippgitHVLLLKDGRVVAA 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-216 |
1.96e-14 |
|
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: 73.09 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 2 VIQAIGLTSaSRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPA------ 74
Cdd:COG1127 5 MIEVRNLTK-SFGDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIgLLRPDSGEILVDGQDITGLSEKElyelrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 75 --------GA----------VGVLLGDVPGHPSRTARGHLRMlaaaagapaeradqVLEIVGLRETAGRRLSTFSLGMDR 136
Cdd:COG1127 83 rigmlfqgGAlfdsltvfenVAFPLREHTDLSEAEIRELVLE--------------KLELVGLPGAADKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 137 RLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGA--VVVTcADPKAAGRLGDRVVTLDKGRLVADQSAH 214
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLtsVVVT-HDLDSAFAIADRVAVLADGKIIAEGTPE 227
|
..
gi 517388152 215 EF 216
Cdd:COG1127 228 EL 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
3-215 |
3.17e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRgeeppaVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITLFGGRPL----------HR--- 69
Cdd:COG4138 1 LQLNDVAVAGR------LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLsdwsaaelarHRayl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 70 --HTHPAGAVGVL----LGdVPGHPSRTARGHLrmlaaaagapaerADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAA 143
Cdd:COG4138 75 sqQQSPPFAMPVFqylaLH-QPAGASSEAVEQL-------------LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 144 LL-----GDPPA--LLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:COG4138 141 LLqvwptINPEGqlLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-210 |
5.23e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 69.76 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLHRHThPAGAVgvllgdvpghpsrtARGhl 96
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKiLSGLYKPDSGEILVDGKEVSFAS-PRDAR--------------RAG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 97 rmlaaaagapaeradqvLEIVglretagrrlSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYA 176
Cdd:cd03216 77 -----------------IAMV----------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR 129
|
170 180 190
....*....|....*....|....*....|....
gi 517388152 177 ARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03216 130 AQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-215 |
6.25e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.97 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPL----------------HRHTH 72
Cdd:PRK11231 9 TVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKcFARLLTPQSGTVFLGDKPIsmlssrqlarrlallpQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 73 PAG-AVGVLL--GDVPghpsrtargHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPP 149
Cdd:PRK11231 88 PEGiTVRELVayGRSP---------WLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 150 ALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-291 |
6.40e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRlMLE--LEPGRG-ITLFGGRPLHRHTHPAGAVGVLLG-------DVP--- 85
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIK-MLTgiLVPTSGeVRVLGYVPFKRRKEFARRIGVVFGqrsqlwwDLPaid 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 86 ---------GHPSRTARGHLRMLaaaagapaeraDQVLEIVGLRETAGRRLstfSLG--MdrRLGVAAALLGDPPALLLD 154
Cdd:COG4586 116 sfrllkaiyRIPDAEYKKRLDEL-----------VELLDLGELLDTPVRQL---SLGqrM--RCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 155 DPAQGLSPHDTAWLYGLLKAYAARGGA-VVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFgRRRLRPYVAVHSPQAE 233
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTtILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEEL-KERFGPYKTIVLELAE 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 234 RLGLLLTDDGTEITHESGSRIRVHGATTAQVGEaafrngiLLHRLAD--EVADTGVPEAP 291
Cdd:COG4586 259 PVPPLELPRGGEVIEREGNRVRLEVDPRESLAE-------VLARLLAryPVRDLTIEEPP 311
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
16-235 |
6.88e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.23 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 16 EPPAVDDLSFDARPGEITVLLGDGGAG--KSTVLRLMLELEPGRgitlfggRPLHRHTHPAGAVGVLLGDVPGHPSRTAR 93
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR-------RPWRF*TWCANRRALRRTIG*HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 94 GHL-----------RMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:NF000106 98 RESfsgrenlymigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 163 HDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEF-----GRR-RLRPyvaVHSPQAERL 235
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELktkvgGRTlQIRP---AHAAELDRM 253
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-208 |
8.12e-14 |
|
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: 71.07 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-P--------GRGITLFGG---RPLHRH 70
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLErPtsgsvlvdGTDLTLLSGkelRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 71 thpagavgvlLGDVPGH----PSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAA 142
Cdd:cd03258 84 ----------IGMIFQHfnllSSRTVFENvalpLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 143 ALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-210 |
9.54e-14 |
|
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: 70.70 E-value: 9.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLhRHTHPAgavgVL---LGDVPGHPS 89
Cdd:cd03245 14 NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLyKPTSGSVLLDGTDI-RQLDPA----DLrrnIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 90 RTArGHLR--MLAAAAGAPAERADQVLEIVGLRETAGRRlstfSLGMDRRLG---------------VAAALLGDPPALL 152
Cdd:cd03245 89 LFY-GTLRdnITLGAPLADDERILRAAELAGVTDFVNKH----PNGLDLQIGergrglsggqrqavaLARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 153 LDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTcaDPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDKTLIIIT--HRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-215 |
1.02e-13 |
|
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: 73.65 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPA--GAVGV 79
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrFLDPQSGSITLGGVDLRDLDEDDlrRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 llgdVPGHP---SRTARGHLRMlaaaagAPAERAD----QVLEIVGLRET--------------AGRRLSTfslGMDRRL 138
Cdd:COG4987 414 ----VPQRPhlfDTTLRENLRL------ARPDATDeelwAALERVGLGDWlaalpdgldtwlgeGGRRLSG---GERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 139 GVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTcADPKAAGRlGDRVVTLDKGRLVADQSAHE 215
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLIT-HRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
8-205 |
1.26e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 74.28 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 8 LTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHThpaGAVGVLLGDVPG 86
Cdd:TIGR01257 1943 LTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTgDTTVTSGDATVAGKSILTNI---SDVHQNMGYCPQ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 87 HPS----RTARGHLRMLAAAAGAPAERADQV----LEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQ 158
Cdd:TIGR01257 2020 FDAiddlLTGREHLYLYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTT 2099
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517388152 159 GLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKG 205
Cdd:TIGR01257 2100 GMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-162 |
3.38e-13 |
|
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: 68.11 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHP-AGAVGVLlgdvpghpsrT 91
Cdd:cd03247 12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTgDLKPQQGEITLDGVPVSDLEKAlSSLISVL----------N 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517388152 92 ARGHLRMlaaaagapaeradqvleiVGLRETAGRRlstFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:cd03247 82 QRPYLFD------------------TTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-208 |
4.12e-13 |
|
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: 68.80 E-value: 4.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGAVGVLLGDVPGHPSRT----- 91
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFEtPTSGEILLDGKDITNLPPHKRPVNTVFQNYALFPHLTvfeni 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGhLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGL 171
Cdd:cd03300 94 AFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 517388152 172 LKAYAARGGA--VVVTcADPKAAGRLGDRVVTLDKGRLV 208
Cdd:cd03300 173 LKRLQKELGItfVFVT-HDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-210 |
5.21e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 68.09 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 22 DLSFDArPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPL-----HRHTHPAG-AVGVLLGDVPGHPSRTARG 94
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEkPDGGTIVLNGTVLfdsrkKINLPPQQrKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 95 HLR--MLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLL 172
Cdd:cd03297 95 NLAfgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 517388152 173 KAYAAR-GGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03297 175 KQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-207 |
1.12e-12 |
|
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: 66.09 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRhTHPA---GAVGVLLGDVpghps 89
Cdd:cd03246 12 GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTSGRVRLDGADISQ-WDPNelgDHVGYLPQDD----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 90 rtarghlrmlaaaagapAERADQVLEIVglretagrrlstFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLY 169
Cdd:cd03246 86 -----------------ELFSGSIAENI------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 517388152 170 GLLKAYAARGGAVVVTcADPKAAGRLGDRVVTLDKGRL 207
Cdd:cd03246 137 QAIAALKAAGATRIVI-AHRPETLASADRILVLEDGRV 173
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-215 |
1.25e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 23 LSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITLFGGRPL----------HR-----HTHPAGAVGVL----LGD 83
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLeawsaaelarHRaylsqQQTPPFAMPVFqyltLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 84 VPGHPSRTARGHLrmlaaaagapaeraDQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPA-------LLLDDP 156
Cdd:PRK03695 95 PDKTRTEAVASAL--------------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDinpagqlLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-210 |
2.70e-12 |
|
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: 69.48 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 13 RGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLhRHTHPA---GAVGVLLGDVP--- 85
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLyEPTSGRILIDGIDL-RQIDPAslrRQIGVVLQDVFlfs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 86 ---------GHPSRTARghlRMLaaaagapaeradQVLEIVGLRETAgRRL------------STFSLGMDRRLGVAAAL 144
Cdd:COG2274 563 gtirenitlGDPDATDE---EII------------EAARLAGLHDFI-EALpmgydtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 145 LGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTcADPKAAgRLGDRVVTLDKGRLVAD 210
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA-HRLSTI-RLADRIIVLDKGRIVED 690
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-208 |
3.09e-12 |
|
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: 65.65 E-value: 3.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGR--GITLFGGRPLHRHTHPAgavgvLLGDVPGHpsrtarghl 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGvsGEVLINGRPLDKRSFRK-----IIGYVPQD--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 97 rmlaaaagapaeraDQVLEIVGLRET-----AGRRLSTfslGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGL 171
Cdd:cd03213 91 --------------DILHPTLTVRETlmfaaKLRGLSG---GERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 517388152 172 LKAYAARGGAVVVTCADPKAAG-RLGDRVVTLDKGRLV 208
Cdd:cd03213 154 LRRLADTGRTIICSIHQPSSEIfELFDKLLLLSQGRVI 191
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
19-208 |
4.23e-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: 65.74 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGR------PLHRHthpagaVGVLLGDVPGHPSRT 91
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEePTSGRIYIGGRdvtdlpPKDRD------IAMVFQNYALYPHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAW 167
Cdd:cd03301 89 VYDNiafgLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517388152 168 LYGLLKAYAARGGAVVV-TCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:cd03301 169 MRAELKRLQQRLGTTTIyVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-185 |
5.98e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 1 MVIQAIGLtSASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLM---LELEPGRgITLFGGRPlhRHTHPAGAV 77
Cdd:PRK13539 1 MMLEGEDL-ACVRGGRV-LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIaglLPPAAGT-IKLDGGDI--DDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 GVLlgdvpGH-----PSRTARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALL 152
Cdd:PRK13539 76 HYL-----GHrnamkPALTVAENLEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|...
