|
Name |
Accession |
Description |
Interval |
E-value |
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-298 |
1.45e-142 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 403.34 E-value: 1.45e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAItAKVGYMPEE 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-RRIGYLPEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:COG4152 80 RGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 161 LDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLRLDIEGYQNVERLKRI 240
Cdd:COG4152 160 LDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAGWLRAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 241 QGVKKVTLMANGVHLELNNEQCGKIIFTEVTKHGYVPVFNQHYPDLEAIFKYEVHKKA 298
Cdd:COG4152 240 PGVTVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-212 |
1.34e-96 |
|
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: 283.40 E-value: 1.34e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITaKVGYMPEER 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN-RIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 GLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGL 161
Cdd:cd03269 80 GLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 162 DPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-221 |
4.33e-81 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 244.97 E-value: 4.33e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK--VGYMPE 79
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 160 GLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQF 221
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-227 |
7.00e-76 |
|
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: 232.06 E-value: 7.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYMP 78
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRkePREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPF 158
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 159 SGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLRLD 227
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-207 |
3.47e-61 |
|
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: 191.84 E-value: 3.47e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK--VGYMPE 79
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYfaalhgmkkaeaiillddwmkrlnvvgkstdkieslSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:cd03230 81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 951434962 160 GLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-212 |
4.46e-53 |
|
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: 172.94 E-value: 4.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKV 74
Cdd:cd03266 1 MITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVkePAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYMPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 155 DEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-217 |
3.11e-47 |
|
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: 157.67 E-value: 3.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN--FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYM 77
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRtdRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 158 FSGLDPVnSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:cd03263 161 TSGLDPA-SRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
8.11e-47 |
|
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: 157.11 E-value: 8.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA---KVGYM 77
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 ---PEerglypketikSQLLY--------FAALH-GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACL 145
Cdd:COG1122 81 fqnPD-----------DQLFAptveedvaFGPENlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 146 MFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLE 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-212 |
2.70e-46 |
|
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: 155.07 E-value: 2.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKI-LWSGKPLTPDAITAKVGYMPEE 80
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHGMKKAEAiillddwMKRLNVVGKST---DKIESLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRI-------DEVLDVVGLKDsakKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 158 FSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-217 |
1.34e-45 |
|
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: 154.13 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITakvgymp 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITglpPHEIA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 eERG---------LYPKETI----------KSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKV 139
Cdd:cd03219 74 -RLGigrtfqiprLFPELTVlenvmvaaqaRTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 140 QLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:cd03219 153 EIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
9.62e-45 |
|
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: 151.09 E-value: 9.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYMP 78
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRdaREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERGLYPKETIKSQLLYFAALHGMKKAEAiiLLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPF 158
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 951434962 159 SGLDPVNSELLIKAILTAKQQGTMVIFSTH---NMDNVQKLS 197
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHqplELAAARVLD 201
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-290 |
1.29e-44 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 153.70 E-value: 1.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 9 KRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYMPEERGLYPK 86
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVrePRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNS 166
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 167 ELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGR-----LRLDIEGYQNVERLKRIQ 241
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKdtlesRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 242 ------GVKKVTLMANGVHLELNN-EQCGKIIFTEVTKHGY-VPVFNQHYPDLEAIF 290
Cdd:TIGR01188 241 lgetglGLLAVTVDSDRIKILVPDgDETVPEIVEAAIRNGIrIRSISTERPSLDDVF 297
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
6.99e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.16 E-value: 6.99e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAitAKVGYMPEE 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR--RRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGL---YP---KETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVqLIA-CLMFKPQLLI 153
Cdd:COG1121 84 AEVdwdFPitvRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV-LLArALAQDPDLLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQtVLKGTPTEIYRQ 220
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGL-VAHGPPEEVLTP 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-217 |
3.38e-42 |
|
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: 145.95 E-value: 3.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAkvgym 77
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpPHRIAR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 peeRG---------LYPKET----------IKSQLLYFAALHGMKK-----AEAIILLDDWMKRLNVVGKSTDKIESLSK 133
Cdd:COG0411 79 ---LGiartfqnprLFPELTvlenvlvaahARLGRGLLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 134 GNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEG 235
|
....*
gi 951434962 213 TPTEI 217
Cdd:COG0411 236 TPAEV 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-206 |
8.72e-42 |
|
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: 143.44 E-value: 8.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDaiTAKVGYMPEERG 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--RKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 L---YP---KETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVqLIA-CLMFKPQLLILD 155
Cdd:cd03235 79 IdrdFPisvRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRV-LLArALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 156 EPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHG 206
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-212 |
8.14e-41 |
|
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: 140.79 E-value: 8.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGqILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYMPE 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkqPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 951434962 160 GLDPVnSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03264 160 GLDPE-ERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-219 |
9.86e-41 |
|
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: 141.67 E-value: 9.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN-FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGYM 77
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqdPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNV-VGKSTDKIES-LSKGNAQKVQLIACLMFKPQLLILD 155
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdPAEFADRYPHeLSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 156 EPFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYR 219
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-207 |
1.42e-40 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 140.29 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFGNFN--AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD---AITAKVGYM 77
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLslkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 ---PEerglypketikSQLLY--------FAALH-GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACL 145
Cdd:cd03225 81 fqnPD-----------DQFFGptveeevaFGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 146 MFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
1.04e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.16 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PdaitakvgymP 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglP----------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERG---------LYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKP 149
Cdd:COG3842 75 EKRNvgmvfqdyaLFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951434962 150 QLLILDEPFSGLDPVNSE---LLIKAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:COG3842 155 RVLLLDEPLSALDAKLREemrEELRRLQ--RELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-207 |
1.06e-39 |
|
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: 136.22 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA---KVGYMPE 79
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 erglypketiksqllyfaalhgmkkaeaiillddwmkrlnvvgkstdkiesLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 951434962 160 GLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-217 |
2.13e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 138.64 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGYM 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAslsRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEER--------------GLYPketiksqllYFAALHGMKKA-EAIIllDDWMKRLNVVGKSTDKIESLSKGNAQKVqLI 142
Cdd:COG1120 81 PQEPpapfgltvrelvalGRYP---------HLGLFGRPSAEdREAV--EEALERTGLEHLADRPVDELSGGERQRV-LI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 143 A-CLMFKPQLLILDEPFSGLDPVNS-ELL--IKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG1120 149 ArALAQEPPLLLLDEPTSHLDLAHQlEVLelLRRL--ARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-207 |
2.45e-39 |
|
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: 136.16 E-value: 2.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAIT-----AKVGY 76
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpplrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLYfaalhgmkkaeaiillddwmkrlnvvgkstdkieSLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 951434962 157 PFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
8.51e-39 |
|
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: 142.73 E-value: 8.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF-----GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD------A 69
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrslrE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 70 ITAKVGY---MPeERGLYPKETIKSQLLYFAALHG-MKKAEAIILLDDWMKRlnvVGKSTDKIE----SLSKGNAQKVqL 141
Cdd:COG1123 340 LRRRVQMvfqDP-YSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLER---VGLPPDLADryphELSGGQRQRV-A 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 142 IAC-LMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYR 219
Cdd:COG1123 415 IARaLALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
.
gi 951434962 220 Q 220
Cdd:COG1123 495 N 495
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-217 |
3.11e-38 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 134.48 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAK-VGYM 77
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKSQLLYFAALHGMKKAEAIIlldDWM--------KRLNVVGkstdkiESLSKGNAQkvQL-IA-CLMF 147
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARL---ERVyelfprlkERRKQLA------GTLSGGEQQ--MLaIArALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 148 KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-217 |
4.51e-38 |
|
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: 134.03 E-value: 4.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAIT--AKVGYMPE 79
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvrRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 160 GLDPVNSELL---IKAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:cd03265 161 GLDPQTRAHVweyIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-209 |
8.12e-38 |
|
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: 131.40 E-value: 8.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGym 77
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFasprDARRAGIA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 peerglypkeTIkSQllyfaalhgmkkaeaiillddwmkrlnvvgkstdkiesLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03216 79 ----------MV-YQ--------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 951434962 158 FSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-212 |
9.41e-38 |
|
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: 131.79 E-value: 9.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVGYMPe 79
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLaslSPKELARKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 erglypketiksQLlyfaalhgmkkaeaiillddwMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:cd03214 80 ------------QA---------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 160 GLDPVNS-ELL--IKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03214 127 HLDIAHQiELLelLRRL--ARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-221 |
2.17e-37 |
|
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: 132.21 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPdaITAKVGYM 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG--PGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 158 FSGLDPVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQKLSDYIVmlkhgqtVLKGTPTEIYRQF 221
Cdd:cd03293 159 FSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVV-------VLSARPGRIVAEV 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
4.22e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.52 E-value: 4.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF----GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdAITAKVGY 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT--GPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:COG1116 85 VFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 157 PFSGLDPV-----NSELLikAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHG 206
Cdd:COG1116 165 PFGALDALtrerlQDELL--RLW--QETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-209 |
5.90e-37 |
|
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: 131.10 E-value: 5.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT-PDAITAKVGYMPEE 80
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTgVPPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 951434962 161 LDP-VNSEL--LIKAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:cd03259 161 LDAkLREELreELKELQ--RELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-218 |
6.79e-37 |
|
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: 131.51 E-value: 6.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK----VGYM 77
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 158 FSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
1.61e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 133.42 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA--KVGYMPE 79
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAraRIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYFAALHGMK--KAEAII--LLDdwMKRLNvvGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILD 155
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMStrEIEAVIpsLLE--FARLE--SKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 156 EPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
1.98e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.56 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD------AITAK 73
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgralrRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 74 VGYMPEERGLYP---------------KETIKSQLLYFAALHgmkKAEAIILLDdwmkRLNVVGKSTDKIESLSKGNAQK 138
Cdd:COG3638 82 IGMIFQQFNLVPrlsvltnvlagrlgrTSTWRSLLGLFPPED---RERALEALE----RVGLADKAYQRADQLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 139 VQlIA-CLMFKPQLLILDEPFSGLDPVNSEL---LIKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTP 214
Cdd:COG3638 155 VA-IArALVQEPKLILADEPVASLDPKTARQvmdLLRRI--AREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231
|
...
gi 951434962 215 TEI 217
Cdd:COG3638 232 AEL 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-209 |
1.56e-35 |
|
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: 127.62 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFN----AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP------DAI 70
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 71 TAKVGYMPEE--RGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKrLNVVGKSTDKIES----LSKGNAQKVqLIA- 143
Cdd:cd03257 81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLL-LVGVGLPEEVLNRypheLSGGQRQRV-AIAr 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 144 CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-217 |
1.22e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 127.61 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA--KVGYMPE 79
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 160 GLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-220 |
1.28e-34 |
|
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: 125.43 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP-DAITAKVGYMPEE 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 161 LD-PVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:cd03300 161 LDlKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-209 |
1.56e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.92 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGy 76
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIrsprDAIALGIG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 M----------------------PEERGLYPKETIKSQLLYFAALHGMKkaeaiILLDdwmkrlnvvgkstDKIESLSKG 134
Cdd:COG3845 84 MvhqhfmlvpnltvaenivlglePTKGGRLDRKAARARIRELSERYGLD-----VDPD-------------AKVEDLSVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 135 NAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-220 |
5.07e-34 |
|
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: 130.26 E-value: 5.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGYM 77
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdldPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLyPKETIKSQLLyFAALHG----MKKAEAIILLDDWMKRLN-----VVGkstdkiES---LSKGNAQKVQLIACL 145
Cdd:COG4988 417 PQNPYL-FAGTIRENLR-LGRPDAsdeeLEAALEAAGLDEFVAALPdgldtPLG------EGgrgLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 146 MFKPQLLILDEPFSGLDPVNSELLIKAILTAKqQGTMVIFSTHNMDNVqKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-209 |
8.81e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.60 E-value: 8.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGY 76
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrsprDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYP-----------KETIKSQLLYFAALHgmKKAEAIillddwMKRLNVVGKSTDKIESLSKGNAQKVQlIA-C 144
Cdd:COG1129 84 IHQELNLVPnlsvaeniflgREPRRGGLIDWRAMR--RRAREL------LARLGLDIDPDTPVGDLSVAQQQLVE-IArA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 145 LMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-221 |
9.67e-34 |
|
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: 123.17 E-value: 9.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP------DAITAKV 74
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekelYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYM------------------P-EERGLYPKETIksqllyfaalhgmkkaEAIILLddwmkRLNVVG--KSTDKIES-LS 132
Cdd:COG1127 85 GMLfqggalfdsltvfenvafPlREHTDLSEAEI----------------RELVLE-----KLELVGlpGAADKMPSeLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 133 KGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLK 211
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*..
gi 951434962 212 GTPTEIY-------RQF 221
Cdd:COG1127 224 GTPEELLasddpwvRQF 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
1.05e-33 |
|
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: 123.00 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP-------------- 67
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaelyrlrrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 68 ---------DAITAK--VGYMPEERGLYPKETIKSQLLYFAALHGMKKAEaiillddwmkrlnvvgkstDKIES-LSKGN 135
Cdd:cd03261 81 mlfqsgalfDSLTVFenVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-------------------DLYPAeLSGGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 136 AQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTP 214
Cdd:cd03261 142 KKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
...
gi 951434962 215 TEI 217
Cdd:cd03261 222 EEL 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-217 |
2.78e-33 |
|
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: 122.01 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAK-VGY 76
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITglpPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLYFAALHGMKKAEAIILldDWM--------KRLNVVGKstdkieSLSKGNAQkvQL-IA-CLM 146
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDRAEVRADL--ERVyelfprlkERRRQRAG------TLSGGEQQ--MLaIGrALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 147 FKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-212 |
4.40e-33 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 121.35 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITaKVGYMPEER 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLH-KIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 GLYPKETIKSQLLYFAALHGMKKAEAIILLDdwMKRLNVVGKStdKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGL 161
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLPDSRIDEVLN--IVDLTNTGKK--KAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 162 DPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:TIGR03740 156 DPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQG 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-159 |
1.40e-32 |
|
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: 117.75 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA---KVGYMPEERGLYPKETIKSQL 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 94 LYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIE----SLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-218 |
2.32e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 119.75 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNaVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP-DAITAKVGYMPEE 80
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 161 LDPVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:cd03299 160 LDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-218 |
4.46e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.98 E-value: 4.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAIT--AK--VGY 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHkrARlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEE----RGLypkeTIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQlIA-CLMFKPQL 151
Cdd:COG1137 83 LPQEasifRKL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVE-IArALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951434962 152 LILDEPFSGLDPVN-SEllIKAILT-AKQQGTMVIFSTHnmdNVQ---KLSD--YIvmLKHGQTVLKGTPTEIY 218
Cdd:COG1137 158 ILLDEPFAGVDPIAvAD--IQKIIRhLKERGIGVLITDH---NVRetlGICDraYI--ISEGKVLAEGTPEEIL 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-209 |
9.68e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.46 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN-FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITA---K 73
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkRREIPYlrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 74 VGYMPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVqLIA-CLMFKPQLL 152
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRV-AIArALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 153 ILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-217 |
1.43e-31 |
|
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: 117.28 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKST---TFHMILDFIK--PDSGKILWSGKPL-----TPDAIT 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPgaPDEGEVLLDGKDIydldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 72 AKVGYMPEERGLYPKeTIKSQLLYFAALHGMKKAEAI----------ILLDDWMK-RLNVVGkstdkiesLSKGNAQKVQ 140
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELderveealrkAALWDEVKdRLHALG--------LSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 141 LIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQgTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
1.73e-31 |
|
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: 122.70 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF--GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPD---SGKILWSGKPL---TPDAITA 72
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlelSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 KVGYMPEE--RGLYPkETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQ 150
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 151 LLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALA 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-207 |
1.85e-31 |
|
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: 115.17 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN--AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVGY 76
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrdlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYpKETIKSqllyfaalhgmkkaeaiillddwmkrlNVvgkstdkiesLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:cd03228 81 VPQDPFLF-SGTIRE---------------------------NI----------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 157 PFSGLDPVNSELLIKAILTAKQQGTmVIFSTHNMDNVQKlSDYIVMLKHGQ 207
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKT-VIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-209 |
1.50e-30 |
|
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: 113.89 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFG-NFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKVGYMPEE- 80
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 -RGLYpKETIKSQLLYFAALHGMKKAEAiillDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:cd03226 81 dYQLF-TDSVREELLLGLKELDAGNEQA----ETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 951434962 160 GLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-217 |
1.56e-30 |
|
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: 114.97 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN-FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD------AITAKV 74
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYMPEERGLYPKETIKSQLL--------YFAALHGM----KKAEAIILLDdwmkRLNVVGKSTDKIESLSKGNAQKVQLI 142
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLsgrlgrrsTWRSLFGLfpkeEKQRALAALE----RVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 143 ACLMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
2.12e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 117.10 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdaitakvGYMPEE 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--------DLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RG---------LYP----KETIKSQLlyfaALHGMKKAE--------AIIL-LDDWMKRlnvvgkstdKIESLSKGNAQK 138
Cdd:COG3839 75 RNiamvfqsyaLYPhmtvYENIAFPL----KLRKVPKAEidrrvreaAELLgLEDLLDR---------KPKQLSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 139 VQLIACLMFKPQLLILDEPFSGLDP---VNSELLIKAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPT 215
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAklrVEMRAEIKRLH--RRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
....*
gi 951434962 216 EIYRQ 220
Cdd:COG3839 220 ELYDR 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-220 |
2.24e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 117.17 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpltpDAITA------KVG 75
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR----DLFTNlpprerRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEERGLYPKETIksqllyF----AALHGMKKAEAII--LLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKP 149
Cdd:COG1118 79 FVFQHYALFPHMTV------AeniaFGLRVRPPSKAEIraRVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951434962 150 QLLILDEPFSGLDP-VNSEL--LIKAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:COG1118 153 EVLLLDEPFGALDAkVRKELrrWLRRLH--DELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-207 |
3.12e-30 |
|
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: 113.35 E-value: 3.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITA-- 72
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 --KVGYMPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVqLIA-CLMFKP 149
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRV-AIArALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 150 QLLILDEPFSGLDPVNSELLIKAIL-TAKQQGTMVIFSTHNMDnVQKLSDYIVMLKHGQ 207
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLReLNKEAGTTIVVVTHDPE-LAEYADRIIELRDGK 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-218 |
1.90e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 112.79 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 20 LSFSLHSgqILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD-----AITAKVGYM---PEERGLYPKetIKS 91
Cdd:PRK13638 22 LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSkrgllALRQQVATVfqdPEQQIFYTD--IDS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 92 QLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIK 171
Cdd:PRK13638 98 DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 951434962 172 AILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-225 |
2.56e-29 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 112.54 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFG-----NFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD------AI 70
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKkkkklkDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 71 TAKVGY---MPEERgLYpKETIKSQLLY----FaalhGMKKAEAIILLDDWMKrlnVVGKSTDKIE----SLSKGNAQKV 139
Cdd:TIGR04521 81 RKKVGLvfqFPEHQ-LF-EETVYKDIAFgpknL----GLSEEEAEERVKEALE---LVGLDEEYLErspfELSGGQMRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 140 QLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231
|
....*..