gi 517388152 153 LDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVT 185
Cdd:PRK13539 151 LDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-248 |
6.33e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 6.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 13 RGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTV-LRLMLELEPGRGITLFGGRPLHRHTHPAGAVGVLLGDVPGHPSRT 91
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 A---------RGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:PRK13638 90 IfytdidsdiAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 163 HDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE-FGRRRL-------RPY-VAVHSpqae 233
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEvFACTEAmeqagltQPWlVKLHT---- 245
|
250
....*....|....*
gi 517388152 234 RLGLLLTDDGTEITH 248
Cdd:PRK13638 246 QLGLPLCKTETEFFH 260
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-215 |
6.57e-12 |
|
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: 67.86 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPAGAVGVLLgdVPGHP 88
Cdd:COG4988 343 SFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLgFLPPYSGSILINGVDLSDLDPASWRRQIAW--VPQNP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 ---SRTARGHLRMlaAAAGAPAERADQVLEIVGLRE--------------TAGRRLstfSLGMDRRLGVAAALLGDPPAL 151
Cdd:COG4988 421 ylfAGTIRENLRL--GRPDASDEELEAALEAAGLDEfvaalpdgldtplgEGGRGL---SGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517388152 152 LLDDPAQGLSPHDTAWLYGLLKAYAArgGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-211 |
1.27e-11 |
|
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: 64.05 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 22 DLSFDArpGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGG----------RPL-------HRHTHPAGAVGVLLGD 83
Cdd:cd03298 18 DLTFAQ--GEITAIVGPSGSGKSTLLNLIAGFEtPQSGRVLINGvdvtaappadRPVsmlfqenNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 84 VPGhpsrtarghLRMlaaaAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPH 163
Cdd:cd03298 96 SPG---------LKL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517388152 164 DTAWLYGL-LKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQ 211
Cdd:cd03298 163 LRAEMLDLvLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-211 |
2.74e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRP---LHRHTHPA--GAVGVLLGDVPG--HPSRT 91
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLEsPSQGNVSWRGEPlakLNRAQRKAfrRDIQMVFQDSISavNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGHLR-----MLAAAAGAPAERADQVLEIVGLR-ETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDT 165
Cdd:PRK10419 108 VREIIReplrhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517388152 166 AWLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLVADQ 211
Cdd:PRK10419 188 AGVIRLLKKLQQQFGtACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-185 |
3.15e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 62.90 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 23 LSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPAGAVGVLLGDVPGHPSR-TARGHLRMLA 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLsPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTlSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 101 AAAGAPAEraDQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGG 180
Cdd:cd03231 99 ADHSDEQV--EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGG 176
|
....*
gi 517388152 181 AVVVT 185
Cdd:cd03231 177 MVVLT 181
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
18-207 |
3.82e-11 |
|
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: 63.13 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGAVGVLLGDVPGHPSRTARGH- 95
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLErPDSGTILFGGEDATDVPVQERNVGFVFQHYALFRHMTVFDNv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 96 ---LRMLAAAAGAPAER----ADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWL 168
Cdd:cd03296 96 afgLRVKPRSERPPEAEirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517388152 169 YGLLKAYAARGG--AVVVTcADPKAAGRLGDRVVTLDKGRL 207
Cdd:cd03296 176 RRWLRRLHDELHvtTVFVT-HDQEEALEVADRVVVMNKGRI 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2-185 |
3.97e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 2 VIQAIGLTsASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPAGAVGVL 80
Cdd:PRK13538 1 MLEARNLA-CERDERI-LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLaRPDAGEVLWQGEPIRRQRDEYHQDLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 LGDVPG-HPSRTARGHLRMLAAAAGAPAE-RADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQ 158
Cdd:PRK13538 79 LGHQPGiKTELTALENLRFYQRLHGPGDDeALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180
....*....|....*....|....*..
gi 517388152 159 GLSPHDTAWLYGLLKAYAARGGAVVVT 185
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILT 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-215 |
3.99e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 63.18 E-value: 3.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 4 QAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRGItlfggrpLHRHthpaGAVGVLLG 82
Cdd:COG1134 26 ELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPTSGR-------VEVN----GRVSALLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 83 dvPG---HPSRTAR------GhlRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLL 153
Cdd:COG1134 95 --LGagfHPELTGReniylnG--RLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 154 DDpaqGLSPHDTAWL---YGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:COG1134 171 DE---VLAVGDAAFQkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-216 |
4.26e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITL--------FGGRP-------LHRHthpagaVGVLLGD 83
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPsdkaireLRRN------VGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 84 VPGHPSRTARGHL-----RMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQ 158
Cdd:PRK11124 91 YNLWPHLTVQQNLieapcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 159 GLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCF 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-202 |
5.55e-11 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 65.00 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEePPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLhRHTHPAGAVG--V 79
Cdd:TIGR02857 322 LEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVNGVPL-ADADADSWRDqiA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 LLGDVPGHPSRTARGHLRMlaAAAGAPAERADQVLEIVGLRET-----------AGRRLSTFSLGMDRRLGVAAALLGDP 148
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRL--ARPDASDAEIREALERAGLDEFvaalpqgldtpIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517388152 149 PALLLDDPAQGLSPHDTAWLYGLLKAYaARGGAVVVTCADPKAAgRLGDRVVTL 202
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-206 |
9.24e-11 |
|
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: 60.47 E-value: 9.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPA--GAVGVllgdVPGHP-- 88
Cdd:cd03228 12 GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLrLYDPTSGEILIDGVDLRDLDLESlrKNIAY----VPQDPfl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 -SRTARghlrmlaaaagapaeraDQVLeivglretagrrlstfSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAW 167
Cdd:cd03228 88 fSGTIR-----------------ENIL----------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 517388152 168 LYGLLKAYAARGGAVVVTCADpkAAGRLGDRVVTLDKGR 206
Cdd:cd03228 135 ILEALRALAKGKTVIVIAHRL--STIRDADRIIVLDDGR 171
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-207 |
1.27e-10 |
|
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: 61.39 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGAVGVLLGDVPGH----PSRTAR 93
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEePDSGTIIIDGLKLTDDKKNINELRQKVGMVFQQfnlfPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 94 GHLrMLAAAAGAPAERAD------QVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAW 167
Cdd:cd03262 95 ENI-TLAPIKVKGMSKAEaeeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 517388152 168 LYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRL 207
Cdd:cd03262 174 VLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-216 |
1.44e-10 |
|
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: 61.54 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLHR-HTHPAGAVGVLLgdVP-GH---PSRT 91
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLLPPRSGSIRFDGEDITGlPPHRIARLGIGY--VPeGRrifPSLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGHLRM---LAAAAGAPAERADQVLEIV-GLRETAGRRLSTFSLG---MdrrLGVAAALLGDPPALLLDDPAQGLSPHD 164
Cdd:COG0410 95 VEENLLLgayARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGeqqM---LAIGRALMSRPKLLLLDEPSLGLAPLI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517388152 165 TAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:COG0410 172 VEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-207 |
2.42e-10 |
|
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: 60.56 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPL----HRHTHpagAVGVLLGDVPGHPSRTA 92
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFyQPQGGQVLLDGKPIsqyeHKYLH---SKVSLVGQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 93 RGHLR--------MLAAAAGAPAERADQVLEIV-GLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPH 163
Cdd:cd03248 105 QDNIAyglqscsfECVKEAAQKAHAHSFISELAsGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517388152 164 DTAWLYGLLKAYAARGGAVVVtcadpkaAGRL-----GDRVVTLDKGRL 207
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVI-------AHRLstverADQILVLDGGRI 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-209 |
3.50e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.17 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHThpAGAVGVLLGDVPGHP 88
Cdd:PRK09536 10 SVEFGDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINgTLTPTAGTVLVAGDDVEALS--ARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 S--------------RTArgHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLD 154
Cdd:PRK09536 87 SlsfefdvrqvvemgRTP--HRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 155 DPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVA 209
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRA 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-221 |
3.51e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLH-RHTHPAGAVGV---------------- 79
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKiLSGVYQPDSGEILLDGEPVRfRSPRDAQAAGIaiihqelnlvpnlsva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 ---LLGDVPGHPSRTARGHLRmlaaaagapaERADQVLEIVGLRETAGRRLSTFSLGmDRRLgV--AAALLGDPPALLLD 154
Cdd:COG1129 98 eniFLGREPRRGGLIDWRAMR----------RRARELLARLGLDIDPDTPVGDLSVA-QQQL-VeiARALSRDARVLILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 155 DPAQGLSPHDTAWLYGLLKAYAARGGAVV--------VTcadpkaagRLGDRVVTLDKGRLVADQSAHEFGRRRL 221
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRLKAQGVAIIyishrldeVF--------EIADRVTVLRDGRLVGTGPVAELTEDEL 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-156 |
3.59e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRGITLFGGRPLhrhTHPAGAVGVLLGDVPGHPSRTARGH- 95
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDGKPV---EGPGAERGVVFQNEGLLPWRNVQDNv 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517388152 96 ---LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:PRK11248 92 afgLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-247 |
3.67e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 61.02 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLHRHTHPA----GAVGVLLGDvPGHPSRTAR 93
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQnLNGILKPSSGRILFDGKPIDYSRKGLmklrESVGMVFQD-PDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 94 -------GHLRMlAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTA 166
Cdd:PRK13636 100 vyqdvsfGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 167 WLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE-FGRRRLRPYVAVHSPQAERL-GLLLTDDG 243
Cdd:PRK13636 179 EIMKLLVEMQKELGlTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEvFAEKEMLRKVNLRLPRIGHLmEILKEKDG 258
|
....