gi 951434962 219 RQFGRLR 225
Cdd:TIGR04521 232 SDVDELE 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-209 |
4.78e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.50 E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRfgnfNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGYMP 78
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIrsprDAIRAGIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EER---GLYPKETIK-----SQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTD-KIESLSKGNAQKVqLIA-CLMFK 148
Cdd:COG1129 334 EDRkgeGLVLDLSIRenitlASLDRLSRGGLLDRRRERALAEEYIKRLRIKTPSPEqPVGNLSGGNQQKV-VLAkWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 149 PQLLILDEPFSGLDpVNSelliKA-----ILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:COG1129 413 PKVLILDEPTRGID-VGA----KAeiyrlIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-217 |
6.32e-29 |
|
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: 111.58 E-value: 6.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 7 VSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdAITA---------KVGYM 77
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIA--AMSRkelrelrrkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 158 FSGLDPV-----NSELLikaILTAKQQGTMViFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:cd03294 188 FSALDPLirremQDELL---RLQAELQKTIV-FITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-218 |
9.43e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 110.47 E-value: 9.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN-FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP------DAITAK 73
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkklRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 74 VGYMPEERGLYPKETIKSQLLY------------FAALHGMKKAEAIILLDdwmkRLNVVGKSTDKIESLSKGNAQKVQL 141
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHgrlgykptwrslLGRFSEEDKERALSALE----RVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 142 IACLMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRiNKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-243 |
1.10e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.88 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN--AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA---ITAKVGY 76
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 M---PEERglYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK13635 86 VfqnPDNQ--FVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTAKQQGTMVIFS-THNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFGRLR---LDIE 229
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQeigLDVP 242
|
250
....*....|....*
gi 951434962 230 -GYQNVERLKRiQGV 243
Cdd:PRK13635 243 fSVKLKELLKR-NGI 256
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-217 |
4.27e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 108.92 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYMP 78
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 --EERGLYPKETIKSQLL----------YFAALH---GMKKAE--AIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQL 141
Cdd:PRK11300 85 tfQHVRLFREMTVIENLLvaqhqqlktgLFSGLLktpAFRRAEseALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 142 IACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-207 |
5.67e-28 |
|
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: 106.36 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGYMPEER---GLYPKET 88
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrsprDAIRAGIAYVPEDRkreGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 89 IksqllyfaalhgmkkAEAIILLDdwmkrlnvvgkstdkieSLSKGNAQKVqLIA-CLMFKPQLLILDEPFSGLDPVNSE 167
Cdd:cd03215 95 V---------------AENIALSS-----------------LLSGGNQQKV-VLArWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 951434962 168 LLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd03215 142 EIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-289 |
9.46e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.41 E-value: 9.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF----------GNF-----------NAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIl 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 60 wsgkpltpdaitaKV-GYMPEERGLYPKETI------KSQLLY----------FAALHGMKKAEAIILLDDWMKRLNVVG 122
Cdd:COG4586 80 -------------RVlGYVPFKRRKEFARRIgvvfgqRSQLWWdlpaidsfrlLKAIYRIPDAEYKKRLDELVELLDLGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 123 KSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDpVNSELLIKAILTA--KQQGTMVIFSTHNMDNVQKLSDYI 200
Cdd:COG4586 147 LLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD-VVSKEAIREFLKEynRERGTTILLTSHDMDDIEALCDRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 201 VMLKHGQTVLKGTPTEIYRQFG---RLRLDIEGYQNVERLKRiqGVKKVTLMANGVHLELNNEQCGKIIFTEVTKHGYVP 277
Cdd:COG4586 226 IVIDHGRIIYDGSLEELKERFGpykTIVLELAEPVPPLELPR--GGEVIEREGNRVRLEVDPRESLAEVLARLLARYPVR 303
|
330
....*....|..
gi 951434962 278 VFNQHYPDLEAI 289
Cdd:COG4586 304 DLTIEEPPIEEV 315
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-245 |
1.41e-27 |
|
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: 112.80 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP--DAITAKVGYMPEERGLYPKETIKSQL 93
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETnlDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 94 LYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVnSELLIKAI 173
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY-SRRSIWDL 1103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951434962 174 LTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGR-LRLDIegyqnVERLKRIQGVKK 245
Cdd:TIGR01257 1104 LLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTgFYLTL-----VRKMKNIQSQRG 1171
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-219 |
2.80e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 110.91 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKP---LTPdAITAKVG-Y 76
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarLTP-AKAHQLGiY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 M-PEERGLYPKETIKSQLLYfaalhGM-KKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:PRK15439 90 LvPQEPLLFPNLSVKENILF-----GLpKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 155 DEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGtPTEIYR 219
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG-KTADLS 228
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
4.22e-27 |
|
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: 110.63 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF--GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGY 76
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdldEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYpKETIKSQLLYF----------AALhgmKKAEaiilLDDWMKRLN-----VVGkstDKIESLSKGNAQKVQL 141
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRLArpdatdeelwAAL---ERVG----LGDWLAALPdgldtWLG---EGGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 142 IACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTmVIFSTHNMDNVQKLsDYIVMLKHGQTVLKGTPTEIYRQF 221
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT-VLLITHRLAGLERM-DRILVLEDGRIVEQGTHEELLAQN 560
|
....
gi 951434962 222 GRLR 225
Cdd:COG4987 561 GRYR 564
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-207 |
4.26e-27 |
|
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: 105.03 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdaitaKVGymPEER 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT------DLP--PKDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 G---------LYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLL 152
Cdd:cd03301 73 DiamvfqnyaLYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 153 ILDEPFSGLDP---VNSELLIKAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd03301 153 LMDEPLSNLDAklrVQMRAELKRLQ--QRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ 208
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-218 |
9.26e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 9.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD-------AITAKVGYM---PEERgLYpKET 88
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknlkKLRKKVSLVfqfPEAQ-LF-ENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 89 IKSQLLYFAALHGMKKAEAIILLDDWMKRlnvVGKSTDKIE----SLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPV 164
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLKK---VGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 951434962 165 NSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-222 |
1.13e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 109.83 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA--KVGYMPE 79
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATrrRVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 160 GLDPVNS----ELLIKaiLTAKQQGTmvIF-STHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFG 222
Cdd:NF033858 427 GVDPVARdmfwRLLIE--LSREDGVT--IFiSTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG 489
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-217 |
1.14e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.45 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNavsdLSFSLH--SGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAitakvgymP 78
Cdd:COG3840 1 MLRLDDLTYRYGDFP----LRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP--------P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERG---------LYPKETIKsQLLYFaALH-GMK-KAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMF 147
Cdd:COG3840 69 AERPvsmlfqennLFPHLTVA-QNIGL-GLRpGLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951434962 148 KPQLLILDEPFSGLDPV-NSEL--LIKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG3840 147 KRPILLLDEPFSALDPAlRQEMldLVDEL--CRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
1.18e-26 |
|
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: 109.54 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNF--NAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGY 76
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqidPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPkETIKSQLLYFAALHGMKKAEAII----LLDDWMKR---LN-VVGkstDKIESLSKGNAQKVqLIA-CLMF 147
Cdd:COG2274 554 VLQDVFLFS-GTIRENITLGDPDATDEEIIEAArlagLHDFIEALpmgYDtVVG---EGGSNLSGGQRQRL-AIArALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 148 KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTmVIFSTHNMDNVqKLSDYIVMLKHGQTVLKGTPTEIYRQFGR 223
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRT-VIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKGL 702
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-217 |
2.67e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 103.54 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD-----AITAKVG 75
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkdinKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEERGLYPKETIKSQLLYfaAL---HGMKKAEAIillDDWMKRLNVVGKStDKIES----LSKGNAQKVQlIA-CLMF 147
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTL--APikvKKMSKAEAE---ERAMELLERVGLA-DKADAypaqLSGGQQQRVA-IArALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951434962 148 KPQLLILDEPFSGLDP--VNsELLiKAILTAKQQG-TMVIfSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG1126 154 EPKVMLFDEPTSALDPelVG-EVL-DVMRDLAKEGmTMVV-VTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-209 |
2.99e-26 |
|
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: 102.76 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQhVSKRFGNFNAvsDLSFSLhSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA-------K 73
Cdd:cd03297 1 MLCVD-IEKRLPDFTL--KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqqrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 74 VGYMPEERGLYPKETIKSQLLYfaALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:cd03297 77 IGLVFQQYALFPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 154 LDEPFSGLD-PVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:cd03297 155 LDEPFSALDrALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-207 |
3.31e-26 |
|
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: 102.61 E-value: 3.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD-----AITAKVGY 76
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDkkninELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLYfaAL---HGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL--APikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 154 LDEPFSGLDP--VNSEL-LIKAIltAKQQGTMVIfSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd03262 159 FDEPTSALDPelVGEVLdVMKDL--AEEGMTMVV-VTHEMGFAREVADRVIFMDDGR 212
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-203 |
4.45e-26 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 102.31 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 4 LQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGK-PLTPDAITA------KVGY 76
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQeTPPLNSKKAskfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 951434962 157 PFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDnVQKLSDYIVML 203
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPE-VAKQADRVIEL 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-225 |
6.24e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.77 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN-FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA-----ITAKV 74
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglmkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYMPEErglyPKETIKSQLLY----FAALH-GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKP 149
Cdd:PRK13636 85 GMVFQD----PDNQLFSASVYqdvsFGAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 150 QLLILDEPFSGLDPVNSELLIKAIL-TAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVeMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-220 |
1.15e-25 |
|
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: 101.89 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP------DAI 70
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 71 TAKVGYMPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQ 150
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 151 LLILDEPFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
1.46e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGYM 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwsPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PE--------------ERGLYPketiksqllyfaalHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQL-- 141
Cdd:PRK13548 82 PQhsslsfpftveevvAMGRAP--------------HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLar 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 142 ----IACLMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTE 216
Cdd:PRK13548 148 vlaqLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-212 |
1.80e-25 |
|
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: 101.25 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGkilwsgkpltpdaiTAKV-GYMPEERGLYPKETI----- 89
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG--------------EVRVaGLVPWKRRKKFLRRIgvvfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 90 -KSQL---------LYF-AALHGMKKAEAIILLDDWMKRLNvVGKSTDK-IESLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03267 102 qKTQLwwdlpvidsFYLlAAIYDLPPARFKKRLDELSELLD-LEELLDTpVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 158 FSGLDpVNSELLIKAILTA--KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03267 181 TIGLD-VVAQENIRNFLKEynRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-225 |
1.81e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD-----AITAKVGYM---PEERGLYPke 87
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksllEVRKTVGIVfqnPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 88 TIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSE 167
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 168 LLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-225 |
2.13e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.70 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF--GNFN---AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdaitakvg 75
Cdd:COG1101 1 MLELKNLSKTFnpGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEER--------------GLYPKETIKSQLLyFAALHGMKKAEAIILL----DDWMKRLNVVG-----KSTDKIESLS 132
Cdd:COG1101 72 KLPEYKrakyigrvfqdpmmGTAPSMTIEENLA-LAYRRGKRRGLRRGLTkkrrELFRELLATLGlglenRLDTKVGLLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 133 KGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKaiLT----AKQQGT--MVifsTHNMDNVQKLSDYIVMLKHG 206
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE--LTekivEENNLTtlMV---THNMEQALDYGNRLIMMHEG 225
|
250 260
....*....|....*....|....*..
gi 951434962 207 QTVL--KG------TPTEIYRQFGRLR 225
Cdd:COG1101 226 RIILdvSGeekkklTVEDLLELFEEIR 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-217 |
5.51e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 5.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVGYM 77
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsmlSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERgLYPkETIKSQLL--Y----FAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQL 151
Cdd:PRK11231 82 PQHH-LTP-EGITVRELvaYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 152 LILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-217 |
6.12e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.97 E-value: 6.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 5 QHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK----VGYMPEE 80
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARarrgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAAL-HGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 160 GLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-191 |
7.27e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 98.65 E-value: 7.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD-----AITAKVGYM---PEERGLYPke 87
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSrkgllERRQRVGLVfqdPDDQLFAA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 88 TIkSQLLYFAALH-GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNS 166
Cdd:TIGR01166 85 DV-DQDVAFGPLNlGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGR 163
|
170 180
....*....|....*....|....*
gi 951434962 167 ELLIKAILTAKQQGTMVIFSTHNMD 191
Cdd:TIGR01166 164 EQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
8.93e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 8.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITA---KVGY 76
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 M---PEERGLYPkeTIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK13652 83 VfqnPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 154 LDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ---FGRLRLDIE 229
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQpdlLARVHLDLP 240
|
250
....*....|....
gi 951434962 230 GYQNVERLKRIQGV 243
Cdd:PRK13652 241 SLPKLIRSLQAQGI 254
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-220 |
1.16e-24 |
|
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: 99.34 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP-DAITAKVGYMPEE 80
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDvPVQERNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYfaalhGMK-KAEAIILLDDWMKR-----LNVVGksTDKIES-----LSKGNAQKVQLIACLMFKP 149
Cdd:cd03296 83 YALFRHMTVFDNVAF-----GLRvKPRSERPPEAEIRAkvhelLKLVQ--LDWLADrypaqLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951434962 150 QLLILDEPFSGLDP-VNSELliKAILTAKQQGTMV--IFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:cd03296 156 KVLLLDEPFGALDAkVRKEL--RRWLRRLHDELHVttVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-221 |
1.90e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 102.94 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSkrF---GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVG 75
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdlTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEERGLYpKETIKSQLLYF----------AALhgmKKAEAiillDDWMKRLN-----VVGkstdkiE---SLSKGnaQ 137
Cdd:COG1132 418 VVPQDTFLF-SGTIRENIRYGrpdatdeeveEAA---KAAQA----HEFIEALPdgydtVVG------ErgvNLSGG--Q 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 138 KvQLIA---CLMFKPQLLILDEPFSGLDPVnSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTP 214
Cdd:COG1132 482 R-QRIAiarALLKDPPILILDEATSALDTE-TEALIQEALERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTH 558
|
250
....*....|...
gi 951434962 215 TE------IYRQF 221
Cdd:COG1132 559 EEllarggLYARL 571
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-214 |
2.05e-24 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 99.03 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpltpdaitAKVGYMPEE 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--------LRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 rgLYPKETIKSQLLYFAALH-GMKKAEAIILLddwmKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:PRK09544 76 --LYLDTTLPLTVNRFLRLRpGTKKEDILPAL----KRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 160 GLDpVNSEL----LIKAILTakQQGTMVIFSTHNMDNVQKLSDYIVMLKHgQTVLKGTP 214
Cdd:PRK09544 150 GVD-VNGQValydLIDQLRR--ELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTP 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-247 |
3.72e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 101.80 E-value: 3.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMI--LDFIKPDSGKILWSGkpltpdAITAKVGYM-- 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHV------ALCEKCGYVer 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLY-PK--ETIKSQLLYFAAL-----HGMKKAEAIIL------------LDDWMKRLN--------VVGKSTDKIE 129
Cdd:TIGR03269 75 PSKVGEPcPVcgGTLEPEEVDFWNLsdklrRRIRKRIAIMLqrtfalygddtvLDNVLEALEeigyegkeAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 130 -------------SLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQK 195
Cdd:TIGR03269 155 mvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIED 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 951434962 196 LSDYIVMLKHGQTVLKGTPTEIYRQFGRLRLDIEGYQNVERLKRIQGVKKVT 247
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGEPIIKVRNVS 286
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-250 |
4.69e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAItaKVGYMPEERGL---YPK-----E 87
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKV--KLSDIRKKVGLvfqYPEyqlfeE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 88 TIKSQLLYFAALHGMKKAEaiiLLDDWMKRLNVVGKSTDKIE-----SLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEE---IENRVKRAMNIVGLDYEDYKdkspfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 163 PVNSELLIKAILTAKQQGTM-VIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRqfgrlrldiegyqNVERLKRIQ 241
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMtIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK-------------EVETLESIG 243
|
250
....*....|
gi 951434962 242 -GVKKVTLMA 250
Cdd:PRK13637 244 lAVPQVTYLV 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
6.45e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.46 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF----------------------GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKI 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 59 LWSGKPLTPDAITAkvGYMPEERGLypketiksQLLYF-AALHGMKKAEAIILLDDwmkrlnVV-----GKSTD-KIESL 131
Cdd:COG1134 84 EVNGRVSALLELGA--GFHPELTGR--------ENIYLnGRLLGLSRKEIDEKFDE------IVefaelGDFIDqPVKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 132 SKGnaQKVQL---IAcLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQT 208
Cdd:COG1134 148 SSG--MRARLafaVA-TAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
250 260
....*....|....*....|
gi 951434962 209 VLKGTPTEI---YRQFGRLR 225
Cdd:COG1134 225 VMDGDPEEViaaYEALLAGR 244
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-220 |
6.85e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 98.34 E-value: 6.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF-----GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIL------W----SGKPL 65
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdeWvdmtKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 66 TPDAITAKVGYMPEERGLYPKETIksqllyfaaLHGMKKAEAIILLDDWMKR-----LNVVGKSTDKIES--------LS 132
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTV---------LDNLTEAIGLELPDELARMkavitLKMVGFDEEKAEEildkypdeLS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 133 KGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQ--GTMVIFStHNMDNVQKLSDYIVMLKHGQTVL 210
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVS-HDMDFVLDVCDRAALMRDGKIVK 508
|
250
....*....|
gi 951434962 211 KGTPTEIYRQ 220
Cdd:TIGR03269 509 IGDPEEIVEE 518
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-230 |
6.89e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.06 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL----TPDAITAKVGYMP 78
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERGLYPKETIKSQLL--YFAALHGMKKAEAiiLLDDWMKRLNVVGKSTD---KIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK11288 86 QELHLVPEMTVAENLYlgQLPHKGGIVNRRL--LNYEAREQLEHLGVDIDpdtPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV-----LKGTPTE------------ 216
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVatfddMAQVDRDqlvqamvgreig 243
|
250
....*....|....*....
gi 951434962 217 -IY----RQFGRLRLDIEG 230
Cdd:PRK11288 244 dIYgyrpRPLGEVRLRLDG 262
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
8-218 |
7.79e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.07 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 8 SKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKI----LWSG-----KPLTPDAITAKVGYMP 78
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGdkknnHELITNPYSKKIKNFK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERGL------YP-----KETIKSQLLYFAALHGMKKAEAIILLDdwmKRLNVVGKSTDKIE----SLSKGNAQKVQLIA 143
Cdd:PRK13631 113 ELRRRvsmvfqFPeyqlfKDTIEKDIMFGPVALGVKKSEAKKLAK---FYLNKMGLDDSYLErspfGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 144 CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-227 |
1.07e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.38 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLtpDAITAKVGYMPEE 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV--EGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 161 LDPVNSELLIKAILTAKQ-QGTMVIFSTHNMDNVQKLSDYIVMLKHGqtvlkgtPTEIYRqfgRLRLD 227
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQeTGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVVE---RLPLN 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-207 |
1.65e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWsGKpltpdaiTAKVGYMPEE 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-------TVKIGYFDQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 R-GLYPKETIKSQLLYFAAlhGMKKAEAIILL-------DDWMKrlnvvgkstdKIESLSKGnaQKVQL-IACLMF-KPQ 150
Cdd:COG0488 387 QeELDPDKTVLDELRDGAP--GGTEQEVRGYLgrflfsgDDAFK----------PVGVLSGG--EKARLaLAKLLLsPPN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 151 LLILDEPFSGLDPVNSELLIKAILTAKqqGTmVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDFP--GT-VLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-228 |
2.29e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.03 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFN---AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA---ITAKV 74
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYM---PEERglYPKETIKSQLLYFAALHGMKKAEAIILLDDwmkRLNVVGKSTDKIES---LSKGNAQKVQLIACLMFK 148
Cdd:PRK13650 84 GMVfqnPDNQ--FVGATVEDDVAFGLENKGIPHEEMKERVNE---ALELVGMQDFKEREparLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 149 PQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFS-THNMDNVqKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR-- 225
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISiTHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLLql 237
|
....
gi 951434962 226 -LDI 228
Cdd:PRK13650 238 gLDI 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-207 |
2.43e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 96.61 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGYMPEER-------GLYP 85
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqDGLANGIVYISEDRkrdglvlGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 86 KETIK-SQLLYFAALHG-MKKAEAIILLDDWMKRLNVVGKSTDK-IESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:PRK10762 348 KENMSlTALRYFSRAGGsLKHADEQQAVSDFIRLFNIKTPSMEQaIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 951434962 163 PVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
3.35e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.87 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVGYM 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 P-----------EE---RGLYPketiksqllyfaalHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIA 143
Cdd:COG4559 81 PqhsslafpftvEEvvaLGRAP--------------HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 144 CL-------MFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTE 216
Cdd:COG4559 147 VLaqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-213 |
4.33e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.38 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHM--ILDFikPDSGKILWSG------KPLTPDAITA- 72
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVlnLLET--PDSGQLNIAGhqfdfsQKPSEKAIRLl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 --KVGYMPEERGLYPKETIKSQLLyfAA---LHGMKKAEAIILLDDWMKRLNVvgksTDKIES----LSKGNAQKVQLIA 143
Cdd:COG4161 81 rqKVGMVFQQYNLWPHLTVMENLI--EApckVLGLSKEQAREKAMKLLARLRL----TDKADRfplhLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 144 CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGT 213
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-212 |
5.25e-22 |
|
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: 91.07 E-value: 5.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTtfhmILDFI------KPDSGKILWSGKPLTPDAITAKVGYMPEERGLYPKETIK 90
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKST----LLNALagrrtgLGVSGEVLINGRPLDKRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 91 SQLLYFAALHGMKKAEaiillddwMKRLNvvgkstdkieslskgnaqkvqlIAC-LMFKPQLLILDEPFSGLDPVNSELL 169
Cdd:cd03213 101 ETLMFAAKLRGLSGGE--------RKRVS----------------------IALeLVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 951434962 170 IKAILTAKQQGTMVIFSTHN-MDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03213 151 MSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-220 |
7.07e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.02 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK-VGYMPEE 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 161 LDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-206 |
1.00e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGYM 77
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYpKETIKSQLLYFAALHGmKKAEAIILLDDWMkRLNVVGKSTDK-IESLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:PRK10247 87 AQTPTLF-GDTVYDNLIFPWQIRN-QQPDPAIFLDDLE-RFALPDTILTKnIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 157 PFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHG 206
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRyVREQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-207 |
1.14e-21 |
|
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: 90.96 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF-----GN--FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIL--WSGKPLtpDAIT 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrHDGGWV--DLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 72 AKVGYMPEERglypKETIK--SQLLYF----AAL---------HGMKKAEAIILLDDWMKRLNVVgkstdkiESL----- 131
Cdd:COG4778 82 ASPREILALR----RRTIGyvSQFLRViprvSALdvvaeplleRGVDREEARARARELLARLNLP-------ERLwdlpp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 132 ---SKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGT-MV-IFstHNMDNVQKLSDYIVMLKHG 206
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIgIF--HDEEVREAVADRVVDVTPF 228
|
.
gi 951434962 207 Q 207
Cdd:COG4778 229 S 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-206 |
1.15e-21 |
|
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: 90.54 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN-FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITA----KV 74
Cdd:cd03292 1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlRGRAIPylrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYMPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 951434962 155 DEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHG 206
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERG 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-274 |
1.27e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA-------ITAKVGYM---PEERgLYp 85
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdikqIRKKVGLVfqfPESQ-LF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 86 KETIKSQLLYFAALHGMKKAEAIILLDDwmkRLNVVGKSTDKIE----SLSKGNAQKVQLIACLMFKPQLLILDEPFSGL 161
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQEEAEALARE---KLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 162 DPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIyrqfgrlrldiegYQNVERLKRIQ 241
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI-------------FQDVDFLEEKQ 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 951434962 242 -GVKKVTLMANGV--------HLELNNEQcgkiiFTEVTKHG 274
Cdd:PRK13649 244 lGVPKITKFAQRLadrgisfsSLPITIEE-----FREVLKHG 280
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
7-216 |
1.32e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.87 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 7 VSKRFGNfNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKVGYMPEERGLYPK 86
Cdd:PRK15056 14 VTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ETIKSQLLYFAALHG------MKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:PRK15056 93 FPVLVEDVVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 161 LDpVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQKLSDYIVMLKhgQTVLKGTPTE 216
Cdd:PRK15056 173 VD-VKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVK--GTVLASGPTE 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-212 |
1.77e-21 |
|
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: 90.24 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSlhSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK-VGYMPEE 80
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpVSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQ--LLYFAALH-------GMKKAEAIILLDDWMKRLNvvgkstdkiESLSKGNAQKVQLIACLMFKPQL 151
Cdd:cd03298 79 NNLFAHLTVEQNvgLGLSPGLKltaedrqAIEVALARVGLAGLEKRLP---------GELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 152 LILDEPFSGLDPVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
2.03e-21 |
|
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: 93.89 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGYM 77
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdadADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKeTIKSQLLYF---AALHGMKKAEAIILLDDWMKRL-----NVVGKSTdkiESLSKGNAQKVQLIACLMFKP 149
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLArpdASDAEIREALERAGLDEFVAALpqgldTPIGEGG---AGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 951434962 150 QLLILDEPFSGLDPvNSELLIKAILTAKQQGTMVIFSTHNmDNVQKLSDYIVML 203
Cdd:TIGR02857 478 PLLLLDEPTAHLDA-ETEAEVLEALRALAQGRTVLLVTHR-LALAALADRIVVL 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-213 |
2.25e-21 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpDAITAK-----VG 75
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-DWQTAKimreaVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEERGLYPKETIKSQLL---YFAALHgmKKAEAIILLDDWMKRLNvvGKSTDKIESLSKGNAQKVQLIACLMFKPQLL 152
Cdd:PRK11614 84 IVPEGRRVFSRMTVEENLAmggFFAERD--QFQERIKWVYELFPRLH--ERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 153 ILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGT 213
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-218 |
2.53e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 92.70 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdaitakvGYMPEER 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--------HVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 ---------GLYPKETIKSQLLYfaALHgMKK------------AEAIILLDDWMKRlnvvgkstdKIESLSKGNAQKVQ 140
Cdd:PRK09452 87 hvntvfqsyALFPHMTVFENVAF--GLR-MQKtpaaeitprvmeALRMVQLEEFAQR---------KPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 141 LIACLMFKPQLLILDEPFSGLD-----PVNSELliKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPT 215
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDyklrkQMQNEL--KAL--QRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
...
gi 951434962 216 EIY 218
Cdd:PRK09452 231 EIY 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-212 |
3.27e-21 |
|
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: 89.51 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF----------------------GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIL 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 60 WSGKPLTPDAITAkvGYMPEERGLypkETIksqllYF-AALHGMKKAEAIILLDDwMKRLNVVGKSTDK-IESLSKGnaQ 137
Cdd:cd03220 81 VRGRVSSLLGLGG--GFNPELTGR---ENI-----YLnGRLLGLSRKEIDEKIDE-IIEFSELGDFIDLpVKTYSSG--M 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 138 KVQL---IAcLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03220 148 KARLafaIA-TALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-225 |
4.24e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA-------ITAKVGYM---PEERGLyp 85
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeikpVRKKVGVVfqfPESQLF-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 86 KETIKSQLLYFAALHGMKKAEAIILLddwMKRLNVVGKSTDKIE----SLSKGNAQKVQLIACLMFKPQLLILDEPFSGL 161
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIA---AEKLEMVGLADEFWEkspfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951434962 162 DPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLK 239
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-217 |
4.63e-21 |
|
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: 89.76 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSG---KILwsGKPL---TPDAITAKV 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRggeDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 G---------YMPEER-------------GLYPKETiksqllyfaalhgmkkAEAIILLDDWMKRLNVVGKSTDKIESLS 132
Cdd:COG1119 81 GlvspalqlrFPRDETvldvvlsgffdsiGLYREPT----------------DEQRERARELLELLGLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 133 KGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLK 211
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
....*.
gi 951434962 212 GTPTEI 217
Cdd:COG1119 225 GPKEEV 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
4.81e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.46 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFgNFN------AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD------- 68
Cdd:PRK13634 3 ITFQKVEHRY-QYKtpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 69 AITAKVGYM---PEERgLYpKETIKSQLLYFAALHGMKKAEAIILLDDWMKrlnVVGKSTDKIE----SLSKGNAQKVQL 141
Cdd:PRK13634 82 PLRKKVGIVfqfPEHQ-LF-EETVEKDICFGPMNFGVSEEDAKQKAREMIE---LVGLPEELLArspfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 142 IACLMFKPQLLILDEPFSGLDPVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYR 219
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-217 |
5.16e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 89.76 E-value: 5.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL--TPDAITAK-VGYM 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVatTPSRELAKrLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKsQLLYFaalhG--------MKKA-EAIIllDDWMKRLNVVGKSTDKIESLSKGNAQKVqLIAclMFK 148
Cdd:COG4604 81 RQENHINSRLTVR-ELVAF----GrfpyskgrLTAEdREII--DEAIAYLDLEDLADRYLDELSGGQRQRA-FIA--MVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 149 PQ---LLILDEPFSGLDPVNSELLIKAI--LTAKQQGTMVI------FSTHnmdnvqkLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG4604 151 AQdtdYVLLDEPLNNLDMKHSVQMMKLLrrLADELGKTVVIvlhdinFASC-------YADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-207 |
7.22e-21 |
|
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: 87.27 E-value: 7.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNA--VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGY 76
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEErglypketiksqllyfaalhgmkkaeaIILLDdwmkrlnvvGKSTDKIesLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:cd03246 81 LPQD---------------------------DELFS---------GSIAENI--LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 157 PFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMdNVQKLSDYIVMLKHGQ 207
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-218 |
8.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.77 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 13 NFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAI---TAKVGYM---PEERglYPK 86
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlRRKIGMVfqnPDNQ--FVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNS 166
Cdd:PRK13642 97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 951434962 167 ELLIKAILTAKQQGTMVIFS-THNMDNVQKlSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK13642 177 QEIMRVIHEIKEKYQLTVLSiTHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-223 |
1.11e-20 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 88.37 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSG---KPLTPDAITAKVGYMPEERGLYPKeTIKSQLLY 95
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdiRDLNLRWLRSQIGLVSQEPVLFDG-TIAENIRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 96 FA-------ALHGMKKAEAIILLDDWMKRLN-VVGkstDKIESLSKGnaQKvQLIA---CLMFKPQLLILDEPFSGLDpV 164
Cdd:cd03249 100 GKpdatdeeVEEAAKKANIHDFIMSLPDGYDtLVG---ERGSQLSGG--QK-QRIAiarALLRNPKILLLDEATSALD-A 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 165 NSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFGR 223
Cdd:cd03249 173 ESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
18-188 |
1.33e-20 |
|
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: 87.55 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 18 SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL--TPDAITAKVGYMPEERGLYPKETIKSQLLY 95
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfQRDSIARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 96 FAALHGMKKAEaiilldDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILT 175
Cdd:cd03231 97 WHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
170
....*....|...
gi 951434962 176 AKQQGTMVIFSTH 188
Cdd:cd03231 171 HCARGGMVVLTTH 183
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-218 |
1.40e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.66 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK-VGYMPE 79
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRpINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 160 GLD-PVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK11607 179 ALDkKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
1.71e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNF--NAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAIT---AKVG 75
Cdd:PRK13632 7 MIKVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeirKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YM---PE----------------ERGLYPKETIKSQLLYFAALHGMKKaeaiiLLDDwmkrlnvvgkstdKIESLSKGNA 136
Cdd:PRK13632 87 IIfqnPDnqfigatveddiafglENKKVPPKKMKDIIDDLAKKVGMED-----YLDK-------------EPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 137 QKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFS-THNMDNVQkLSDYIVMLKHGQTVLKGTPT 215
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPK 227
|
..