gi 517388152 244 TEIT 247
Cdd:PRK13636 259 FVFD 262
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-208 |
6.71e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.60 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 27 ARPGEITVLLGDGGAGKSTVL-----RLMLELEPGRGITLfGGRPLHRHTHPAGAVGVLLGDVpGHPSRTAR------GH 95
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMnalafRSPKGVKGSGSVLL-NGMPIDAKEMRAISAYVQQDDL-FIPTLTVRehlmfqAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 96 LRMLAAAAGAP-AERADQVLEIVGLRETA------GRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWL 168
Cdd:TIGR00955 126 LRMPRRVTKKEkRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517388152 169 YGLLKAYAARGGAVVVTCADPKAA-GRLGDRVVTLDKGRLV 208
Cdd:TIGR00955 206 VQVLKGLAQKGKTIICTIHQPSSElFELFDKIILMAEGRVA 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-215 |
7.66e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 17 PPAVDDLSFDARPGEITVLLGDGGAGKS-TVLRLMLELEPG----RGITLFGGRPLhrhtHPAGAVGVLLGDVPGHPS-- 89
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAGvrqtAGRVLLDGKPV----APCALRGRKIATIMQNPRsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 90 ----RTARGHLR--MLAAAAGAPAERADQVLEIVGLrETAGRRLSTF----SLGMDRRLGVAAALLGDPPALLLDDPAQG 159
Cdd:PRK10418 92 fnplHTMHTHARetCLALGKPADDATLTAALEAVGL-ENAARVLKLYpfemSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 160 LSPHDTAWLYGLLKAYAA-RGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK10418 171 LDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVET 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-212 |
1.16e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPAGA---VGVLLGD----------- 83
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhEPTKGTITINNINYNKLDHKLAAqlgIGIIYQElsvideltvle 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 84 ---VPGHPSRTARGhlrMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGL 160
Cdd:PRK09700 100 nlyIGRHLTKKVCG---VNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 161 SPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKG-----RLVADQS 212
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGssvcsGMVSDVS 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-221 |
1.65e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.87 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-----EPGRGITLFG---------GRPLHRHTHPAGAV------- 77
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdkSAGSHIELLGrtvqregrlARDIRKSRANTGYIfqqfnlv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 -------GVLLGDVPGHPsrTARGHLRMLAAAAGAPAEradQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPA 150
Cdd:PRK09984 99 nrlsvleNVLIGALGSTP--FWRTCFSWFTREQKQRAL---QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517388152 151 LLLDDPAQGLSPHDTAWLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRRRL 221
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERF 245
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-172 |
1.99e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.46 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHT-HPAGAVGV----------------- 79
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFyKPTGGTILLRGQHIEGLPgHQIARMGVvrtfqhvrlfremtvie 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 -LLgdVPGHpSRTARGHLRMLAAAAGAPAERADQV------LEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALL 152
Cdd:PRK11300 100 nLL--VAQH-QQLKTGLFSGLLKTPAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180
....*....|....*....|
gi 517388152 153 LDDPAQGLSPHDTAWLYGLL 172
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELI 196
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-211 |
2.04e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPA-----GAVGVLLGDVPGHPSRTA 92
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIErPSAGKIWFSGHDITRLKNREvpflrRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 93 RGHLRM-LAAAAGAPAERADQV---LEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWL 168
Cdd:PRK10908 97 YDNVAIpLIIAGASGDDIRRRVsaaLDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517388152 169 YGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQ 211
Cdd:PRK10908 177 LRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGV 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-215 |
2.43e-09 |
|
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: 58.01 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPA--GAVGVLLGDVP--------- 85
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFyDVSSGSILIDGQDIREVTLDSlrRAIGVVPQDTVlfndtigyn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 86 ---GHPS----------RTARGHLRMLaaaagapaERADQVLEIVGLRetaGRRLSTfslGMDRRLGVAAALLGDPPALL 152
Cdd:cd03253 95 iryGRPDatdeevieaaKAAQIHDKIM--------RFPDGYDTIVGER---GLKLSG---GEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 153 LDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVtcadpkaAGRL-----GDRVVTLDKGRlVADQSAHE 215
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVI-------AHRLstivnADKIIVLKDGR-IVERGTHE 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-215 |
3.31e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEP---GR----GITLFGGRPLHRHTH-PAGAV------------ 77
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEitsGDlivdGLKVNDPKVDERLIRqEAGMVfqqfylfphlta 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 --GVLLGdvPGHPSRTARGHLRMLAAaagapaeradQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDD 155
Cdd:PRK09493 95 leNVMFG--PLRVRGASKEEAEKQAR----------ELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 156 PAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-210 |
4.65e-09 |
|
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: 56.77 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 8 LTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEP---GRGITLfggrplhrhthpaGAVGVLLGDV 84
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsGTVTVR-------------GRVSSLLGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 85 PG-HPSRTARGHLRMLAAAAGAPAERADQVL-EIV---GLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDdpaQG 159
Cdd:cd03220 93 GGfNPELTGRENIYLNGRLLGLSRKEIDEKIdEIIefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLID---EV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517388152 160 LSPHDTAWL---YGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVAD 210
Cdd:cd03220 170 LAVGDAAFQekcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-210 |
8.39e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.36 E-value: 8.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 22 DLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGA------VGVLLGDVPGHPSRTARG 94
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDtPTSGDVIFNGQPMSKLSSAAKAelrnqkLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 95 HLRMLAAAAGAPAERADQ----VLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYG 170
Cdd:PRK11629 107 NVAMPLLIGKKKPAEINSraleMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQ 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 517388152 171 LLKAYAAR-GGAVVVTCADPKAAGRLgDRVVTLDKGRLVAD 210
Cdd:PRK11629 187 LLGELNRLqGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-207 |
9.65e-09 |
|
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: 55.13 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 17 PPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPG-RGITLFGGRPLHRhTHPAGAVGVLLGDVPGhpSRTARGh 95
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGKPVTR-RSPRDAIRAGIAYVPE--DRKREG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 96 lrmlaaaagapaeradqVLEIVGLRE--TAGRRLSTfslGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLK 173
Cdd:cd03215 89 -----------------LVLDLSVAEniALSSLLSG---GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIR 148
|
170 180 190
....*....|....*....|....*....|....