gi 951434962 216 EI 217
Cdd:PRK13632 228 EI 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-207 |
2.97e-20 |
|
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: 90.65 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILD-FIKPDSGKILWSGKPL---TP-DAITAKVGYMPEER---GLYP--- 85
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVdirNPaQAIRAGIAMVPEDRkrhGIVPilg 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 86 --KETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTD-KIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:TIGR02633 356 vgKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 951434962 163 PVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-209 |
4.69e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTfhM-ILDFIKPD---SGKILWSGKPLTPDAITAKvgy 76
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTL--MkVLSGVYPHgtyEGEIIFEGEELQASNIRDT--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 mpEERGLypkeTIKSQLLyfAALHGMKKAEAIIL---------LDD---------WMKRLNVVGKSTDKIESLSKGNAQK 138
Cdd:PRK13549 80 --ERAGI----AIIHQEL--ALVKELSVLENIFLgneitpggiMDYdamylraqkLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 139 VQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-217 |
8.36e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 86.30 E-value: 8.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSG-KPLTPDA----ITAKVG 75
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVderlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEERGLYPKETIKSQLLyFAALH--GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVM-FGPLRvrGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTAKQQG-TMVIFsTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGmTMVIV-THEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-212 |
9.00e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.22 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILD-FIKPDSGKILWSGKPLT----PDAITAKVGYMPEER---GLYPKET 88
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKirnpQQAIAQGIAMVPEDRkrdGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 89 IK-----SQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTD-KIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:PRK13549 358 VGknitlAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPElAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 163 pVNSELLI-KAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQtvLKG 212
Cdd:PRK13549 438 -VGAKYEIyKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK--LKG 485
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-225 |
1.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 14 FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA-------ITAKVGYM---PEERgL 83
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkdkyirpVRKRIGMVfqfPESQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 84 YpKETIKSQLLYFAALHGMK----KAEAIILLDDWMKRLNVVGKSTDKiesLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:PRK13646 99 F-EDTVEREIIFGPKNFKMNldevKNYAHRLLMDLGFSRDVMSQSPFQ---MSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 160 GLDPvNSELLIKAILTAKQ--QGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:PRK13646 175 GLDP-QSKRQVMRLLKSLQtdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLA 241
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
16-217 |
1.47e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP-------DAITAKVGYMPEERGLYPKET 88
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelrEVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 89 IKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDP-VNSE 167
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPlIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 951434962 168 L---LIKaiLTAKQQGTmVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK10070 203 MqdeLVK--LQAKHQRT-IVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-209 |
1.81e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 88.34 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHmILDFIKPD---SGKILWSGKPLTPDAIT----AK 73
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLKASNIRdterAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 74 VGYMPEERGLYPKETIKSQLL--YFAALHG--MKKAEAIILLDDWMKRLNV-VGKSTDKIESLSKGNAQKVQLIACLMFK 148
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFlgNEITLPGgrMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 149 PQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-225 |
2.11e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAV---SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP---DAITAKVG 75
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVpvlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEERGLYP---KETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNvvGKSTDKIES---LSKGNAQKVQLIACLMFKP 149
Cdd:TIGR00958 559 LVGQEPVLFSgsvRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPN--GYDTEVGEKgsqLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 150 QLLILDEPFSGLDpVNSELLIKAilTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:TIGR00958 637 RVLILDEATSALD-AECEQLLQE--SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-225 |
2.48e-19 |
|
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: 84.97 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSkrFG---NFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVG 75
Cdd:cd03253 1 IEFENVT--FAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIrevTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YMPEERGLYpKETIKSQLLY---FAALHGMKKAEAIILLDDWMKRLN-----VVGKSTDKiesLSKGNAQKVQLIACLMF 147
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYgrpDATDEEVIEAAKAAQIHDKIMRFPdgydtIVGERGLK---LSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 148 KPQLLILDEPFSGLDpVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:cd03253 155 NPPILLLDEATSALD-THTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-218 |
3.61e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.24 E-value: 3.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN--AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDS---GKILWSGKPLTPDA---ITAK 73
Cdd:PRK13640 6 VEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTvwdIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 74 VGYM---PEERglYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQ 150
Cdd:PRK13640 86 VGIVfqnPDNQ--FVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 151 LLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFS-THNMDNVQkLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSPVEIF 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-218 |
4.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 84.65 E-value: 4.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFN-AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSG----KPLTPDAITAKVG 75
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YM---PEERglYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLL 152
Cdd:PRK13644 81 IVfqnPETQ--FVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 153 ILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQkLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-220 |
4.94e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.91 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP-DAITAKVGYMPEE 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLY-FAALHGMKKAEAIILLDDWMKRLNVV--GKSTDKIES-LSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:PRK10851 83 YALFRHMTVFDNIAFgLTVLPRRERPNAAAIKAKVTQLLEMVqlAHLADRYPAqLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 157 PFSGLDP-VNSEL---LIKaiLTAKQQGTMViFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:PRK10851 163 PFGALDAqVRKELrrwLRQ--LHEELKFTSV-FVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-217 |
5.38e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 5.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF----GNF-----NAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT----- 66
Cdd:PRK15112 4 LLEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdys 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 67 ----------PDAITAkvgympeergLYPKETIkSQLLYF-----AALHGMKKAEAIIllddwmKRLNVVGKSTDKI--- 128
Cdd:PRK15112 84 yrsqrirmifQDPSTS----------LNPRQRI-SQILDFplrlnTDLEPEQREKQII------ETLRQVGLLPDHAsyy 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 129 -ESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQ-QGTMVIFSTHNMDNVQKLSDYIVMLKHG 206
Cdd:PRK15112 147 pHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
250
....*....|.
gi 951434962 207 QTVLKGTPTEI 217
Cdd:PRK15112 227 EVVERGSTADV 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-213 |
7.05e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 83.53 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHmILDFIK-PDSGKILWSG------KPLTPDAITA-- 72
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSGTLNIAGnhfdfsKTPSDKAIRElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 -KVGYMPEERGLYPKETIKSQLLyfAA---LHGMKKAEAIILLDDWMKRLNVvgksTDKIES----LSKGNAQKVQLIAC 144
Cdd:PRK11124 82 rNVGMVFQQYNLWPHLTVQQNLI--EApcrVLGLSKDQALARAEKLLERLRL----KPYADRfplhLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 145 LMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQG-TMVIFsTHNMDNVQKLSDYIVMLKHGQTVLKGT 213
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIV-THEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-218 |
8.65e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 8.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKP-DS-----GKILWSGKPL-TPDAITAK--VGYMPEERGLYPKE 87
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIfQIDAIKLRkeVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 88 TIKSQLLYFAALHGMK-KAEAIILLDDWMKRLNVVGKSTDKIES----LSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 163 PVNSELLIKAILTAKQQGTMVIFStHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-212 |
1.12e-18 |
|
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: 82.64 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN--FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSG---KPLTPDAITAKVGY 76
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdiRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYpKETIKSQLLYFAALHG----MKKAEaIILLDDWMKR----LNV-VGkstDKIESLSKGNAQKVQLIACLMF 147
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGAPLADderiLRAAE-LAGVTDFVNKhpngLDLqIG---ERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 148 KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIfSTHNMdNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLII-ITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
1.14e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.65 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNA--VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD---AITAKVG 75
Cdd:PRK13648 7 IIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnfeKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 YM---PEERglYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLL 152
Cdd:PRK13648 87 IVfqnPDNQ--FVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 153 ILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFS-THNMDNVQKlSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-197 |
1.52e-18 |
|
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: 81.64 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL--TPDAITAKVGYMPEERGLYPKETIKSQL 93
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeQRDEPHENILYLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 94 LYFAALHGmkkaEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAI 173
Cdd:TIGR01189 95 HFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170 180
....*....|....*....|....*..
gi 951434962 174 LTAKQQGTMVIFSTH---NMDNVQKLS 197
Cdd:TIGR01189 171 RAHLARGGIVLLTTHqdlGLVEARELR 197
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-225 |
1.65e-18 |
|
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: 82.66 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN--FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSG---KPLTPDAITAKVGY 76
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYpKETIKSQLLYfaALHGMKKAEAI-----ILLDDWMKRL-----NVVGkstDKIESLSKGNAQKVQlIACLM 146
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAY--GRPGATREEVEeaaraANAHEFIMELpegydTVIG---ERGVKLSGGQRQRIA-IARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 147 FK-PQLLILDEPFSGLDpVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:cd03251 154 LKdPPILILDEATSALD-TESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
1.87e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 82.88 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKI------LWSGKPLTPD-----A 69
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditIDTARSLSQQkglirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 70 ITAKVGYMPEERGLYPKETIKSQLLYFAAL-HGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFK 148
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 149 PQLLILDEPFSGLDPvnsELLIKAILT----AKQQGTMVIFsTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY------ 218
Cdd:PRK11264 163 PEVILFDEPTSALDP---ELVGEVLNTirqlAQEKRTMVIV-THEMSFARDVADRAIFMDQGRIVEQGPAKALFadpqqp 238
|
....*
gi 951434962 219 --RQF 221
Cdd:PRK11264 239 rtRQF 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-207 |
3.84e-18 |
|
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: 81.36 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 15 NAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP---DAITAKVGYMPEERGLYPKeTIKS 91
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehKYLHSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 92 QLLY---FAALHGMKKAEAIILLDDWMKRLNvVGKSTDKIES---LSKGNAQKVQLIACLMFKPQLLILDEPFSGLDpVN 165
Cdd:cd03248 107 NIAYglqSCSFECVKEAAQKAHAHSFISELA-SGYDTEVGEKgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD-AE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 951434962 166 SELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQ 207
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-217 |
3.93e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKP---LTP-DAITAKVGY 76
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHkLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLlyFAALHGMKKAEAIILLdDW--MKR-----LNVVGKSTD---KIESLSKGNAQKVQLIACLM 146
Cdd:PRK09700 85 IYQELSVIDELTVLENL--YIGRHLTKKVCGVNII-DWreMRVraammLLRVGLKVDldeKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 147 FKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-209 |
4.55e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.04 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAV---------SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP---- 67
Cdd:PRK10419 3 LLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 68 --------------DAITAkvgympeergLYPKETIKSQLLY-FAALHGMKKAEAIILLDDWMKRLNVVGKSTDKI-ESL 131
Cdd:PRK10419 83 qrkafrrdiqmvfqDSISA----------VNPRKTVREIIREpLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 132 SKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVnSELLIKAILTAKQQ--GTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLV-LQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-207 |
5.18e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.90 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---P-DAITAKVGY 76
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPkSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLY-------FAALHGMK-KAEAIILLddwmKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFK 148
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLgrefvnrFGRIDWKKmYAEADKLL----ARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 149 PQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-207 |
5.78e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.64 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGkpltpdaiTAKVGYMPEer 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------TVKIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 glypketiksqllyfaalhgmkkaeaiillddwmkrlnvvgkstdkiesLSKGnaQKVQL-IACLMF-KPQLLILDEPFS 159
Cdd:cd03221 71 -------------------------------------------------LSGG--EKMRLaLAKLLLeNPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 951434962 160 GLDPVNSELLIKAILtaKQQGTmVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:cd03221 100 HLDLESIEALEEALK--EYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-209 |
6.25e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPD-----SGKILWSGKPLtpdaITAKVGYMPEERG--------- 82
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESL----LHASEQTLRGVRGnkiamifqe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 ----LYPKETIKSQLLYFAALH-GMKK----AEAIILLD-----DWMKRLNvvgkstDKIESLSKGNAQKVQLIACLMFK 148
Cdd:PRK15134 101 pmvsLNPLHTLEKQLYEVLSLHrGMRReaarGEILNCLDrvgirQAAKRLT------DYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951434962 149 PQLLILDEPFSGLDpVNSELLIKAILTAKQQ--GTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:PRK15134 175 PELLIADEPTTALD-VSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-163 |
6.67e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.22 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPD---SGKILWSGKPLTPDAITAK-VGY 76
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRrIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLyFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:COG4136 81 LFQDDLLFPHLSVGENLA-FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
....*..
gi 951434962 157 PFSGLDP 163
Cdd:COG4136 160 PFSKLDA 166
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-222 |
6.84e-18 |
|
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: 84.29 E-value: 6.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA--ITAKVGYMPEERGLYPKETIKSQL 93
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNIsdVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 94 LYFAALHGMKkAEAIILLDDW-MKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKA 172
Cdd:TIGR01257 2034 YLYARLRGVP-AEEIEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 951434962 173 ILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFG 222
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2-232 |
9.96e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 9.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRfgnfNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIkPDSGKILWSGKPLTpdaitakvgympeer 81
Cdd:PRK03695 1 MQLNDVAVS----TRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLE--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 gLYPKETIKSQLLYFA---------------ALH---GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIA 143
Cdd:PRK03695 61 -AWSAAELARHRAYLSqqqtppfampvfqylTLHqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 144 -CLMFKP------QLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTE 216
Cdd:PRK03695 140 vVLQVWPdinpagQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
250 260
....*....|....*....|....*
gi 951434962 217 IYRQ------FG---RlRLDIEGYQ 232
Cdd:PRK03695 220 VLTPenlaqvFGvnfR-RLDVEGHP 243
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-225 |
1.14e-17 |
|
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: 80.22 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAV--SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGY 76
Cdd:cd03252 1 ITFEHVRFRYKPDGPVilDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLD--DWMKRL-----NVVGkstDKIESLSKGNAQKVQLIACLMFKP 149
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGahDFISELpegydTIVG---EQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 150 QLLILDEPFSGLDpVNSELLIKAILTAKQQGTMVIFSTHNMDNVqKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLR 225
Cdd:cd03252 158 RILIFDEATSALD-YESEHAIMRNMHDICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-219 |
1.14e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 20 LSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVGYMPEE----RGLYPKETIK-- 90
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswSSKAFARKVAYLPQQlpaaEGMTVRELVAig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 91 -----SQLLYFAALHGMKKAEAIIL--LDDWMKRLnvvgkstdkIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD- 162
Cdd:PRK10575 110 rypwhGALGRFGAADREKVEEAISLvgLKPLAHRL---------VDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDi 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 163 --PVNSELLIKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYR 219
Cdd:PRK10575 181 ahQVDVLALVHRL--SQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-241 |
1.14e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.21 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 14 FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILwSGKPLTPDAITA--KVGYMPEERGL---YP--- 85
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI-VGDYAIPANLKKikEVKRLRKEIGLvfqFPeyq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 86 --KETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIE-SLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:PRK13645 103 lfQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 163 PVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIyrqfgrlrldiegYQNVERLKRIQ 241
Cdd:PRK13645 183 PKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI-------------FSNQELLTKIE 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-207 |
1.33e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.77 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVS-KRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGYM 77
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsprERRRLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEER---GLYPKETI---------------KSQLLYFAALHgmKKAEAIIllddwmKRLNVVGKSTD-KIESLSKGNAQK 138
Cdd:COG3845 339 PEDRlgrGLVPDMSVaenlilgryrrppfsRGGFLDRKAIR--AFAEELI------EEFDVRTPGPDtPARSLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 139 VqLIA-CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:COG3845 411 V-ILArELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-222 |
1.71e-17 |
|
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: 79.58 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKP---LTPDAITAKVGYMPEERGLYPKeTIKSQ 92
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDirdISRKSLRSMIGVVLQDTFLFSG-TIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 93 LLYF---AALHGMKKAEAIILLDDWMKRL-----NVVGkstDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPV 164
Cdd:cd03254 97 IRLGrpnATDEEVIEAAKEAGAHDFIMKLpngydTVLG---ENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 165 nSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFG 222
Cdd:cd03254 174 -TEKLIQEALEKLMKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
2.43e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGN-----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKVGY 76
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYP----------------------------KETIKSQLLYFAALHGMKKAEAIILLDDWMKrlnVVGKSTDKI 128
Cdd:PRK13651 83 VLEKLVIQKtrfkkikkikeirrrvgvvfqfaeyqlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIE---LVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 129 E----SLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLK 204
Cdd:PRK13651 160 QrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|...
gi 951434962 205 HGQTVLKGTPTEI 217
Cdd:PRK13651 240 DGKIIKDGDTYDI 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-260 |
3.15e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.75 E-value: 3.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFN------AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKI------------LWSG 62
Cdd:PRK13633 4 MIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 63 KPLT------PD-AITAK-----VGYMPEERGLYPKEtIKSQLlyfaalhgmkkaeaiillDDWMKRLNVVGKSTDKIES 130
Cdd:PRK13633 84 RNKAgmvfqnPDnQIVATiveedVAFGPENLGIPPEE-IRERV------------------DESLKKVGMYEYRRHAPHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 131 LSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTV 209
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 951434962 210 LKGTPTEIYRQfgrlrldiegyqnVERLKRIQ-GVKKVTLMAngvhLELNNE 260
Cdd:PRK13633 224 MEGTPKEIFKE-------------VEMMKKIGlDVPQVTELA----YELKKE 258
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-188 |
3.97e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.92 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 18 SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYMPEERGLYPKETIKSQLLY 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 96 FAALHGMKKAEAIIlldDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILT 175
Cdd:PRK13538 98 YQRLHGPGDDEALW---EALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ 174
|
170
....*....|...
gi 951434962 176 AKQQGTMVIFSTH 188
Cdd:PRK13538 175 HAEQGGMVILTTH 187
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-199 |
4.11e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.06 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKST---TFHMILDFIKP--DSGKILWSGKPL-----TPDAIT 71
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPGfrVEGKVTFHGKNLyapdvDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 72 AKVGYMPEERGLYPKeTIKSQLLYFAALHGMKkAEAIILLDDWMKRLNVVGKSTDKIE----SLSKGNAQKVQLIACLMF 147
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGARINGYK-GDMDELVERSLRQAALWDEVKDKLKqsglSLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 951434962 148 KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFsTHNMDNVQKLSDY 199
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV-THNMQQAARVSDM 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-157 |
1.21e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 4 LQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpltpdaitAKVGYMPEERGL 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG--------LRIGYLPQEPPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 84 YPKETIKSQLL------------YFAALHGMKKAEA-----------IILLDDW---------MKRLNVVGKSTD-KIES 130
Cdd:COG0488 73 DDDLTVLDTVLdgdaelraleaeLEELEAKLAEPDEdlerlaelqeeFEALGGWeaearaeeiLSGLGFPEEDLDrPVSE 152
|
170 180
....*....|....*....|....*..
gi 951434962 131 LSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-222 |
1.76e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGYM 77
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarhrRAVCPRIAYM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERG--LYPKETIKSQLLYFAALHGMKKAE-----AIIL----LDDWMKRLnvVGKstdkiesLSKGNAQKVQLIACLM 146
Cdd:NF033858 82 PQGLGknLYPTLSVFENLDFFGRLFGQDAAErrrriDELLratgLAPFADRP--AGK-------LSGGMKQKLGLCCALI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 147 FKPQLLILDEPFSGLDPvnseL-------LIKAIlTAKQQGTMVIFSTHNMDNVQKLsDYIVMLKHGQTVLKGTPTEIYR 219
Cdd:NF033858 153 HDPDLLILDEPTTGVDP----LsrrqfweLIDRI-RAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
...
gi 951434962 220 QFG 222
Cdd:NF033858 227 RTG 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-212 |
2.15e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 76.54 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMI---LDFIKPDSGKILWSGKPLTPDAITAKVGYMPEERGLYPKETIKsQL 93
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVR-ET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 94 LYFAALHGM--KKAEAIILLDDWMKRLNVVGKST---DKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSEL 168
Cdd:cd03234 102 LTYTAILRLprKSSDAIRKKRVEDVLLRDLALTRiggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 951434962 169 LIKAILTAKQQGTMVIFSTHN-MDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:cd03234 182 LVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
18-196 |
2.33e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 18 SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKVGYMPEERGLYPKETIKSQLLYFA 97
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 98 ALHGmkkaEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAK 177
Cdd:PRK13539 99 AFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170 180
....*....|....*....|..
gi 951434962 178 QQGTMVIFSTHN---MDNVQKL 196
Cdd:PRK13539 175 AQGGIVIAATHIplgLPGAREL 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-217 |
4.84e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 77.04 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF----GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMI--LDfiKPDSGKILWSGKPLTpdAITAKv 74
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInlLE--RPTSGSVLVDGVDLT--ALSER- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 gympEERGL------------------------YPKEtiksqllyfaaLHGMKKAEAIillddwmKR----LNVVGKStD 126
Cdd:COG1135 76 ----ELRAArrkigmifqhfnllssrtvaenvaLPLE-----------IAGVPKAEIR-------KRvaelLELVGLS-D 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 127 KIES----LSKGNAQKVQlIA-CLMFKPQLLILDEPFSGLDPVNSelliKAILT-----AKQQGTMVIFSTHNMDNVQKL 196
Cdd:COG1135 133 KADAypsqLSGGQKQRVG-IArALANNPKVLLCDEATSALDPETT----RSILDllkdiNRELGLTIVLITHEMDVVRRI 207
|
250 260
....*....|....*....|.
gi 951434962 197 SDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG1135 208 CDRVAVLENGRIVEQGPVLDV 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-222 |
8.51e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 20 LSFSLHSGQILSLIGQNGAGKSTTFHMILDFIkPDSGKILWSGKPLTPDAIT------AKVGYMPeergLYPKETIKSQL 93
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPEswrkhlSWVGQNP----QLPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 94 LYFAA-------LHGMKKAEAIILLDDWMKRLN-VVGkstDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDpVN 165
Cdd:PRK11174 444 LLGNPdasdeqlQQALENAWVSEFLPLLPQGLDtPIG---DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD-AH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 166 SELLIKAILTAKQQGTMVIFSTHNMDNVQKLsDYIVMLKHGQTVLKGTPTEIYRQFG 222
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-217 |
9.43e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.26 E-value: 9.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 6 HVSKRFGNFnavsdlSFSLHSGQILSLIGQNGAGKSTTFHMILDFIkPDSGKILWSGKPL---TPDAITAKVGYMPEErg 82
Cdd:COG4138 7 AVAGRLGPI------SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLsdwSAAELARHRAYLSQQ-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 lypketiksQLLYFA-------ALH---GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIA-CLMFKP-- 149
Cdd:COG4138 78 ---------QSPPFAmpvfqylALHqpaGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAvLLQVWPti 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 150 ----QLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG4138 149 npegQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEV 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-242 |
1.63e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 12 GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPD---SGKILWSGKPLT--PDAITAKVgyMPEE------ 80
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnlPEKELNKL--RAEQismifq 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 ---RGLYPKETIKSQLLYFAALH-GMKKAEA----IILLD-----DWMKRLNVVGkstdkiESLSKGNAQKVQLIACLMF 147
Cdd:PRK09473 105 dpmTSLNPYMRVGEQLMEVLMLHkGMSKAEAfeesVRMLDavkmpEARKRMKMYP------HEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 148 KPQLLILDEPFSGLDpVNSELLIKAILT--AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQ----- 220
Cdd:PRK09473 179 RPKLLIADEPTTALD-VTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQpshpy 257
|
250 260
....*....|....*....|....*..
gi 951434962 221 -FGRL----RLDIEGyqnvERLKRIQG 242
Cdd:PRK09473 258 sIGLLnavpRLDAEG----ESLLTIPG 280
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-226 |
2.15e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 9 KRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT----PDAiTAKVGYMPEERGLY 84
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdKDG-QLKVADKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 85 PKETIKSQLL----YFAALH----------GMKKAEAIILLDDWMKRLNVVGKSTDKIES-LSKGNAQKVQLIACLMFKP 149
Cdd:PRK10619 92 TRLTMVFQHFnlwsHMTVLEnvmeapiqvlGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 150 QLLILDEPFSGLDP--VNSELLIKAILtAKQQGTMVIFsTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLRL 226
Cdd:PRK10619 172 EVLLFDEPTSALDPelVGEVLRIMQQL-AEEGKTMVVV-THEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-199 |
2.76e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.06 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPD--AITAKVGYMPEERGLYPKETIKSQLL 94
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDlcTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 95 YfaALHGMKKAEAIilldDWMKRLNVVGKSTD-KIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAI 173
Cdd:PRK13540 97 Y--DIHFSPGAVGI----TELCRLFSLEHLIDyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKI 170
|
170 180
....*....|....*....|....*.
gi 951434962 174 LTAKQQGTMVIFSTHNMDNVQKlSDY 199
Cdd:PRK13540 171 QEHRAKGGAVLLTSHQDLPLNK-ADY 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-189 |
2.94e-15 |
|
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: 75.86 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGYM 77
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSsldQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYpKETIKSQLLyFAALHG----MKKAEAIILLDDWMKRLNvVGKSTDKIE---SLSKGNAQKVQLIACLMFKPQ 150
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLR-LARPDAtdeeLWAALERVGLADWLRALP-DGLDTVLGEggaRLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*....
gi 951434962 151 LLILDEPFSGLDPVNSELLIKAILTAkQQGTMVIFSTHN 189
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
18-207 |
4.99e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 18 SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKVG----YMPEER---GLYpketIK 90
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLArglvYLPEDRqssGLY----LD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 91 SQLLY--FAALHGMK------KAEAIILlDDWMKRLNVvgKSTDK---IESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:PRK15439 356 APLAWnvCALTHNRRgfwikpARENAVL-ERYRRALNI--KFNHAeqaARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 160 GLD-PVNSEL--LIKAIltaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK15439 433 GVDvSARNDIyqLIRSI---AAQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
6.12e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.23 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN-AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA---ITAKVGYM 77
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENekwVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEErglyPKETIKSQLLY----FAALH-GMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLL 152
Cdd:PRK13647 85 FQD----PDDQVFSSTVWddvaFGPVNmGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 153 ILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTP 214
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-212 |
6.38e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.92 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 27 GQILSLIGQNGAGKSTTFHMILDFIKPDS--GKILWSGKPLTpDAITAKVGYMPEERGLYPKETIKSQLLYFAAL---HG 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT-KQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 102 MKKAEAIILLDDWMKRL-------NVVGKSTdkIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAIL 174
Cdd:PLN03211 173 LTKQEKILVAESVISELgltkcenTIIGNSF--IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLG 250
|
170 180 190
....*....|....*....|....*....|....*....
gi 951434962 175 TAKQQGTMVIFSTHNMDN-VQKLSDYIVMLKHGQTVLKG 212
Cdd:PLN03211 251 SLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-225 |
8.22e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 74.36 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIkPDSGKILWSGKPL--------TPDAITAKVGYMPEERGLYPK- 86
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLhnlnrrqlLPVRHRIQVVFQDPNSSLNPRl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ---ETIKSQL-LYFAALHGMKKAEAIILLddwMKRLNVVGKSTDKIES-LSKGNAQKVQLIACLMFKPQLLILDEPFSGL 161
Cdd:PRK15134 380 nvlQIIEEGLrVHQPTLSAAQREQQVIAV---MEEVGLDPETRHRYPAeFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 162 D-PVNSELLikAILTAKQQGTMV--IFSTHNMDNVQKLSDYIVMLKHGQTVLKG-------TPTEIY-RQFGRLR 225
Cdd:PRK15134 457 DkTVQAQIL--ALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGdcervfaAPQQEYtRQLLALS 529
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-216 |
1.08e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 7 VSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL----TPDAITAKVGYMPEERG 82
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 LYPKETIKSQL-LYFAALHGM--------KKAEAIillddwMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK10982 84 LVLQRSVMDNMwLGRYPTKGMfvdqdkmyRDTKAI------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTV----LKGTPTE 216
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIatqpLAGLTMD 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-217 |
1.34e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.34 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKP---LTPDAITAKVGYM 77
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDveaLSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGL---YPKETI-----KSQLLYFAAlHGMKKAEAIillDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKP 149
Cdd:PRK09536 83 PQDTSLsfeFDVRQVvemgrTPHRSRFDT-WTETDRAAV---ERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 150 QLLILDEPFSGLDpVNSEL-LIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK09536 159 PVLLLDEPTASLD-INHQVrTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-199 |
1.47e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.99 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKST---TFHMILDFIkPD---SGKILWSGKP-LTPD----AI 70
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLI-PGarvEGEILLDGEDiYDPDvdvvEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 71 TAKVGYMPEERGLYPKeTIKSQLLYFAALHGMK-KAEaiilLDD-----------W--MK-RLNvvgKS-TdkieSLSKG 134
Cdd:COG1117 91 RRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKsKSE----LDEiveeslrkaalWdeVKdRLK---KSaL----GLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 135 NAQKvqL-IA-CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFsTHNMDNVQKLSDY 199
Cdd:COG1117 159 QQQR--LcIArALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIV-THNMQQAARVSDY 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-239 |
2.05e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDS---------GKILWSGKPLTPD--A 69
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDirK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 70 ITAKVGYMPEERGLYPKETIKSQLL---------------YFAALHGMKKAEAiillddwMKRLNVVGKSTDKIESLSKG 134
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLigalgstpfwrtcfsWFTREQKQRALQA-------LTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 135 NAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGT 213
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
250 260
....*....|....*....|....*.
gi 951434962 214 PteiyRQFGRLRLDiEGYQNVERLKR 239
Cdd:PRK09984 237 S----QQFDNERFD-HLYRSINRVEE 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-220 |
2.13e-14 |
|
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: 73.18 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMIL----DFIKPDSGKILWSGKPLT--PDAI 70
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILrllpDPAAHPSGSILFDGQDLLglSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 71 TAKVgympeeRG-------------LYPKETIKSQLLYFAALH-GMKKAEA---IIlldDWMKRlnvVG--KSTDKIES- 130
Cdd:COG4172 86 LRRI------RGnriamifqepmtsLNPLHTIGKQIAEVLRLHrGLSGAAArarAL---ELLER---VGipDPERRLDAy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 131 ---LSKGNAQKVQL---IAClmfKPQLLILDEPFSGLDpvnseLLIKA-ILT-----AKQQGTMVIFSTHNMDNVQKLSD 198
Cdd:COG4172 154 phqLSGGQRQRVMIamaLAN---EPDLLIADEPTTALD-----VTVQAqILDllkdlQRELGMALLLITHDLGVVRRFAD 225
|
250 260
....*....|....*....|..
gi 951434962 199 YIVMLKHGQTVLKGTPTEIYRQ 220
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-231 |
2.52e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 70.25 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDF--IKPDSGKILWSGKPLTpdAITakvgymPE 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT--DLP------PE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ER---GLYpketIKSQllYFAALHGMKkaeaiilLDDWMKRLNvvgkstdkiESLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:cd03217 73 ERarlGIF----LAFQ--YPPEIPGVK-------NADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 157 PFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNmdnvQKLSDYIV-----MLKHGQTVLKGtPTEIYRQFGRlrldiEGY 231
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHY----QRLLDYIKpdrvhVLYDGRIVKSG-DKELALEIEK-----KGY 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-162 |
2.88e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.66 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIlwsgkpltpdAI--TAKVGYMPE 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI----------EIgeTVKLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ER-GLYPKETIksqllyFAALHG----MKKAEAIILLDDWMKRLNVvgKSTD---KIESLSKGNAQKVQLIACLMFKPQL 151
Cdd:TIGR03719 393 SRdALDPNKTV------WEEISGgldiIKLGKREIPSRAYVGRFNF--KGSDqqkKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|.
gi 951434962 152 LILDEPFSGLD 162
Cdd:TIGR03719 465 LLLDEPTNDLD 475
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-212 |
3.31e-14 |
|
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: 69.26 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN--AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT--PDAITAKVGYM 77
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdlEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYpKETIksqllyfaalhgmkkaeaiillddwmkrLNVVGKstdkieSLSKGNAQKVQLIACLMFKPQLLILDEP 157
Cdd:cd03247 81 NQRPYLF-DTTL----------------------------RNNLGR------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 158 FSGLDPVNSELLIKAILTAKQQGTmVIFSTHNMDNVQKLsDYIVMLKHGQTVLKG 212
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKT-LIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-207 |
3.49e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRfgNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGYMP 78
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPrsplDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EER---GLYPKETIKSQL--LYFAALHGMKKAEAII-------LLDDWMKRLNVVGKSTDK-IESLSKGNAQKVQLIACL 145
Cdd:PRK09700 345 ESRrdnGFFPNFSIAQNMaiSRSLKDGGYKGAMGLFhevdeqrTAENQRELLALKCHSVNQnITELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 146 MFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-218 |
3.55e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQhVSKRFGNFNAVSDLSfsLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpDAITA-------- 72
Cdd:PRK11144 1 MLELN-FKQQLGDLCLTVNLT--LPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF-DAEKGiclppekr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 KVGYMPEERGLYPKETIKSQLLYfaalhGMKKAEAiILLDDWMKRLNvvgkstdkIE--------SLSKGNAQKVQLIAC 144
Cdd:PRK11144 77 RIGYVFQDARLFPHYKVRGNLRY-----GMAKSMV-AQFDKIVALLG--------IEplldrypgSLSGGEKQRVAIGRA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 145 LMFKPQLLILDEPFSGLD-PVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK11144 143 LLTAPELLLMDEPLASLDlPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVW 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-221 |
3.80e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.95 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILW-------------------- 60
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdgenipamsrsrlytvrkrm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 61 -----SGKPLTPDAITAKVGYMPEERGLYPKETIKSQLlyfaalhgMKKAEAIILLddwmkrlnvvGKSTDKIESLSKGN 135
Cdd:PRK11831 87 smlfqSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTV--------MMKLEAVGLR----------GAAKLMPSELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 136 AQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAI--LTAKQQGTMVIFStHNMDNVQKLSDYIVMLKHGQTVLKGT 213
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVS-HDVPEVLSIADHAYIVADKKIVAHGS 227
|
250
....*....|....*
gi 951434962 214 PTEIY-------RQF 221
Cdd:PRK11831 228 AQALQanpdprvRQF 242
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-207 |
3.97e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 18 SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGYMPEER---GLYP----K 86
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIrsprDAIRAGIMLCPEDRkaeGIIPvhsvA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ETI-----KSQLLYFAALHGMKKAEaiiLLDDWMKRLNVVGKSTD-KIESLSKGNAQKVQLIACLMFKPQLLILDEPFSG 160
Cdd:PRK11288 350 DNInisarRHHLRAGCLINNRWEAE---NADRFIRSLNIKTPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 951434962 161 LDpVNSELLIKAILTA-KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK11288 427 ID-VGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-212 |
4.28e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.73 E-value: 4.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 5 QHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpltpDAITAKVGYMPE-ER-- 81
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR----DGQLRDLYALSEaERrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 ---------------GLYPKET----IKSQLLYFAALH-GMKKAEAIilldDWMKRLNVvgkSTDKIESL----SKGNAQ 137
Cdd:PRK11701 86 llrtewgfvhqhprdGLRMQVSaggnIGERLMAVGARHyGDIRATAG----DWLERVEI---DAARIDDLpttfSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 138 KVQLIACLMFKPQLLILDEPFSGLD-PVNSELL--IKAILTakQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKG 212
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDvSVQARLLdlLRGLVR--ELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-218 |
7.13e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 70.99 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF----GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITA- 72
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsEKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 --KVGY------------------MPEERGLYPKETIKSqllyfaalhgmKKAEaiiLLDdwmkrlnVVGKStDKIES-- 130
Cdd:PRK11153 81 rrQIGMifqhfnllssrtvfdnvaLPLELAGTPKAEIKA-----------RVTE---LLE-------LVGLS-DKADRyp 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 131 --LSKGNAQKVQLIACLMFKPQLLILDEPFSGLDP--VNSEL-LIKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKH 205
Cdd:PRK11153 139 aqLSGGQKQRVAIARALASNPKVLLCDEATSALDPatTRSILeLLKDI--NRELGLTIVLITHEMDVVKRICDRVAVIDA 216
|
250
....*....|...