gi 517388152 174 AYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRL 207
Cdd:cd03215 149 ELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-160 |
1.07e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 57.91 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGRPLHRHTHPA--GAVGVLLGDVpgHP-S 89
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQGEILLNGQPIADYSEAAlrQAISVVSQRV--HLfS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 90 RTARGHLRMlaaaagAPAERAD----QVLEIVGLRETA-------------GRRLSTfslGMDRRLGVAAALLGDPPALL 152
Cdd:PRK11160 428 ATLRDNLLL------AAPNASDealiEVLQQVGLEKLLeddkglnawlgegGRQLSG---GEQRRLGIARALLHDAPLLL 498
|
....*...
gi 517388152 153 LDDPAQGL 160
Cdd:PRK11160 499 LDEPTEGL 506
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-154 |
1.29e-08 |
|
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: 55.69 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 12 SRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPA--GAVGVLLGDvPGHP 88
Cdd:cd03254 11 SYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFyDPQKGQILIDGIDIRDISRKSlrSMIGVVLQD-TFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 SRTARGHLRMlaaaagAPAERADQVLEIV---------------GLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLL 153
Cdd:cd03254 90 SGTIMENIRL------GRPNATDEEVIEAakeagahdfimklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILIL 163
|
.
gi 517388152 154 D 154
Cdd:cd03254 164 D 164
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-208 |
1.45e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.69 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRL---MLELEPG---RGITLFGGR-----PLHRHTHPAGAVGVLLGDVPGHP 88
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarvSGEVYLDGQdifkmDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 --SRTARG-HLRMLAAAAGAPAERADQVLEIVGLRETAGRRL----STFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS 161
Cdd:PRK14247 99 ifENVALGlKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLdapaGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517388152 162 PHDTAWLYGLLKAYAARGGAVVVTCADPKAAgRLGDRVVTLDKGRLV 208
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAA-RISDYVAFLYKGQIV 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-216 |
2.42e-08 |
|
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: 54.86 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPL-HRHTHPAGAVGvlLGDVPGHPS------ 89
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGKILLDGQDItKLPMHKRARLG--IGYLPQEASifrklt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 90 --RTARGHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAW 167
Cdd:cd03218 92 veENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517388152 168 LYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:cd03218 172 IQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-220 |
2.55e-08 |
|
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: 54.80 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 13 RGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLH--RHTHPAGAVGVLL-------G 82
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLAlaDPAWLRRQVGVVLqenvlfnR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 83 DVPGHPSRTARGHLRMLAAAAGAPAERADQVLEI-VGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS 161
Cdd:cd03252 91 SIRDNIALADPGMSMERVIEAAKLAGAHDFISELpEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 162 PHDTAWLYGLLKAYAArgGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHEFGRRR 220
Cdd:cd03252 171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-216 |
2.65e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 54.76 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 24 SFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRGITLFGGRPlHRHTHPAG------------------AVGVLLGDV 84
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQD-LTALPPAErpvsmlfqennlfphltvAQNIGLGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 85 PG-HPSRTARGHLrmlaaaagapaeraDQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPH 163
Cdd:COG3840 98 PGlKLTAEQRAQV--------------EQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 164 DTAWLYGLLKAYAARGGAVV--VTcADPKAAGRLGDRVVTLDKGRLVADQSAHEF 216
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVlmVT-HDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-208 |
3.81e-08 |
|
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: 53.81 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGR----GITLFGGRPLH--RHTHPAGAVGVLLGDVpGHPSRT 91
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsveGDIHYNGIPYKefAEKYPGEIIYVSEEDV-HFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARghlrmlaaaagapaeradQVLEIVgLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLsphDTA----W 167
Cdd:cd03233 100 VR------------------ETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL---DSStaleI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 517388152 168 LYGLLKAYAARGGAVVVTC--ADPKAAGrLGDRVVTLDKGRLV 208
Cdd:cd03233 158 LKCIRTMADVLKTTTFVSLyqASDEIYD-LFDKVLVLYEGRQI 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-215 |
4.31e-08 |
|
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: 55.60 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGR--GITLFGGRPLHRHThPAGAVGVLLGDVP------GHPSRT 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfeGNVFINGKPVDIRN-PAQAIRAGIAMVPedrkrhGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGH-LRMLAAAAGAPAERADQVLEIVGLRETAGR-RLSTFS--LGMDRRLG-------VAAALLGDPPALLLDDPAQGL 160
Cdd:TIGR02633 355 GVGKnITLSVLKSFCFKMRIDAAAELQIIGSAIQRlKVKTASpfLPIGRLSGgnqqkavLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 161 SPHDTAWLYGLLKAYAARGGAVVVTCAD-PKAAGrLGDRVVTLDKGRLVADQSAHE 215
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLG-LSDRVLVIGEGKLKGDFVNHA 489
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-174 |
8.80e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITLFGGRPLHRHTH----------------PAGAVGVLLg 82
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRrqllpvrhriqvvfqdPNSSLNPRL- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 83 DVPGHPSRTARGHLRMLAAAAGAPAERadQVLEIVGLR-ETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS 161
Cdd:PRK15134 380 NVLQIIEEGLRVHQPTLSAAQREQQVI--AVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170
....*....|...
gi 517388152 162 PHDTAWLYGLLKA 174
Cdd:PRK15134 458 KTVQAQILALLKS 470
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-208 |
9.98e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 54.27 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPA------GAVGVLLGDVPGHPSRT 91
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLIDGVDIAKISDAElrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 ARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPH-DTA 166
Cdd:PRK10070 123 VLDNtafgMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLiRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 517388152 167 WLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-209 |
1.19e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.20 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTvlrLMLELE----PGRGITLFGGRPLHRHTHP--AGAVGVLLGDvpghP---- 88
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKST---LLLHLNgiylPQRGRVKVMGREVNAENEKwvRSKVGLVFQD----Pddqv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 -SRT-----ARGHLRMlAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:PRK13647 93 fSSTvwddvAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517388152 163 HDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVA 209
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
12-273 |
1.23e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.54 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 12 SRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRL--MLElEPGRGITLFGGRPLH----------RHThpagaVGV 79
Cdd:COG1135 13 TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCinLLE-RPTSGSVLVDGVDLTalserelraaRRK-----IGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 ------LLgdvpghPSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPP 149
Cdd:COG1135 87 ifqhfnLL------SSRTVAENvalpLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 150 ALLLDDPAQGLSPHDTAWLYGLLKAYAARGGA--VVVT---------CadpkaagrlgDRVVTLDKGRLVAD-------- 210
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLtiVLIThemdvvrriC----------DRVAVLENGRIVEQgpvldvfa 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 211 QSAHEFGRRRLRPYVAVHSPQAERLGLLLTDDGTEIThesgsRIRVHGATTAQ--VGEAAFRNGI 273
Cdd:COG1135 231 NPQSELTRRFLPTVLNDELPEELLARLREAAGGGRLV-----RLTFVGESADEplLSELARRFGV 290
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
8-160 |
1.83e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 53.30 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 8 LTSASRGEepPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLhRHTHP-AGAVGVLLGDVP 85
Cdd:PRK11607 25 LTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEqPTAGQIMLDGVDL-SHVPPyQRPINMMFQSYA 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 86 GHPSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGL 160
Cdd:PRK11607 102 LFPHMTVEQNiafgLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-209 |
2.33e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLH-RHTHPAGAVGVL-----LGDVP------ 85
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKiLSGNYQPDAGSILIDGQEMRfASTTAALAAGVAiiyqeLHLVPemtvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 86 ----GH-PSRTARGHLRMLAAAAGAPaeradqvLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGL 160
Cdd:PRK11288 99 nlylGQlPHKGGIVNRRLLNYEAREQ-------LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517388152 161 SPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVA 209
Cdd:PRK11288 172 SAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-205 |
2.45e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 1 MVIQAIGLTSasRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITLFGGRPlhrhTHPAGAVGVL 80
Cdd:COG2401 29 IVLEAFGVEL--RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVP----DNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 LGDVPGHPSRTArghlrmlaaaagapaerADQVLEIVGLRETAG--RRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQ 158
Cdd:COG2401 103 IDAIGRKGDFKD-----------------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 517388152 159 GLSPhDTAWL--YGLLKAYAARGGAVVVTCADPKAAGRLG-DRVVTLDKG 205
Cdd:COG2401 166 HLDR-QTAKRvaRNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-215 |
2.91e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 51.67 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 23 LSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRG------ITLFGGRPLHRHTHPAGA----VGVLLGDVPGHPSRT 91
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEqPEAGtirvgdITIDTARSLSQQKGLIRQlrqhVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 92 A-----RGHLRMLAAAAGAPAERADQVLEIVGL--RETA-GRRLSTfslGMDRRLGVAAALLGDPPALLLDDPAQGLSPH 163
Cdd:PRK11264 102 VleniiEGPVIVKGEPKEEATARARELLAKVGLagKETSyPRRLSG---GQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 517388152 164 DTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-185 |
3.30e-07 |
|
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: 53.13 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRGITLFGGRPLHRHTHPAGAVGVLLGDVPGHP 88
Cdd:TIGR02868 341 SAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 -SRTARGHLRMLAAAAGAPAERAdqVLEIVGLRETA-----------GRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:TIGR02868 421 fDTTVRENLRLARPDATDEELWA--ALERVGLADWLralpdgldtvlGEGGARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180
....*....|....*....|....*....
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVT 185
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAALSGRTVVLIT 527
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-215 |
3.81e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 52.26 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGR------PLHRHTH---------PAGAV--GV 79
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFEtPDSGRIMLDGQdithvpAENRHVNtvfqsyalfPHMTVfeNV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 LLGdvpghpsrtarghLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPaqg 159
Cdd:PRK09452 108 AFG-------------LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES--- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 160 LSPHDtawlYGL-------LKAYAARGGA--VVVTcADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK09452 172 LSALD----YKLrkqmqneLKALQRKLGItfVFVT-HDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
18-206 |
4.30e-07 |
|
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: 50.90 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRL-----------MLELEPGRGITLFGGRP-----LHRHThpAGAVGVLL 81
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCiygnylpdsgsILVRHDGGWVDLAQASPreilaLRRRT--IGYVSQFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 82 GDVP---------------GHPSRTARGHLRMLaaaagapaeradqvLEIVGLREtagrRL-----STFSLGMDRRLGVA 141
Cdd:COG4778 103 RVIPrvsaldvvaepllerGVDREEARARAREL--------------LARLNLPE----RLwdlppATFSGGEQQRVNIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 142 AALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGR 206
Cdd:COG4778 165 RGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
18-156 |
4.85e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 52.02 E-value: 4.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLM--LElEPGRGITLFGGRPLHrhthpagavgvllgDVPGH-------- 87
Cdd:COG3842 19 TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagFE-TPDSGRILLDGRDVT--------------GLPPEkrnvgmvf 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 88 ------PSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:COG3842 84 qdyalfPHLTVAENvafgLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEP 162
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-207 |
5.83e-07 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 51.99 E-value: 5.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 21 DDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGitlfggrplhRHTHPAGA-VGVLLGDVPGHPSRTAR----- 93
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAgELEPDSG----------EVSIPKGLrIGYLPQEPPLDDDLTVLdtvld 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 94 --GHLRMLAAAAGAPAERAD-----------------------------QVLEIVGL-RETAGRRLSTFSLGMDRRLGVA 141
Cdd:COG0488 85 gdAELRALEAELEELEAKLAepdedlerlaelqeefealggweaearaeEILSGLGFpEEDLDRPVSELSGGWRRRVALA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 142 AALLGDPPALLLDDPAQGLsphD---TAWLYGLLKAYAargGAVVVTCADpkaagR--LgDRVVT----LDKGRL 207
Cdd:COG0488 165 RALLSEPDLLLLDEPTNHL---DlesIEWLEEFLKNYP---GTVLVVSHD-----RyfL-DRVATrileLDRGKL 227
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
112-208 |
7.34e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 112 QVLEIVGLreTAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYaarGGAVVVTCADPKA 191
Cdd:PRK11147 141 EVLAQLGL--DPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISHDRSF 215
|
90
....*....|....*..
gi 517388152 192 AGRLGDRVVTLDKGRLV 208
Cdd:PRK11147 216 IRNMATRIVDLDRGKLV 232
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-209 |
1.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.50 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFG-----GRPLHRHTHPA-GAVGVL----------- 80
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQhLNGLLQPTEGKVTVGdivvsSTSKQKEIKPVrKKVGVVfqfpesqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 --LGDVPGHPSRtarghlrmLAAAAGAPAERADQVLEIVGLRETAGRRlSTFSL--GMDRRLGVAAALLGDPPALLLDDP 156
Cdd:PRK13643 101 tvLKDVAFGPQN--------FGIPKEKAEKIAAEKLEMVGLADEFWEK-SPFELsgGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVA 209
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
19-208 |
1.36e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLM-LELEPGRGITLF---GGRPLHRHTHPAGAVGVLL----GDVPGHPsr 90
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYrmrDGQLRDLYALSEAERRRLLrtewGFVHQHP-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 91 taRGHLRMlaaaagapaeradQV---------LEIVG------LRETAGRRLS--------------TFSLGMDRRLGVA 141
Cdd:PRK11701 99 --RDGLRM-------------QVsaggnigerLMAVGarhygdIRATAGDWLErveidaariddlptTFSGGMQQRLQIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 142 AALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGlAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-221 |
1.98e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTvlrLM--L--ELEPGRGITLFGGRPLhRHTHPAGA----VG------------ 78
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKST---LMkiLygLYQPDSGEILIDGKPV-RIRSPRDAialgIGmvhqhfmlvpnl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 -----VLLGDVPGHPSRTARGHLRmlaaaagapaeraDQVLEI---VGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPA 150
Cdd:COG3845 96 tvaenIVLGLEPTKGGRLDRKAAR-------------ARIRELserYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 151 LLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVV--------VTcadpkaagRLGDRVVTLDKGRLVADQSAHEFGRRRL 221
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIfithklreVM--------AIADRVTVLRRGKVVGTVDTAETSEEEL 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-71 |
2.08e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 50.55 E-value: 2.08e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 14 GEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHT 71
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTSGRILIDGVDIRDLT 408
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-215 |
2.42e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.02 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 23 LSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGA--VGVLLGDVPGHPSRTARGHLRM- 98
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQpPSEGEILLDAQPLESWSSKAFArkVAYLPQQLPAAEGMTVRELVAIg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 99 -------LAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLS-PHDTAWLYG 170
Cdd:PRK10575 110 rypwhgaLGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDiAHQVDVLAL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 517388152 171 LLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK10575 190 VHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
19-269 |
2.76e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.03 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLR-LMLELEPGRGITLFGGRPLHRHThpAGAVGVLLGDVPGHP-----SRTA 92
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRhFNGILKPTSGSVLIRGEPITKEN--IREVRKFVGLVFQNPddqifSPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 93 RGHLRM----LAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWL 168
Cdd:PRK13652 97 EQDIAFgpinLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 169 YGLLKAYAAR-GGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE-FGRRRLRPYVAVHSPQAERLGLLLTDDGTEI 246
Cdd:PRK13652 177 IDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEiFLQPDLLARVHLDLPSLPKLIRSLQAQGIAI 256
|
250 260
....*....|....*....|...
gi 517388152 247 THesgsrirvhgATTAQVGEAAF 269
Cdd:PRK13652 257 DM----------AYTYQEAEDAF 269
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-156 |
2.92e-06 |
|
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: 49.28 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGIT----LFGGRPLHRHTH-----------------PAGA 76
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITsgeiLFDGEDLLKLSEkelrkirgreiqmifqdPMTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 77 ------VGVLLGDVP----GHPSRTARGHLRmlaaaagapaeradQVLEIVGLREtAGRRLS----TFSLGMDRRLGVAA 142
Cdd:COG0444 99 lnpvmtVGDQIAEPLrihgGLSKAEARERAI--------------ELLERVGLPD-PERRLDryphELSGGMRQRVMIAR 163
|
170
....*....|....