gi 951434962 206 GQTVLKGTPTEIY 218
Cdd:PRK11153 217 GRLVEQGTVSEVF 229
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-219 |
7.14e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.93 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFI----KPDSGKILWSGKPLTpdAITA 72
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQ--RISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 K-----VG------YMPEERGLYPKETIKSQLLYFAALH--GMKKA---EAIILLD-----DWMKRLNVVGkstdkiESL 131
Cdd:PRK11022 81 KerrnlVGaevamiFQDPMTSLNPCYTVGFQIMEAIKVHqgGNKKTrrqRAIDLLNqvgipDPASRLDVYP------HQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 132 SKGNAQKVQL---IAClmfKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTM-VIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK11022 155 SGGMSQRVMIamaIAC---RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMaLVLITHDLALVAEAAHKIIVMYAGQ 231
|
250
....*....|..
gi 951434962 208 TVLKGTPTEIYR 219
Cdd:PRK11022 232 VVETGKAHDIFR 243
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
19-236 |
7.92e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.71 E-value: 7.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTTFHMIL--DFIKPDSGKILWSGKPLTPDAitakvgymPEER---GL-----YPKEt 88
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELS--------PDERaraGIflafqYPVE- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 89 IK----SQLLYFA--ALHG--MKKAEAIILLDDWMKRLNVvgkSTDKI-----ESLSKGNAQK---VQLiacLMFKPQLL 152
Cdd:COG0396 89 IPgvsvSNFLRTAlnARRGeeLSAREFLKLLKEKMKELGL---DEDFLdryvnEGFSGGEKKRneiLQM---LLLEPKLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 153 ILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNmdnvQKLSDYIV-----MLKHGQTVLKGTPtEIYrqfgrLRLD 227
Cdd:COG0396 163 ILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY----QRILDYIKpdfvhVLVDGRIVKSGGK-ELA-----LELE 232
|
....*....
gi 951434962 228 IEGYQNVER 236
Cdd:COG0396 233 EEGYDWLKE 241
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-217 |
1.22e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.84 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNavsdLSFSLH--SGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK-VGYM 77
Cdd:PRK10771 1 MLKLTDITWLYHHLP----MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRpVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKETIKSQL-LyfaALH-GMK-------KAEAI---ILLDDWMKRLNvvgkstdkiESLSKGNAQKVQLIACL 145
Cdd:PRK10771 77 FQENNLFSHLTVAQNIgL---GLNpGLKlnaaqreKLHAIarqMGIEDLLARLP---------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951434962 146 MFKPQLLILDEPFSGLDPVnselLIKAILT------AKQQGTMVIFStHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK10771 145 VREQPILLLDEPFSALDPA----LRQEMLTlvsqvcQERQLTLLMVS-HSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-202 |
1.37e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.69 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAK-------VGYMPEERGLYPK----E 87
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnqkLGFIYQFHHLLPDftalE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 88 TIKSQLLyfaaLHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSE 167
Cdd:PRK11629 107 NVAMPLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 951434962 168 LLIKAI-LTAKQQGTMVIFSTHNMDNVQKLSDYIVM 202
Cdd:PRK11629 183 SIFQLLgELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-207 |
1.38e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 4 LQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdAITAKVGYMPEERGL 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA--EAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 84 YP-KETIKSQLLyfaALHGMKKAEAiillddwMKRLNVVG---KSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:PRK11247 93 LPwKKVIDNVGL---GLKGQWRDAA-------LQALAAVGladRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 951434962 160 GLDP---VNSELLIKAILtaKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK11247 163 ALDAltrIEMQDLIESLW--QQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-207 |
4.08e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 67.21 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP------DAITAK 73
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 74 VGYMPEERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-218 |
4.60e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 4 LQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpDAITAK--VGYMPEER 81
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAErgVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 GLYPKETIKSQLLYFAALHGMKKAE---------AIILLDDWMKRlnvvgkstdKIESLSKGNAQKVQLIACLMFKPQLL 152
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKKEEinqrvnqvaEVLQLAHLLDR---------KPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 153 ILDEPFSGLDP---VNSELLIkAILTAKQQGTMvIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK11000 156 LLDEPLSNLDAalrVQMRIEI-SRLHKRLGRTM-IYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-223 |
4.85e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.22 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN-AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSG---KPLTPDAITAKVGYM 77
Cdd:PRK13657 335 VEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEERGLYPKeTIKSQL-----------LYFAAlhgmKKAEAIILLDDWMKRLN-VVGkstDKIESLSKGNAQKVQLIACL 145
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIrvgrpdatdeeMRAAA----ERAQAHDFIERKPDGYDtVVG---ERGRQLSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 146 MFKPQLLILDEPFSGLDpVNSELLIKAILTAKQQG--TMVIfsTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFGR 223
Cdd:PRK13657 487 LKDPPILILDEATSALD-VETEAKVKAALDELMKGrtTFII--AHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGR 562
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-89 |
5.37e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.99 E-value: 5.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIlwsgkpltpdAI--TAKVGYMPE 79
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----------KIgeTVKLAYVDQ 394
|
90
....*....|.
gi 951434962 80 ER-GLYPKETI 89
Cdd:PRK11819 395 SRdALDPNKTV 405
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
1.12e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTtFHMILDFIKPDSGKILWSGKP--LTPDAITAKVGYMPE 79
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKST-FLKCLNRMNELESEVRVEGRVefFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 ERGL---YPKETIKSQLLYFAALHGMK------KAEAIILLDDWMKRLNVVGKSTDKIES----LSKGNAQKVQLIACLM 146
Cdd:PRK14258 87 RRQVsmvHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 147 FKPQLLILDEPFSGLDPVNS---ELLIKAiLTAKQQGTMVIFsTHNMDNVQKLSDYIVMLKH-----GQTVLKGTPTEIY 218
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASmkvESLIQS-LRLRSELTMVIV-SHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-219 |
1.14e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 14 FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILwSGKPL-------TPDAITAKVGYMPEERG---- 82
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ-CDKMLlrrrsrqVIELSEQSAAQMRHVRGadma 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 ---------LYPKETIKSQLLYFAALH-GMKKAEAIILLDDWMKRLNVvgKSTDKIES-----LSKGNAQKVQLIACLMF 147
Cdd:PRK10261 108 mifqepmtsLNPVFTVGEQIAESIRLHqGASREEAMVEAKRMLDQVRI--PEAQTILSryphqLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951434962 148 KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTM-VIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYR 219
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-242 |
1.24e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.45 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTfHMILDFIKPDSGKILWSGKPLTPD--AITAKVG-YMP 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANrrALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERGLYPKETIKSQLLYFAALHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPF 158
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 159 SGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYRQFGRLRLDIEGYQNVErLK 238
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHAAE-LD 251
|
....
gi 951434962 239 RIQG 242
Cdd:NF000106 252 RMVG 255
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-218 |
1.54e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTpdAITAKvgYMPEER------------GL 83
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL--GMKDD--EWRAVRsdiqmifqdplaSL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 84 YPKETIKSQL-----LYFAAlhgMKKAEAIILLDDWMKRL----NVVGKSTdkiESLSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:PRK15079 112 NPRMTIGEIIaeplrTYHPK---LSRQEVKDRVKAMMLKVgllpNLINRYP---HEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 155 DEPFSGLDP------VNselLIKAIltAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK15079 186 DEPVSALDVsiqaqvVN---LLQQL--QREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVY 250
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
2.35e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.70 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIK--PD---SGKILWSGKPL----------- 65
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIfkmdvielrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 66 ------TPDAITAKVGYMPEERGLYPKETIKSQLLYFAALH-GMKKAEaiiLLDDWMKRLNVVGKStdkiesLSKGNAQK 138
Cdd:PRK14247 84 vqmvfqIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRwALEKAQ---LWDEVKDRLDAPAGK------LSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 139 VQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFsTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLV-THFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-209 |
3.43e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.35 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTfhM-ILDFIKPD---SGKILWSGKPLTPDAITAKvgy 76
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTL--MkVLSGVYPHgsyEGEILFDGEVCRFKDIRDS--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 mpEERGLypkeTIKSQLLyfAALHGMKKAEAIIL--------LDDW---MKR----LNVVGKSTD---KIESLSKGNAQK 138
Cdd:NF040905 76 --EALGI----VIIHQEL--ALIPYLSIAENIFLgnerakrgVIDWnetNRRarelLAKVGLDESpdtLVTDIGVGKQQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951434962 139 VQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQG-TMVIFStHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:NF040905 148 VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIIS-HKLNEIRRVADSITVLRDGRTI 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-216 |
3.79e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 26 SGQILSLIGQNGAGKSTTFHMILDFIKPD---SGKILWSGKPLTPDAITAKVGYMPEERGLYPKETIKSQLLYFAALH-- 100
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRmp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 101 -GMKKAEAIILLDDWMKRLN-------VVGkSTDKIESLSKGNAQKVQlIAC-LMFKPQLLILDEPFSGLDPVNSELLIK 171
Cdd:TIGR00955 130 rRVTKKEKRERVDEVLQALGlrkcantRIG-VPGRVKGLSGGERKRLA-FASeLLTDPPLLFCDEPTSGLDSFMAYSVVQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 951434962 172 AILTAKQQGTMVIFSTHN-MDNVQKLSDYIVMLKHGQTVLKGTPTE 216
Cdd:TIGR00955 208 VLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-198 |
6.15e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.41 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMI--LDFIKPD---SGKILWSGKPL-TPDAITA-- 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIySPRTDTVdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 73 --KVGYMPEERGLYPKeTIKSQLLYFAALHGMKKAEaiiLLDDWMKRlNVVGKST---------DKIESLSKGNAQKVQL 141
Cdd:PRK14239 85 rkEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQ---VLDEAVEK-SLKGASIwdevkdrlhDSALGLSGGQQQRVCI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 142 IACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFsTHNMDNVQKLSD 198
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV-TRSMQQASRISD 215
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-209 |
6.63e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.03 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTtfhmILDFI---KPD---SGKILWSGKPLTPDaITAKVGYMPEERGLYPKETIKSQ 92
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTT----LLDVLagrKTAgviTGEILINGRPLDKN-FQRSTGYVEQQDVHSPNLTVREA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 93 LLYFAALHGMKKAEAiillddwmKRLNVvgkstdkieslskgnaqKVQLIAclmfKPQLLILDEPFSGLDPVNSELLIK- 171
Cdd:cd03232 100 LRFSALLRGLSVEQR--------KRLTI-----------------GVELAA----KPSILFLDEPTSGLDSQAAYNIVRf 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 951434962 172 ---------AILTAKQQGTMVIFstHNMDNVqklsdyIVMLKHGQTV 209
Cdd:cd03232 151 lkkladsgqAILCTIHQPSASIF--EKFDRL------LLLKRGGKTV 189
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-221 |
6.90e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 64.44 E-value: 6.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTtFHMILDFI-KPDSGKILWSGKP--LTPDA-------- 69
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKST-FLRCINLLeTPDSGEIRVGGEEirLKPDRdgelvpad 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 70 ------ITAKVGYMPEERGLYPKETIKsQLLYFAALH--GMKKAEAIillDDWMKRLNVVGKStDKIES----LSKGNAQ 137
Cdd:COG4598 87 rrqlqrIRTRLGMVFQSFNLWSHMTVL-ENVIEAPVHvlGRPKAEAI---ERAEALLAKVGLA-DKRDAypahLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 138 KVQLIACLMFKPQLLILDEPFSGLDPvnsEL------LIKAIltAKQQGTMVIFsTHNMDNVQKLSDYIVMLKHGQTVLK 211
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDP---ELvgevlkVMRDL--AEEGRTMLVV-THEMGFARDVSSHVVFLHQGRIEEQ 235
|
250
....*....|....*...
gi 951434962 212 GTPTEIY--------RQF 221
Cdd:COG4598 236 GPPAEVFgnpkserlRQF 253
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-188 |
7.45e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 20 LSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKVGYMPEERGLYPKETIKSQLLYFAAL 99
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 100 HGMK------KAEAIILLDDWMKRLnvvgkstdkIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAI 173
Cdd:PRK13543 110 HGRRakqmpgSALAIVGLAGYEDTL---------VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 951434962 174 LTAKQQGTMVIFSTH 188
Cdd:PRK13543 181 SAHLRGGGAALVTTH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-214 |
1.13e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.54 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 21 SFSLH------SGQILSLIGQNGAGKSTTFHMILDFIKPDSGKilWSGKPLTPDAITAKVG-----YMPEERGLYPKETI 89
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFRGselqnYFTKLLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 90 KSQL--LYFAALHG-----MKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:cd03236 92 KPQYvdLIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 163 ---PVNSELLIKAILtakQQGTMVIFSTHNMDNVQKLSDYIvmlkhgqTVLKGTP 214
Cdd:cd03236 172 ikqRLNAARLIRELA---EDDNYVLVVEHDLAVLDYLSDYI-------HCLYGEP 216
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-213 |
1.15e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpltpdaitAKVGYMPEEr 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--------ANIGYYAQD- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 glypketiksqllyfaalHGMKKAEAIILLdDWMK-----------------RL----NVVGKStdkIESLSkGNAQKVQ 140
Cdd:PRK15064 391 ------------------HAYDFENDLTLF-DWMSqwrqegddeqavrgtlgRLlfsqDDIKKS---VKVLS-GGEKGRM 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 141 LIACLMF-KPQLLILDEPFSGLDPVNSELLIKAIltAKQQGTmVIFSTHNMDNVQKLSDYIVMLKHGQTV-LKGT 213
Cdd:PRK15064 448 LFGKLMMqKPNVLVMDEPTNHMDMESIESLNMAL--EKYEGT-LIFVSHDREFVSSLATRIIEITPDGVVdFSGT 519
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-217 |
1.23e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 12 GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPD----SGKILWSGKPLTPDAITAKVGYMPEE------- 80
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKIIGREiamifqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 --RGLYPKETIKSQLL----------YFAALHGMKKAEAIILLddwmKRlnvVG-KSTDKIES-----LSKGNAQKVQLI 142
Cdd:COG4170 98 psSCLDPSAKIGDQLIeaipswtfkgKWWQRFKWRKKRAIELL----HR---VGiKDHKDIMNsypheLTEGECQKVMIA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 143 ACLMFKPQLLILDEPFSGLDPVNsELLIKAILTA--KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTT-QAQIFRLLARlnQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-209 |
1.24e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 15 NAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGK---PLTPDAITA-----KVGYMPEERGLYPK 86
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQAlrrdiQFIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ETIKSQLLYFAALHGMKKAEAIILLDDWMkrLNVVGKSTDKI----ESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAARVAWL--LERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 951434962 163 PVNSELLIKAILTAKQQ-GTMVIFSTHNMDNVQKLSDYIVMLKHGQTV 209
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-188 |
1.82e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTtfhmILDFIKPD-----------------SGKILWSgkp 64
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST----LLSLITGDhpqgysndltlfgrrrgSGETIWD--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 65 ltpdaITAKVGYMPEERGL-YPKET-IKSQLL--YFAALhGMKKA---EAIILLDDWMKRLNVVGKSTDK-IESLSKGNa 136
Cdd:PRK10938 334 -----IKKHIGYVSSSLHLdYRVSTsVRNVILsgFFDSI-GIYQAvsdRQQKLAQQWLDILGIDKRTADApFHSLSWGQ- 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 951434962 137 QKVQLIACLMFK-PQLLILDEPFSGLDPVNSELLIKAILTAKQQG-TMVIFSTH 188
Cdd:PRK10938 407 QRLALIVRALVKhPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGeTQLLFVSH 460
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-220 |
2.28e-11 |
|
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: 63.94 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 9 KRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIkPDSGKILWSGKPLtpDAITAKVgyMPEER------- 81
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDL--DGLSRRA--LRPLRrrmqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 -----GLYPKETIkSQLLyfA---ALH--GMKKAE----AIILLDDwmkrlnvVGKSTDKIE----SLSKGNAQKVQlIA 143
Cdd:COG4172 369 qdpfgSLSPRMTV-GQII--AeglRVHgpGLSAAErrarVAEALEE-------VGLDPAARHryphEFSGGQRQRIA-IA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 144 -CLMFKPQLLILDEPFSGLDpvNS------ELLIKaiLTAKQQGTMvIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTE 216
Cdd:COG4172 438 rALILEPKLLVLDEPTSALD--VSvqaqilDLLRD--LQREHGLAY-LFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQ 512
|
....
gi 951434962 217 IYRQ 220
Cdd:COG4172 513 VFDA 516
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-239 |
3.06e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.16 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 11 FGNFN-----AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGkpltpdaitaKVGYMPEERGLYP 85
Cdd:TIGR01271 431 FSNFSlyvtpVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------RISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 86 KeTIKSQLL---------YFAALHGMKKAEAIILLDDWMKRLNVVGKSTdkiesLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:TIGR01271 501 G-TIKDNIIfglsydeyrYTSVIKACQLEEDIALFPEKDKTVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 157 PFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQ---FGRLRLDIEGYQN 233
Cdd:TIGR01271 575 PFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKrpdFSSLLLGLEAFDN 653
|
....*.
gi 951434962 234 VERLKR 239
Cdd:TIGR01271 654 FSAERR 659
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-218 |
3.14e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKST---TFHMILDfIKPDS---GKILWSGK-----PLTPDAI 70
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLE-LNEEArveGEVRLFGRniyspDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 71 TAKVGYMPEERGLYPKETIKSQLLYFAALHGMKKAEAII------------LLDDWMKRLNvvgkstDKIESLSKGNAQK 138
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELdervewalkkaaLWDEVKDRLN------DYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 139 VQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFsTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-222 |
3.40e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.50 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP---------------------DAITAKV 74
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytlaslrnqvalvsqnvhlfnDTIANNI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYMPEERglYPKETIKSqllyfAA--LHGMkkaEAIILLDDWMKrlNVVGKSTdkiESLSKGNAQKVQLIACLMFKPQLL 152
Cdd:PRK11176 438 AYARTEQ--YSREQIEE-----AArmAYAM---DFINKMDNGLD--TVIGENG---VLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 153 ILDEPFSGLDpVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFG 222
Cdd:PRK11176 503 ILDEATSALD-TESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-162 |
4.66e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKsTTFHMIL------DFIkpdSGKILWSGKPLT----PDAITAKVGYMPEER---GL 83
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGR-TELAMSVfgrsygRNI---SGTVFKDGKEVDvstvSDAIDAGLAYVTEDRkgyGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 84 YPKETIKSQLLyFAALHGMKKA------EAIILLDDWMKRLNVvgKSTD---KIESLSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:NF040905 352 NLIDDIKRNIT-LANLGKVSRRgvidenEEIKVAEEYRKKMNI--KTPSvfqKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
....*...
gi 951434962 155 DEPFSGLD 162
Cdd:NF040905 429 DEPTRGID 436
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-188 |
6.34e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN-AVSDLSFSLHSGQILSLIGQNGAGKStTFHMILD-FIKPDSGKILWSGKPLTPDAITAkvgYmpe 79
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKS-TLAMLLTgLYQPQSGEILLDGKPVTAEQPED---Y--- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 80 eRGLYpkETIKSQLLYFAALHGMKKAEA-IILLDDWMKRLNVVGKST---DKIE--SLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK10522 396 -RKLF--SAVFTDFHLFDQLLGPEGKPAnPALVEKWLERLKMAHKLEledGRISnlKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190
....*....|....*....|....*....|....*.
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTA-KQQGTMVIFSTH 188
Cdd:PRK10522 473 LDEWAADQDPHFRREFYQVLLPLlQEMGKTIFAISH 508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-184 |
7.09e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 7.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 23 SLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpltpdaitaKVGYMPEErgLYPKETIKSQLLYFAALHGM 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD---------TVSYKPQY--IKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 103 KKAEAIIllDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDpVNSELL----IKAILTAKQ 178
Cdd:cd03237 90 YTHPYFK--TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-VEQRLMaskvIRRFAENNE 166
|
....*.
gi 951434962 179 QGTMVI 184
Cdd:cd03237 167 KTAFVV 172
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-217 |
8.24e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 11 FGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDA---ITAKVGYMPEE------- 80
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAskeVARRIGLLAQNattpgdi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 -------RGLYPKETIKSQLlyfaalhgMKKAEAIIllDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK10253 97 tvqelvaRGRYPHQPLFTRW--------RKEDEEAV--TKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 154 LDEPFSGLDpVNSELLIKAILTA--KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK10253 167 LDEPTTWLD-ISHQIDLLELLSElnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-183 |
1.34e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.75 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMIldfikpdSGkiLW---SGKPLTPDAitAKVGYMPEErgLY-PKETIKSQ 92
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------AG--LWpygSGRIARPAG--ARVLFLPQR--PYlPLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 93 LLYFAALHGMKKAEAI-IL----LDDWMKRLNVVgKSTDKIesLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSE 167
Cdd:COG4178 446 LLYPATAEAFSDAELReALeavgLGHLAERLDEE-ADWDQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
170
....*....|....*.
gi 951434962 168 LLIKAILTAKQQGTMV 183
Cdd:COG4178 523 ALYQLLREELPGTTVI 538
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
2.10e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.63 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMI--LDFIKpdSGKILWSGKpltpdaitaKVGYM 77
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagLERIT--SGEIWIGGR---------VVNEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 -PEERG---------LYPKETIKSQLLYFAALHGMKKAE--------AIIL-LDDWMKRlnvvgkstdKIESLSKGNAQK 138
Cdd:PRK11650 72 ePADRDiamvfqnyaLYPHMSVRENMAYGLKIRGMPKAEieervaeaARILeLEPLLDR---------KPRELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 139 VQLIACLMFKPQLLILDEPFSGLDP---VNSELLIKAIltakQQ--GTMVIFSTHnmDNVQ--KLSDYIVMLKHGQTVLK 211
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAklrVQMRLEIQRL----HRrlKTTSLYVTH--DQVEamTLADRVVVMNGGVAEQI 216
|
....*....
gi 951434962 212 GTPTEIYRQ 220
Cdd:PRK11650 217 GTPVEVYEK 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-219 |
2.55e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPD----SGKILWSGKPLTPDAI----TAKVgyMPEERGLY-PKE 87
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCALrgrkIATI--MQNPRSAFnPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 88 TIKSQLLYFAALHGMKKAEAIILlddwmKRLNVVG-KSTDKIESL-----SKGNAQKVQLIACLMFKPQLLILDEPFSGL 161
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLT-----AALEAVGlENAARVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 162 DPVnSELLIKAILTA--KQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIYR 219
Cdd:PRK10418 172 DVV-AQARILDLLESivQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-207 |
5.52e-10 |
|
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: 57.86 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 18 SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpltpdaitakVGYMPEERGLYPkETIKSQLLyFA 97
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS----------IAYVSQEPWIQN-GTIRENIL-FG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 98 ALHGMKKAEAII----LLDDwMKRLN-----VVGkstDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDP-VNSE 167
Cdd:cd03250 90 KPFDEERYEKVIkacaLEPD-LEILPdgdltEIG---EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAhVGRH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 951434962 168 LLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQ 207
Cdd:cd03250 166 IFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-218 |
6.20e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.21 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT-PDAITAKvgympEER------------G 82
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkADPEAQK-----LLRqkiqivfqnpygS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 LYPKETIKSQ----LLYFAALHGMKKAEAIIlldDWMKRlnvVGKSTDKIES----LSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:PRK11308 105 LNPRKKVGQIleepLLINTSLSAAERREKAL---AMMAK---VGLRPEHYDRyphmFSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 155 DEPFSGLD-PVNSELLikAILTAKQQ--GTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEIY 218
Cdd:PRK11308 179 DEPVSALDvSVQAQVL--NLMMDLQQelGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 243
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-214 |
1.16e-09 |
|
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: 57.12 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFG-NFNAV-SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGY 76
Cdd:cd03244 3 IEFKNVSLRYRpNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISkigLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYPKeTIKSQL----------LYfAALHGMKKAEAIILLDDwmkrlnvvGKSTDKIES---LSKGNAQKVQLIA 143
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLdpfgeysdeeLW-QALERVGLKEFVESLPG--------GLDTVVEEGgenLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951434962 144 CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTmVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTP 214
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCT-VLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-223 |
1.42e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.58 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFNAV-SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP---DAITAKVGYM 77
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlshSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 78 PEE-----RGLYPKETIK---SQLLYFAALHGMKKAEAIILLDDWM-KRLNVVGKStdkiesLSKGNAQKVQLIACLMFK 148
Cdd:PRK10790 421 QQDpvvlaDTFLANVTLGrdiSEEQVWQALETVQLAELARSLPDGLyTPLGEQGNN------LSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 149 PQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFStHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQFGR 223
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQGR 567
|
|
| DUF4162 |
pfam13732 |
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC ... |
212-290 |
1.57e-09 |
|
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC transporter proteins. The function is not known.
Pssm-ID: 463971 [Multi-domain] Cd Length: 82 Bit Score: 53.75 E-value: 1.57e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 212 GTPTEIYRQFGRLRLDIEgYQNVERLKRIQGVKKVTLMANGVHLELNNEQCGKIIFTEVTKHGYVPVFNQHYPDLEAIF 290
Cdd:pfam13732 1 GTLEEIKRSYGRNRIEVE-TADAEELLELPGVEEVEEEGGGLELKLEDEEAANELLAALLSGGEIRSFEEEEPSLNDIF 78
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-219 |
4.32e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFG------NFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIK--PDSGKILWSGKPLTPDAITAKv 74
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGREASLID- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 gympeerGLYPKETIKsqlLYFAALHGMKKAEAIILLDdwmkrlnvvgkstdKIESLSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:COG2401 105 -------AIGRKGDFK---DAVELLNAVGLSDAVLWLR--------------RFKELSTGQKFRFRLALLLAERPKLLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 155 DEPFSGLDPVNSELLIKAILT-AKQQGTMVIFSTHNMDNVQKLSDYIVMLKHgqtvLKGTPTEIYR 219
Cdd:COG2401 161 DEFCSHLDRQTAKRVARNLQKlARRAGITLVVATHHYDVIDDLQPDLLIFVG----YGGVPEEKRR 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-214 |
5.16e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.11 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNF--NAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGK-----PLTpdAITAKV 74
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIdistiPLE--DLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 75 GYMPEERGLYpKETIKSQLLYFaalhGMKKAEAIillddwMKRLNVVGKStdkiESLSKGNAQKVQLIACLMFKPQLLIL 154
Cdd:cd03369 85 TIIPQDPTLF-SGTIRSNLDPF----DEYSDEEI------YGALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 155 DEPFSGLDPVNSELLIKAILTAKQQGTMVIFStHNMDNVQKLsDYIVMLKHGQTVLKGTP 214
Cdd:cd03369 150 DEATASIDYATDALIQKTIREEFTNSTILTIA-HRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-223 |
8.22e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 56.37 E-value: 8.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF--GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLT---PDAITAKVGY 76
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAdysEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEERGLYpKETIKSQLLyfaalhgMKKAEAIillDDWMKR-LNVVG--KSTDKIESL-----------SKGNAQKVQLI 142
Cdd:PRK11160 419 VSQRVHLF-SATLRDNLL-------LAAPNAS---DEALIEvLQQVGleKLLEDDKGLnawlgeggrqlSGGEQRRLGIA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 143 ACLMFKPQLLILDEPFSGLDPVnSELLIKAILTAKQQGTMVIFSTHNMDNVQKLsDYIVMLKHGQTVLKGTPTEIYRQFG 222
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAE-TERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
.
gi 951434962 223 R 223
Cdd:PRK11160 566 R 566
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-186 |
9.00e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.11 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 3 ELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIlWSGKPLtpdaitaKVGYMPEERG 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKL-------EVAYFDQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 -LYPKETIKSQLlyfaalhGMKKAEAII---------LLDDWM---KRlnvvgkSTDKIESLSKGNAQKVqLIACLMFKP 149
Cdd:PRK11147 393 eLDPEKTVMDNL-------AEGKQEVMVngrprhvlgYLQDFLfhpKR------AMTPVKALSGGERNRL-LLARLFLKP 458
|
170 180 190
....*....|....*....|....*....|....*...
gi 951434962 150 -QLLILDEPFSGLDPVNSELLIKaiLTAKQQGTMVIFS 186
Cdd:PRK11147 459 sNLLILDEPTNDLDVETLELLEE--LLDSYQGTVLLVS 494
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-235 |
9.05e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 16 AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPdaitakvgympeerglypketiksqlly 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK---------------------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 96 faalhgmkkaeaiILLDDWMKRLNVVGK--------------------STDKIES------------------------- 130
Cdd:PRK10789 382 -------------LQLDSWRSRLAVVSQtpflfsdtvannialgrpdaTQQEIEHvarlasvhddilrlpqgydtevger 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 131 ---LSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPvNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMlKHGQ 207
Cdd:PRK10789 449 gvmLSGGQKQRISIARALLLNAEILILDDALSAVDG-RTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVM-QHGH 526
|
250 260
....*....|....*....|....*...
gi 951434962 208 TVLKGTPTEIYRQFGRLRlDIEGYQNVE 235
Cdd:PRK10789 527 IAQRGNHDQLAQQSGWYR-DMYRYQQLE 553
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-209 |
1.06e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRF----GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMI--LDfiKPDSGKILWSGK---PLTPDAIT 71
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcLD--KPTSGTYRVAGQdvaTLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 72 A----KVGYMPEERGLYPKETIKSQLLYFAALHGMKKAE----AIILLddwmKRLNVVGKSTDKIESLSKGNAQKVQLIA 143
Cdd:PRK10535 82 QlrreHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQrllrAQELL----QRLGLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 144 CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDnVQKLSDYIVMLKHGQTV 209
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIV 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-188 |
1.12e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 53.31 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIlwsGKPLTPDAItakvgYMPeERGLYPKETIKSQLLYf 96
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEDLL-----FLP-QRPYLPLGTLREQLIY- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 97 aalhgmkkaeaiilldDWMKRlnvvgkstdkiesLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPvNSELLIKAILta 176
Cdd:cd03223 87 ----------------PWDDV-------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDE-ESEDRLYQLL-- 134
|
170
....*....|..
gi 951434962 177 KQQGTMVIFSTH 188
Cdd:cd03223 135 KELGITVISVGH 146
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-215 |
1.26e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDfiKPD----SGKILWSGKPLTPdaitakvgY 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILD--------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEER---GL-----YPKE---TIKSQLLYFA-----ALHGMKKAEAIILLDDWMKRLNVVGKSTDKI-----ESLSKGN 135
Cdd:CHL00131 77 EPEERahlGIflafqYPIEipgVSNADFLRLAynskrKFQGLPELDPLEFLEIINEKLKLVGMDPSFLsrnvnEGFSGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 136 AQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHnmdnVQKLSDYIV-----MLKHGQTVL 210
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH----YQRLLDYIKpdyvhVMQNGKIIK 232
|
....*
gi 951434962 211 KGTPT 215
Cdd:CHL00131 233 TGDAE 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-239 |
1.32e-08 |
|
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: 54.86 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 11 FGNFNAV-----SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGkpltpdaitaKVGYMPEERGLYP 85
Cdd:cd03291 42 FSNLCLVgapvlKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----------RISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 86 KeTIKSQLL---------YFAALHGMKKAEAIILLDDwmKRLNVVGKSTdkiESLSKGNAQKVQLIACLMFKPQLLILDE 156
Cdd:cd03291 112 G-TIKENIIfgvsydeyrYKSVVKACQLEEDITKFPE--KDNTVLGEGG---ITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 157 PFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKlSDYIVMLKHGQTVLKGTPTEIYRQ---FGRLRLDIEGYQN 233
Cdd:cd03291 186 PFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQSLrpdFSSKLMGYDTFDQ 264
|
....*.
gi 951434962 234 VERLKR 239
Cdd:cd03291 265 FSAERR 270
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-241 |
1.95e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 4 LQHVSKRF-GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILwsgkpLTPDAitaKVGYMPEERG 82
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----PQPGI---KVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 83 LYPKETIKSQLlyFAALHGMKKA----EAIILL-----DDWMKRLNVVGKSTDKIES----------------------- 130
Cdd:TIGR03719 79 LDPTKTVRENV--EEGVAEIKDAldrfNEISAKyaepdADFDKLAAEQAELQEIIDAadawdldsqleiamdalrcppwd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 131 -----LSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAIltAKQQGTmVIFSTHN---MDNVqklSDYIVM 202
Cdd:TIGR03719 157 advtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGT-VVAVTHDryfLDNV---AGWILE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 951434962 203 LKHGQTV-LKGTPTEIYRQfGRLRLDIEGYQNVERLKRIQ 241
Cdd:TIGR03719 231 LDRGRGIpWEGNYSSWLEQ-KQKRLEQEEKEESARQKTLK 269
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-217 |
2.22e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 12 GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMIL-----------DFIKPDSGKILwsgkPLTPDAITAKVG----- 75
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwrvtaDRMRFDDIDLL----RLSPRERRKLVGhnvsm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 76 -YMPEERGLYPKETIKSQLLyfAALHGMKKAEAIILLDDWMKR-----LNVVG-KSTDKIES-----LSKGNAQKVQLIA 143
Cdd:PRK15093 94 iFQEPQSCLDPSERVGRQLM--QNIPGWTYKGRWWQRFGWRKRraielLHRVGiKDHKDAMRsfpyeLTEGECQKVMIAI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 144 CLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQ-QGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PRK15093 172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-216 |
2.83e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.95 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 11 FGNFNAVSDLSFSLHSGQILSLIGQNGAGKsTTFHMILDFIKPD------SGKILWSGKPL--TPDAIT--AKVGYMPEE 80
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGK-TTFLRTLNRMNDKvsgyrySGDVLLGGRSIfnYRDVLEfrRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLlyfAALHGMKKAEAIILLDDWMKRLNVVG-------KSTDKIESLSKGNAQKVQLIACLMFKPQLLI 153
Cdd:PRK14271 110 PNPFPMSIMDNVL---AGVRAHKLVPRKEFRGVAQARLTEVGlwdavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951434962 154 LDEPFSGLDPVNSELLIKAILTAKQQGTMVIFsTHNMDNVQKLSDYIVMLKHGQTVLKGtPTE 216
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIRSLADRLTVIIV-THNLAQAARISDRAALFFDGRLVEEG-PTE 247
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-217 |
3.59e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.63 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 130 SLSKGNAQKVQLIACLMFK---PQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDnVQKLSDYIVML--- 203
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VIKTADYIIDLgpe 907
|
90
....*....|....*..