gi 517388152 143 ALLGDPPALLLDDP 156
Cdd:COG0444 164 ALALEPKLLIADEP 177
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-215 |
3.24e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPG----RGITLFG-----GRPLHR---------------HTHPAG 75
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggapRGARVTGdvtlnGEPLAAidaprlarlravlpqAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 76 AVG----VLLGDVPghpsrtargHLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAAL------- 144
Cdd:PRK13547 97 AFSareiVLLGRYP---------HARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 145 --LGDPPALLLDDPAQGLsphDTAWLYGLLKAYAARGG----AVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13547 168 daAQPPRYLLLDEPTAAL---DLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
16-215 |
3.36e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 16 EPPAVDDLSFDARPGEITVLLGDGGAGKSTvlrLMLE----LEPGRGITLFGGRPLHRHTHPAG------AVGV------ 79
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHfnalLKPSSGTITIAGYHITPETGNKNlkklrkKVSLvfqfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 -------LLGDVPGHPsrtarghlRMLAAAAGAPAERADQVLEIVGLRETAGRRlSTFSL--GMDRRLGVAAALLGDPPA 150
Cdd:PRK13641 96 aqlfentVLKDVEFGP--------KNFGFSEDEAKEKALKWLKKVGLSEDLISK-SPFELsgGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 151 LLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-208 |
3.54e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 17 PPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGG-------RPLHRHthpagAVGVLLGDvPGHP 88
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVfDPQSGRILIDGtdirtvtRASLRR-----NIAVVFQD-AGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 SRTARGHLRM----LAAAAGAPAERADQVLEIV-----GLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQG 159
Cdd:PRK13657 422 NRSIEDNIRVgrpdATDEEMRAAAERAQAHDFIerkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517388152 160 LSPHDTAWLYGLLKayAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:PRK13657 502 LDVETEAKVKAALD--ELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-210 |
4.14e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEEPPAVDDLSFDARPgeITVLLGDGGAGKSTVLRLMLELEPG------RGITLFGGRPLHRHTH---- 72
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARA--VTSLMGPTGSGKTTFLRTLNRMNDKvsgyrySGDVLLGGRSIFNYRDvlef 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 73 --------------PAGAVGVLLGDVPGH---PSRTARGhlrmlaaaagapaeRADQVLEIVGLRETAGRRLST----FS 131
Cdd:PRK14271 100 rrrvgmlfqrpnpfPMSIMDNVLAGVRAHklvPRKEFRG--------------VAQARLTEVGLWDAVKDRLSDspfrLS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 132 LGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAgRLGDRVVTLDKGRLVAD 210
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAA-RISDRAALFFDGRLVEE 243
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
12-204 |
4.26e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.92 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 12 SRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPL---HRHTHPAgavgvLLGDVPG- 86
Cdd:PRK13543 20 SRNEEP-VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLlHVESGQIQIDGKTAtrgDRSRFMA-----YLGHLPGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 87 HPSRTARGHLRML-AAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDT 165
Cdd:PRK13543 94 KADLSTLENLHFLcGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 517388152 166 AWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDK 204
Cdd:PRK13543 174 TLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
21-206 |
6.74e-06 |
|
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: 45.90 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 21 DDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGItlfggrplhRHTHPAGAVGVLlgdvpghpsrtarghlrml 99
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGI---------VTWGSTVKIGYF------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 100 aaaagapaeraDQvleivglretagrrlstFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAarg 179
Cdd:cd03221 69 -----------EQ-----------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP--- 117
|
170 180
....*....|....*....|....*..
gi 517388152 180 GAVVVTCADPKAAGRLGDRVVTLDKGR 206
Cdd:cd03221 118 GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-74 |
7.75e-06 |
|
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: 48.53 E-value: 7.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITLFGGRPLHRHTHPA 74
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSRRA 356
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-250 |
8.64e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTvlrlMLELEPGRGITLFGGRPLHRHTHPAGAVGV-----------LLGDVPGH 87
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKST----MIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlrkeigLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 88 -------PSRTARGHLRmLAAAAGAPAERADQVLEIVGLRETAGRRlSTFSL--GMDRRLGVAAALLGDPPALLLDDPAQ 158
Cdd:PRK13645 102 qlfqetiEKDIAFGPVN-LGENKQEAYKKVPELLKLVQLPEDYVKR-SPFELsgGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 159 GLSPH-DTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE-FGRRRLRPYVAVHSPQAERLG 236
Cdd:PRK13645 180 GLDPKgEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEiFSNQELLTKIEIDPPKLYQLM 259
|
250
....*....|....
gi 517388152 237 LLLTDDGTEITHES 250
Cdd:PRK13645 260 YKLKNKGIDLLNKN 273
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-249 |
1.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.49 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 16 EPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-----EPGRGITLFGGRpLHRHT-------------HPAGA- 76
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddNPNSKITVDGIT-LTAKTvwdirekvgivfqNPDNQf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 77 VGVLLGDvpghpsRTARGhLRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:PRK13640 98 VGATVGD------DVAFG-LENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE-FGRRRLRPYVAVHSPQAERL 235
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEiFSKVEMLKEIGLDIPFVYKL 250
|
250
....*....|....
gi 517388152 236 GLLLTDDGTEITHE 249
Cdd:PRK13640 251 KNKLKEKGISVPQE 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
10-162 |
1.10e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.07 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 10 SASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLM-LELEPGRGITLFGGR--PLHRHTHPAGA---------V 77
Cdd:PRK11831 14 SFTRGNRC-IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIgGQIAPDHGEILFDGEniPAMSRSRLYTVrkrmsmlfqS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 GVLLGD--VPGHPSRTARGHLRMLAAAAGAPAERAdqvLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDD 155
Cdd:PRK11831 93 GALFTDmnVFDNVAYPLREHTQLPAPLLHSTVMMK---LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
....*..
gi 517388152 156 PAQGLSP 162
Cdd:PRK11831 170 PFVGQDP 176
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
1.19e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTV-LRLMLELEPGRGITLFGGRPLH---------RHThpagaVGVLLGD----- 83
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILKPTSGEVLIKGEPIKydkksllevRKT-----VGIVFQNpddql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 84 -VPGHPSRTARGHLRMLAAAAGAPAERADqVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:PRK13639 92 fAPTVEEDVAFGPLNLGLSKEEVEKRVKE-ALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 517388152 163 HDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13639 171 MGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-207 |
1.33e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 46.89 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 23 LSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTHPAGAVGVLlgdvPGHPSRTARGHLRM--- 98
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEkPSEGSIVVNGQTINLVRDKDGQLKVA----DKNQLRLLRTRLTMvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 99 ---LAAAAGAPAERADQVLEIVGLRETAGRRLSTFSL-------------------GMDRRLGVAAALLGDPPALLLDDP 156
Cdd:PRK10619 100 hfnLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLakvgideraqgkypvhlsgGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRL 207
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-208 |
1.50e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.79 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRP--------LHRHThpagavgVLLGDVPGHP 88
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPTGGQVLLDGVPlvqydhhyLHRQV-------ALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 SRTARGHLrmlaaAAGAPAERADQVLEIV--------------GLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLD 154
Cdd:TIGR00958 568 SGSVRENI-----AYGLTDTPDEEIMAAAkaanahdfimefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 517388152 155 DPAQGLsphDTAWLYgLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:TIGR00958 643 EATSAL---DAECEQ-LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
18-156 |
1.56e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 45.94 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPG---RGITLFGGRPLHRHTHPAGAVGVLLGDV--------- 84
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsaSGEVLLNGRRLTALPAEQRRIGILFQDDllfphlsvg 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 85 -------PGHPSRTARghlrmlaaaagapAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:COG4136 95 enlafalPPTIGRAQR-------------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
14-215 |
1.59e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.80 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 14 GEEPPAV-DDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPL-----------------------H 68
Cdd:PRK10535 17 GEEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDkPTSGTYRVAGQDVatldadalaqlrrehfgfifqryH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 69 RHTHPAGAVGVLLGDVPGHPSRTARghlrmlaaaagapAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDP 148
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVYAGLERKQR-------------LLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 149 PALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRlGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQE 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-208 |
2.07e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 46.72 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 3 IQAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRL--MLElEP--------GRGITLFGGRPLHRHTH 72
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLE-RPtsgrvlvdGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 73 pagAVGV------LLGdvpghpSRTARGH----LRMLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAA 142
Cdd:PRK11153 83 ---QIGMifqhfnLLS------SRTVFDNvalpLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 143 ALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGG----------AVVvtcadpkaaGRLGDRVVTLDKGRLV 208
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGltivlithemDVV---------KRICDRVAVIDAGRLV 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
114-215 |
2.53e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 114 LEIVGLRETAGRRlSTFSL--GMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKA 191
Cdd:PRK13651 149 IELVGLDESYLQR-SPFELsgGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDN 227
|
90 100
....*....|....*....|....
gi 517388152 192 AGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13651 228 VLEWTKRTIFFKDGKIIKDGDTYD 251
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-69 |
2.56e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 46.26 E-value: 2.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHR 69
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLeEPTSGEILFDGQDITG 84
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-186 |
3.09e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.46 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEP-G--RGITLFGGRPLH----RHTHPAGAV-------------- 77
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhGtyEGEIIFEGEELQasniRDTERAGIAiihqelalvkelsv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 --GVLLGDVPGHPSRT--ARGHLRmlaaaagapaerADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLL 153
Cdd:PRK13549 100 leNIFLGNEITPGGIMdyDAMYLR------------AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLIL 167
|
170 180 190
....*....|....*....|....*....|...
gi 517388152 154 DDPAQGLSPHDTAWLYGLLKAYAARGgavvVTC 186
Cdd:PRK13549 168 DEPTASLTESETAVLLDIIRDLKAHG----IAC 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-212 |
3.56e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 45.26 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVL-RLMLELEPGRGITLFGGR-----PLHRHTHPAGAVgvllgdVPGHP---S 89
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLgTLCGDPRATSGRIVFDGKditdwQTAKIMREAVAI------VPEGRrvfS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 90 R-TARGHLRM--LAAAAGAPAERADQVLEIVG-LRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDT 165
Cdd:PRK11614 94 RmTVEENLAMggFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 517388152 166 AWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQS 212
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-67 |
4.94e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 4.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 13 RGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPL 67
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLiSPTSGTLLFEGEDI 71
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-215 |
5.00e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 2 VIQAIGLTSASRGEEppAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEP---GR------GITLFggrPLHRHTH 72
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrdaGNiiiddeDISLL---PLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 73 PAgavgvlLGDVPGHPS--RTARGHLRMLAAAAGAPAERADQ-------VLE---IVGLRETAGRRLSTfslGMDRRLGV 140
Cdd:PRK10895 78 RG------IGYLPQEASifRRLSVYDNLMAVLQIRDDLSAEQredraneLMEefhIEHLRDSMGQSLSG---GERRRVEI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 141 AAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-58 |
6.70e-05 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 45.44 E-value: 6.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 2 VIQAIGLtSASRGEEPpAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRG 58
Cdd:COG0488 315 VLELEGL-SKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAgELEPDSG 370
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-213 |
7.21e-05 |
|
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: 45.59 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPG---RGITLFGGRPLH----RHTHPAGAV-------------- 77
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtwDGEIYWSGSPLKasniRDTERAGIViihqeltlvpelsv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 --GVLLGDVPGHPSRtarghlRMLAAAAGAPAERADQVLEIVGLRETagRRLSTFSLGMDRRLGVAAALLGDPPALLLDD 155
Cdd:TIGR02633 96 aeNIFLGNEITLPGG------RMAYNAMYLRAKNLLRELQLDADNVT--RPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 156 PAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSA 213
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDM 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-221 |
7.93e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.29 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 24 SFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRG--ITLFGGRPLHRHTHPAGAVGVLL--------GDVPGHPSR--- 90
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAgqVYLDGKPIDIRSPRDAIRAGIMLcpedrkaeGIIPVHSVAdni 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 91 --TARGHLRMLAAAAGAPAERADQVLEIVGLR-ETAGRR--LSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDT 165
Cdd:PRK11288 353 niSARRHHLRAGCLINNRWEAENADRFIRSLNiKTPSREqlIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAK 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 166 AWLYGLLKAYAARGGAVVVTCAD-PKAAGrLGDRVVTLDKGRLVADQSAHEFGRRRL 221
Cdd:PRK11288 433 HEIYNVIYELAAQGVAVLFVSSDlPEVLG-VADRIVVMREGRIAGELAREQATERQA 488
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
114-215 |
8.79e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.84 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 114 LEIVGLRETAGRRlSTFSL--GMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKA 191
Cdd:PRK13631 160 LNKMGLDDSYLER-SPFGLsgGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEH 238
|
90 100
....*....|....*....|....
gi 517388152 192 AGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13631 239 VLEVADEVIVMDKGKILKTGTPYE 262
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-156 |
9.41e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 43.86 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 1 MVIQAIGLTSASRGEepPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGR-----PLHRHTHpA 74
Cdd:COG1137 2 MTLEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVkPDSGRIFLDGEdithlPMHKRAR-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 75 GavgvlLGDVPGHPS--R--TARGHLR----MLAAAAGAPAERADQVLE---IVGLRETAGRRLSTfslGMDRRLGVAAA 143
Cdd:COG1137 79 G-----IGYLPQEASifRklTVEDNILavleLRKLSKKEREERLEELLEefgITHLRKSKAYSLSG---GERRRVEIARA 150
|
170
....*....|...
gi 517388152 144 LLGDPPALLLDDP 156
Cdd:COG1137 151 LATNPKFILLDEP 163
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-215 |
9.65e-05 |
|
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: 44.14 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 13 RGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGG--------RPLHRHthpagaVGVLLGD 83
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDSGRILIDGhdvrdytlASLRRQ------IGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 84 V---------------PG-------HPSRTARGHlrmlaaaagapaeraDQVLEI-VGLRETAGRRLSTFSLGMDRRLGV 140
Cdd:cd03251 85 VflfndtvaeniaygrPGatreeveEAARAANAH---------------EFIMELpEGYDTVIGERGVKLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 141 AAALLGDPPALLLDDPAQGLsphDTAWLY----GLLKAYAARGGAVVvtcadpkaAGRL-----GDRVVTLDKGRLVaDQ 211
Cdd:cd03251 150 ARALLKDPPILILDEATSAL---DTESERlvqaALERLMKNRTTFVI--------AHRLstienADRIVVLEDGKIV-ER 217
|
....
gi 517388152 212 SAHE 215
Cdd:cd03251 218 GTHE 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
111-215 |
1.10e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 44.24 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 111 DQVLEIVGLRETAGRRlSTFSL--GMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGG--AVVVTC 186
Cdd:PRK13634 126 REMIELVGLPEELLAR-SPFELsgGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGltTVLVTH 204
|
90 100
....*....|....*....|....*....
gi 517388152 187 ADPKAAgRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13634 205 SMEDAA-RYADQIVVMHKGTVFLQGTPRE 232
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-214 |
1.14e-04 |
|
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: 44.79 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 22 DLSFdaRPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHTHPA-----GAV-------GVLLGDVPGHP 88
Cdd:COG4615 352 DLTI--RRGELVFIVGGNGSGKSTLAKLLTGLyRPESGEILLDGQPVTADNREAyrqlfSAVfsdfhlfDRLLGLDGEAD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 SRTARGHLRMLaaaagapaeradQVLEIVGLRetaGRRLST--FSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTA 166
Cdd:COG4615 430 PARARELLERL------------ELDHKVSVE---DGRFSTtdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 517388152 167 WLYG-LLKAYAARGGAVVVTCADPKAAGrLGDRVVTLDKGRLVADQSAH 214
Cdd:COG4615 495 VFYTeLLPELKARGKTVIAISHDDRYFD-LADRVLKMDYGKLVELTGPA 542
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-208 |
1.24e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.96 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 16 EPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGG------------RPLHRHthpagaVGVL-- 80
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDtlitstsknkdiKQIRKK------VGLVfq 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 -----------LGDVPGHPS----------RTARGHLRMlaaaagapaeradqvleiVGLRETAGRRlSTFSL--GMDRR 137
Cdd:PRK13649 93 fpesqlfeetvLKDVAFGPQnfgvsqeeaeALAREKLAL------------------VGISESLFEK-NPFELsgGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517388152 138 LGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLV 208
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-243 |
1.37e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 43.85 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 16 EPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHT-------------HPAGA-VGVL 80
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITVGGMVLSEETvwdvrrqvgmvfqNPDNQfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 81 LGD----------VPghpsrtargHLRMLaaaagapaERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPA 150
Cdd:PRK13635 99 VQDdvafglenigVP---------REEMV--------ERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 151 LLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCA-DPKAAGRlGDRVVTLDKGRLVAD---QSAHEFGRRRLRpyVA 226
Cdd:PRK13635 162 IILDEATSMLDPRGRREVLETVRQLKEQKGITVLSIThDLDEAAQ-ADRVIVMNKGEILEEgtpEEIFKSGHMLQE--IG 238
|
250
....*....|....*..
gi 517388152 227 VHSPQAERLGLLLTDDG 243
Cdd:PRK13635 239 LDVPFSVKLKELLKRNG 255
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-183 |
1.40e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.66 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 23 LSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITL-FGGRPLHRHThPAGA--VGVLLgdVPGHPsrtarghlrML 99
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeIGGNPCARLT-PAKAhqLGIYL--VPQEP---------LL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 100 AAAAGapaeradqVLE--IVGL--RETAGRRLSTF--SLGMDRRLGVAAA---------------LLGDPPALLLDDPAQ 158
Cdd:PRK15439 98 FPNLS--------VKEniLFGLpkRQASMQKMKQLlaALGCQLDLDSSAGslevadrqiveilrgLMRDSRILILDEPTA 169
|
170 180
....*....|....*....|....*
gi 517388152 159 GLSPHDTAWLYGLLKAYAARGGAVV 183
Cdd:PRK15439 170 SLTPAETERLFSRIRELLAQGVGIV 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
15-218 |
1.70e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 43.57 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 15 EEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRL---MLELEPGRGITLfgGRPLHRHT-----HPAGAV--------- 77
Cdd:PRK13650 18 QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLidgLLEAESGQIIID--GDLLTEENvwdirHKIGMVfqnpdnqfv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 78 -GVLLGDVPGHPSRTARGHLRMlaaaagapAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:PRK13650 96 gATVEDDVAFGLENKGIPHEEM--------KERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE-FGR 218
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSR 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-215 |
1.99e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 43.20 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 13 RGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRH--THPAGAVGVLLG------- 82
Cdd:PRK13648 18 QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEkVKSGEIFYNNQAITDDnfEKLRKHIGIVFQnpdnqfv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 83 ------DVPGHPSRTARGHLRMlaaaagapAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:PRK13648 98 gsivkyDVAFGLENHAVPYDEM--------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTE 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-172 |
3.73e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 42.41 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 22 DLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITlfggrplhRHTHpagavGVLLGDVPGHPSRTARGHL---R 97
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVI--------KRNG-----KLRIGYVPQKLYLDTTLPLtvnR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 98 MLAAAAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLL 172
Cdd:PRK09544 89 FLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-215 |
5.88e-04 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 41.61 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLM--LeLEPGRGITLFGGRPLHR-----------------HTHPAGAVG 78
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrL-LPPDSGEVLVDGLDVATtpsrelakrlailrqenHINSRLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 79 --VLLGDVPGHPSR-TARGHLRMlaaaagapaeraDQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDD 155
Cdd:COG4604 94 elVAFGRFPYSKGRlTAEDREII------------DEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517388152 156 PAQGLSPHDTAWLYGLLKAYA-ARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAHE 215
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLAdELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-50 |
6.37e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 42.00 E-value: 6.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 517388152 10 SASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLM 50
Cdd:PRK13633 16 SNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHM 56
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-269 |
6.99e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.54 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 16 EPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLhrHTHPAGAVGVLLGDVPG-------- 86
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLvESQGGEIIFNGQRI--DTLSPGKLQALRRDIQFifqdpyas 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 87 -HPSRTA--------RGHlRMLAAAAGAPAERadQVLEIVGLR-ETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDP 156
Cdd:PRK10261 414 lDPRQTVgdsimeplRVH-GLLPGKAAAARVA--WLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 157 AQGLSPHDTAWLYGLLKAYAARGG-AVVVTCADPKAAGRLGDRVVTLDKGRLVadqsahEFGRRRL------RPY----- 224
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGiAYLFISHDMAVVERISHRVAVMYLGQIV------EIGPRRAvfenpqHPYtrklm 564
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 517388152 225 --VAVHSPQAER-LGLLLTDDGTEITHESGSRIRVhgATTAQVGEAAF 269
Cdd:PRK10261 565 aaVPVADPSRQRpQRVLLSDDLPSNIHLRGEEVAA--VSLQCVGPGHY 610
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-162 |
7.84e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.11 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 24 SFDARPGEITVLLGDGGAGKSTVLRLMLE-LEPGRGITLFGGRPlHRHTHPAG-AVGVL-----------------LGDV 84
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGfLTPASGSLTLNGQD-HTTTPPSRrPVSMLfqennlfshltvaqnigLGLN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517388152 85 PGhpsrtarghLRMlaaaAGAPAERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSP 162
Cdd:PRK10771 98 PG---------LKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-65 |
1.34e-03 |
|
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: 40.15 E-value: 1.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 517388152 15 EEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGR 65
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLgELEKLSGSVSVPGS 67
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-217 |
1.72e-03 |
|
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: 40.17 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 13 RGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTV----LRlMLELEPGRgITLfggrplhrhthpagaVGVLLGDVPGHP 88
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFR-LVELSSGS-ILI---------------DGVDISKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 89 SRTA-----------RGHLRM-LAAAAGAPAERADQVLEIVGLRETAGRRL-----------STFSLGMDRRLGVAAALL 145
Cdd:cd03244 76 LRSRisiipqdpvlfSGTIRSnLDPFGEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517388152 146 GDPPALLLDDPAQGLSPHDTAWLYGLLKAYAArgGAVVVTCADpkaagRLG-----DRVVTLDKGRLVadqsahEFG 217
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAH-----RLDtiidsDRILVLDKGRVV------EFD 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-216 |
2.28e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.77 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 17 PPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRG--ITLfGGRPLHRHThPAGAV--GVLL--------GDV 84
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSgeIRL-DGKPVRIRS-PRDAIraGIAYvpedrkgeGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 85 PGHPSR--TARGHLRMLAAAAGAPAERADQVLeivglrETAGRRLSTFSLGMDRRLG-----------VAAALLGDPPAL 151
Cdd:COG1129 343 LDLSIRenITLASLDRLSRGGLLDRRRERALA------EEYIKRLRIKTPSPEQPVGnlsggnqqkvvLAKWLATDPKVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 152 LLDDPAQGLsphD---TAWLYGLLKAYAARGGAVVVTCAD-PKAAGrLGDRVVTLDKGRLVADQSAHEF 216
Cdd:COG1129 417 ILDEPTRGI---DvgaKAEIYRLIRELAAEGKAVIVISSElPELLG-LSDRILVMREGRIVGELDREEA 481
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-215 |
2.47e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 20 VDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGR--GITLFGGRPLH-RHTHPAGAVGVLL--------GDVP--- 85
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRweGEIFIDGKPVKiRNPQQAIAQGIAMvpedrkrdGIVPvmg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 86 -GH-------PSRTARGHLrmlaaaagapaeraDQVLEIVGLRETAGR-RLSTFSL---------GMDRRLGVAAALLGD 147
Cdd:PRK13549 358 vGKnitlaalDRFTGGSRI--------------DDAAELKTILESIQRlKVKTASPelaiarlsgGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517388152 148 PPALLLDDPAQGLSPHDTAWLYGLLKAYAARGGAVVVTCAD-PKAAGrLGDRVVTLDKGRLVADQSAHE 215
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSElPEVLG-LSDRVLVMHEGKLKGDLINHN 491
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-162 |
3.08e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEP---GRGITLFGGR--------PLHRHT-------HPAGAVGV 79
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPqgySNDLTLFGRRrgsgetiwDIKKHIgyvssslHLDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 LLGDV--PG-HPS----RTARGHLRMLAaaagapaeraDQVLEIVGL-RETAGRRLSTFSLGMDRRLGVAAALLGDPPAL 151
Cdd:PRK10938 354 SVRNVilSGfFDSigiyQAVSDRQQKLA----------QQWLDILGIdKRTADAPFHSLSWGQQRLALIVRALVKHPTLL 423
|
170
....*....|.
gi 517388152 152 LLDDPAQGLSP 162
Cdd:PRK10938 424 ILDEPLQGLDP 434
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-63 |
4.01e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 39.20 E-value: 4.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517388152 2 VIQAIGLTSASRGEEPPAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRG-ITLFG 63
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLlKPQSGeIKIDG 70
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
30-248 |
4.34e-03 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 39.28 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 30 GEITVLLGDGGAGKSTVLRLMLELE-PGRGITLFGGRPLHRHTH------------PAGAV--GVLLGdvpghpsrtARG 94
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLEtPSAGELLAGTAPLAEAREdtrlmfqdarllPWKKVidNVGLG---------LKG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 95 HLRmlaaaagapaERADQVLEIVGLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLDDPAQGLSPHDTAWLYGLLKA 174
Cdd:PRK11247 109 QWR----------DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIES 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517388152 175 -YAARGGAVVVTCADPKAAGRLGDRVVTLDKGRLVADQSAhEFGRRRLRPYVAVHSPQAERLGLLLTDDGTEITH 248
Cdd:PRK11247 179 lWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTV-DLPRPRRRGSARLAELEAEVLQRVMSRGESEPTR 252
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-71 |
4.96e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 4.96e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLEL-EPGRGITLFGGRPLHRHT 71
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIyQKDSGSILFQGKEIDFKS 66
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-60 |
6.37e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 38.60 E-value: 6.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTVLRL---MLELEPGRGIT 60
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrMNDLNPEVTIT 64
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-65 |
6.95e-03 |
|
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: 38.68 E-value: 6.95e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLML-ELEPGRGITLFGGR 65
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSGR 99
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-50 |
7.13e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.00 E-value: 7.13e-03
10 20 30
....*....|....*....|....*....|..
gi 517388152 19 AVDDLSFDARPGEITVLLGDGGAGKSTvlrLM 50
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKST---LM 44
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-208 |
7.65e-03 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 39.06 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 18 PAVDDLSFDARPGEITVLLGDGGAGKSTVLRLMLELEPGRGITLFGGRPLHR--HTH--------------PAGAV--GV 79
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELREldPESwrkhlswvgqnpqlPHGTLrdNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517388152 80 LLGDVPGHPSRtarghLRMLAAAAgapaeradQVLEIV-----GLRETAGRRLSTFSLGMDRRLGVAAALLGDPPALLLD 154
Cdd:PRK11174 444 LLGNPDASDEQ-----LQQALENA--------WVSEFLpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 517388152 155 DPAQGLSPHDTAWLYGLLKAYAARGGAVVVT--CADPKAAgrlgDRVVTLDKGRLV 208
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAASRRQTTLMVThqLEDLAQW----DQIWVMQDGQIV 562
|
|
| |