gi 951434962 204 ---KHGQTVLKGTPTEI 217
Cdd:TIGR00630 908 ggdGGGTVVASGTPEEV 924
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
8-184 |
5.11e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 8 SKRFGNFNAVSDLSFsLHSGQILSLIGQNGAGKsTTFHMIL-DFIKPDSGKILWsgkpltpdaiTAKVGYMPEERGLYPK 86
Cdd:PRK13409 347 TKKLGDFSLEVEGGE-IYEGEVIGIVGPNGIGK-TTFAKLLaGVLKPDEGEVDP----------ELKISYKPQYIKPDYD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ETIkSQLLYFAAlhgmKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDpVNS 166
Cdd:PRK13409 415 GTV-EDLLRSIT----DDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQ 488
|
170 180
....*....|....*....|..
gi 951434962 167 ELL----IKAILTAKQQGTMVI 184
Cdd:PRK13409 489 RLAvakaIRRIAEEREATALVV 510
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-207 |
5.16e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 14 FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKpLTPDAITAkvGYMPEERGLypkETIKSQL 93
Cdd:PRK13546 37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIAISA--GLSGQLTGI---ENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 94 LyfaaLHGMKKAEAIILLDDWMKRLNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAI 173
Cdd:PRK13546 111 L----CMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190
....*....|....*....|....*....|....
gi 951434962 174 LTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK13546 187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGK 220
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
130-203 |
7.99e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.68 E-value: 7.99e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 130 SLSKGNAQKVQLIACLMF---KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMdNVQKLSDYIVML 203
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLEL 884
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-189 |
1.14e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.70 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGN----FNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP------DAI 70
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeearAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 71 TAK-VGYMPEERGLYPKETIKSQLLYFAALHGMK----KAEAIILLddwmKRLNvVGKSTDKIES-LSKGNAQKVQLIAC 144
Cdd:PRK10584 86 RAKhVGFVFQSFMLIPTLNALENVELPALLRGESsrqsRNGAKALL----EQLG-LGKRLDHLPAqLSGGEQQRVALARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 951434962 145 LMFKPQLLILDEPFSGLDPVNSELLIKAILTA-KQQGTMVIFSTHN 189
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-202 |
1.15e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDsGKILWSGkpLTPDAITAK-----VGYMPEE---------RGLY 84
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDG--VSWNSVTLQtwrkaFGVIPQKvfifsgtfrKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 85 PKETIKSQLLYFAALH-GMKKaeaiiLLDDWMKRLNVVgkSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDP 163
Cdd:TIGR01271 1314 PYEQWSDEEIWKVAEEvGLKS-----VIEQFPDKLDFV--LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
170 180 190
....*....|....*....|....*....|....*....
gi 951434962 164 VNSELLIKAILTAKQQGTmVIFSTHNMDNVQKLSDYIVM 202
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNCT-VILSEHRVEALLECQQFLVI 1424
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-207 |
1.20e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRfgNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTP----DAITAKVGY 76
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnanEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 77 MPEER---GLYPK---------ETIKSQLLYFAALHGMKKAEAIILLDDWMkRLNVVGKSTdKIESLSKGNAQKVQLIAC 144
Cdd:PRK10982 328 VTEERrstGIYAYldigfnsliSNIRNYKNKVGLLDNSRMKSDTQWVIDSM-RVKTPGHRT-QIGSLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 145 LMFKPQLLILDEPFSGLDpVNSELLIKAILT--AKQQGTMVIFSTHnMDNVQKLSDYIVMLKHGQ 207
Cdd:PRK10982 406 LLTQPEILMLDEPTRGID-VGAKFEIYQLIAelAKKDKGIIIISSE-MPELLGITDRILVMSNGL 468
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-162 |
2.01e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 26 SGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIlwsGKPLTPDAI------TAKVGYMpeeRGLYPKE---TIKSQLLYF 96
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVlkrfrgTELQDYF---KKLANGEikvAHKPQYVDL 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951434962 97 A--ALHG-----MKKAEAIILLDDWMKRLNvVGKSTDK-IESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLD 162
Cdd:COG1245 172 IpkVFKGtvrelLEKVDERGKLDELAEKLG-LENILDRdISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-206 |
2.02e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.79 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 13 NFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKvgyMPEERGLYPKETIKSQ 92
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAT---RSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 93 LL--------YFAALHGMKKAEAIILLDDWMKRLNVV--GKSTDKIE---SLSKGNAQKVQLIACLMFKPQLLILDEPFS 159
Cdd:cd03290 90 LLnatveeniTFGSPFNKQRYKAVTDACSLQPDIDLLpfGDQTEIGErgiNLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 951434962 160 GLD-PVNSELLIKAILTAKQQGT-MVIFSTHNMDNVQKlSDYIVMLKHG 206
Cdd:cd03290 170 ALDiHLSDHLMQEGILKFLQDDKrTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-223 |
2.34e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 51.74 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPL---TPDAITAKVGYMPEERGLYpKETIKSQLLY 95
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdvTQASLRAAIGIVPQDTVLF-NDTIAYNIAY 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 96 faALHGMKKAE---AIIL--LDDWMKRL-----NVVGKSTDKiesLSKGNAQKVQlIA-CLMFKPQLLILDEPFSGLDpV 164
Cdd:COG5265 455 --GRPDASEEEveaAARAaqIHDFIESLpdgydTRVGERGLK---LSGGEKQRVA-IArTLLKNPPILIFDEATSALD-S 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951434962 165 NSElliKAILTA-----KQQGTMVIfsTHnmdnvqKLS-----DYIVMLKHGQTVLKGTPTEIYRQFGR 223
Cdd:COG5265 528 RTE---RAIQAAlrevaRGRTTLVI--AH------RLStivdaDEILVLEAGRIVERGTHAELLAQGGL 585
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
131-220 |
3.14e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 131 LSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVL 210
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE 215
|
90
....*....|
gi 951434962 211 KGTPTEIYRQ 220
Cdd:PRK10938 216 TGEREEILQQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-184 |
3.93e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 7 VSKRFGNFNAVSDlSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWsgkpltpdaiTAKVGYMPEerglYPK 86
Cdd:COG1245 347 LTKSYGGFSLEVE-GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE----------DLKISYKPQ----YIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 87 ----ETIKsQLLYFAALHGMkkaEAIILLDDWMKRLNvVGKSTDK-IESLSKGNAQKVQLIACLMFKPQLLILDEPFSGL 161
Cdd:COG1245 412 pdydGTVE-EFLRSANTDDF---GSSYYKTEIIKPLG-LEKLLDKnVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180
....*....|....*....|....*..
gi 951434962 162 DpVNSELL----IKAILTAKQQGTMVI 184
Cdd:COG1245 487 D-VEQRLAvakaIRRFAENRGKTAMVV 512
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
130-214 |
4.70e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.92 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 130 SLSKGNAQKVQLIACLMFK---PQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDnVQKLSDYIVML--- 203
Cdd:cd03271 169 TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VIKCADWIIDLgpe 247
|
90
....*....|....
gi 951434962 204 ---KHGQTVLKGTP 214
Cdd:cd03271 248 ggdGGGQVVASGTP 261
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
127-207 |
4.87e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 127 KIESLSKGNAQKVQLiACLMF---KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDnVQKLSDYIVML 203
Cdd:cd03238 84 KLSTLSGGELQRVKL-ASELFsepPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD-VLSSADWIIDF 161
|
....
gi 951434962 204 KHGQ 207
Cdd:cd03238 162 GPGS 165
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-202 |
7.55e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.47 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 15 NAV-SDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDsGKIL-----WSGKPLTP-----DAITAKVGYM--PEER 81
Cdd:cd03289 17 NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQidgvsWNSVPLQKwrkafGVIPQKVFIFsgTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 82 GLYPKETIKSQLLYfaalhgmKKAEAIIL---LDDWMKRLNVVgkSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPF 158
Cdd:cd03289 96 NLDPYGKWSDEEIW-------KVAEEVGLksvIEQFPGQLDFV--LVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 951434962 159 SGLDPVNSElLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVM 202
Cdd:cd03289 167 AHLDPITYQ-VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVI 209
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-247 |
1.95e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.46 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 27 GQILSLIGQNGAGKsTTFHMILDFIKPD---SGKILWSGKPLTPDAITAKVGYMPEERGLYPKETIKSQLLYFAALHGMK 103
Cdd:PLN03140 906 GVLTALMGVSGAGK-TTLMDVLAGRKTGgyiEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRLPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 104 ---KAEAIILLDDWMKRLN-------------VVGKSTDKIESLSKGnaqkVQLIAclmfKPQLLILDEPFSGLDPVNSE 167
Cdd:PLN03140 985 evsKEEKMMFVDEVMELVEldnlkdaivglpgVTGLSTEQRKRLTIA----VELVA----NPSIIFMDEPTSGLDARAAA 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 168 LLIKAILTAKQQGTMVIFSTH--NMDNVQKLSDYIVMLKHGQTVLKGTpteiyrqFGRlrldiEGYQNVERLKRIQGVKK 245
Cdd:PLN03140 1057 IVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSGP-------LGR-----NSHKIIEYFEAIPGVPK 1124
|
..
gi 951434962 246 VT 247
Cdd:PLN03140 1125 IK 1126
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
2.14e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 1 MIELQHVSKRFGNFNaVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAiTAKVGYMPEE 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKN-LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 81 RGLYPKETIKSQLLYFAALHgmKKAEAIILLDDWMKRLNVVGKstdKIESLSKGNAQKV---QLIAClmfKPQLLILDEP 157
Cdd:PRK13541 79 LGLKLEMTVFENLKFWSEIY--NSAETLYAAIHYFKLHDLLDE---KCYSLSSGMQKIVaiaRLIAC---QSDLWLLDEV 150
|
170 180 190
....*....|....*....|....*....|.
gi 951434962 158 FSGLDPVNSELLIKAILTAKQQGTMVIFSTH 188
Cdd:PRK13541 151 ETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-217 |
3.06e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 20 LSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAIT---AKVGYMPEERGLYPKeTIKSQLLYF 96
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlrRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 97 AALH--GMKKAEAIILLDDWMKR--LNVVGKSTDKIESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKA 172
Cdd:PLN03232 1334 SEHNdaDLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRT 1413
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 951434962 173 ILTAKQQGTMVIFStHNMDNVQKlSDYIVMLKHGQTVLKGTPTEI 217
Cdd:PLN03232 1414 IREEFKSCTMLVIA-HRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
7-189 |
6.76e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.43 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 7 VSKRFGNFNAVSDLSFSlhSGQILSLIGQNGAGKSTTFhmildfikpdsgkilwsgkpltpDAITAKVG--YMPEERGLY 84
Cdd:cd03227 3 VLGRFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTIL-----------------------DAIGLALGgaQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 85 PKETIKSqllyfaalhGMKKAEAIILLDdwmkrlnvvgkstdkieSLSKGNAQKVQLIACL---MFKP-QLLILDEPFSG 160
Cdd:cd03227 58 VKAGCIV---------AAVSAELIFTRL-----------------QLSGGEKELSALALILalaSLKPrPLYILDEIDRG 111
|
170 180
....*....|....*....|....*....
gi 951434962 161 LDPVNSELLIKAILTAKQQGTMVIFSTHN 189
Cdd:cd03227 112 LDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-221 |
1.17e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRFGNFN--------------------AVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWS 61
Cdd:PRK13545 5 VKFEHVTKKYKMYNkpfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 62 GkplTPDAITAKVGYMPEERGLypkETIKSQLLyfaaLHGMKKAE------AIILLDDWMKRLNvvgkstDKIESLSKGN 135
Cdd:PRK13545 85 G---SAALIAISSGLNGQLTGI---ENIELKGL----MMGLTKEKikeiipEIIEFADIGKFIY------QPVKTYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 136 AQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVQKLSDYIVMLKHGQTVLKGTPT 215
Cdd:PRK13545 149 KSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
....*....
gi 951434962 216 EI---YRQF 221
Cdd:PRK13545 229 EVvdhYDEF 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-194 |
5.46e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.63 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 19 DLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSG----KPLTPDAITAKVGYMPEERGLYpKETIKSQLL 94
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINLKWWRSKIGVVSQDPLLF-SNSIKNNIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 95 YfaALHGMKKAEAI--------------------------------------------------------------ILLD 112
Cdd:PTZ00265 482 Y--SLYSLKDLEALsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvdvskkVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 113 DWMKRL-----NVVGKSTDKiesLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILTAK-QQGTMVIFS 186
Cdd:PTZ00265 560 DFVSALpdkyeTLVGSNASK---LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIII 636
|
....*...
gi 951434962 187 THNMDNVQ 194
Cdd:PTZ00265 637 AHRLSTIR 644
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
128-189 |
7.36e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.53 E-value: 7.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951434962 128 IESLSKGNAQKVQLIACLMF---KPQLLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHN 189
Cdd:pfam13304 234 AFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHS 298
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-235 |
8.64e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.17 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 20 LSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKIlwsgkpltpdAITAKVGYMPEERGLyPKETIKSQLLYFAAL 99
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----------HMKGSVAYVPQQAWI-QNDSLRENILFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 100 HG---MKKAEAIILLDDwmkrLNVVgKSTDKIE------SLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLI 170
Cdd:TIGR00957 726 NEkyyQQVLEACALLPD----LEIL-PSGDRTEigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951434962 171 KAILTAKQ--QGTMVIFSTHNMDNVQKLsDYIVMLKHGQTVLKGTPTEIYRQFGRLRLDIEGYQNVE 235
Cdd:TIGR00957 801 EHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDE 866
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-205 |
1.25e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 2 IELQHVSKRF---GNFNAVSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWSGKPLTPDAITAKVGYMP 78
Cdd:PTZ00265 1166 IEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGD 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 79 EERGLYPKE--------------------------------------------TIKSQ--LLYF-------------AAL 99
Cdd:PTZ00265 1246 EEQNVGMKNvnefsltkeggsgedstvfknsgkilldgvdicdynlkdlrnlfSIVSQepMLFNmsiyenikfgkedATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 100 HGMKKAEAIILLDDWMKRL------NV--VGKStdkiesLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPvNSELLI- 170
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLpnkydtNVgpYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIe 1398
|
250 260 270
....*....|....*....|....*....|....*.
gi 951434962 171 KAILTAKQQGTMVIFS-THNMDNVQKlSDYIVMLKH 205
Cdd:PTZ00265 1399 KTIVDIKDKADKTIITiAHRIASIKR-SDKIVVFNN 1433
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-196 |
2.06e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 26 SGQILSLIGQNGAGKSTTFHMILDFIKPDSGKILWsgkpLTPDAITAKVGYMPEERGLYPKEtiksqllyfaalhgmkka 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----IDGEDILEEVLDQLLLIIVGGKK------------------ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 106 eaiillddwmkrlnvvgkstdkiESLSKGNAQKVQLIACLMFKPQLLILDEPFSGLDPVNSELLIKAILT------AKQQ 179
Cdd:smart00382 59 -----------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrlllllKSEK 115
|
170
....*....|....*..
gi 951434962 180 GTMVIFSTHNMDNVQKL 196
Cdd:smart00382 116 NLTVILTTNDEKDLGPA 132
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-217 |
2.65e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 128 IESLSKGNAQKVQLIAclmfkpQ--------LLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVqKLSDY 199
Cdd:TIGR00630 486 AGTLSGGEAQRIRLAT------QigsgltgvLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTI-RAADY 558
|
90 100
....*....|....*....|....
gi 951434962 200 IVML-----KH-GQTVLKGTPTEI 217
Cdd:TIGR00630 559 VIDIgpgagEHgGEVVASGTPEEI 582
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-156 |
9.39e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.50 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 17 VSDLSFSLHSGQILSLIGQNGAGKSTTFHMILDfikpdsgkiLWS--GKPLTPDAiTAKVGYMPeERGLYPKETIKSQLL 94
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGE---------LWPvyGGRLTKPA-KGKLFYVP-QRPYMTLGTLRDQII 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951434962 95 YFAALHGMKKA-------EAIIL---LDDWMKRLNVVGKSTDKIESLSKGNAQKVQLiACLMF-KPQLLILDE 156
Cdd:TIGR00954 537 YPDSSEDMKRRglsdkdlEQILDnvqLTHILEREGGWSAVQDWMDVLSGGEKQRIAM-ARLFYhKPQFAILDE 608
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
128-201 |
3.01e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.39 E-value: 3.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951434962 128 IESLSKGNAQKVQLIACLMFKPQ--LLILDEPFSGLDPVNSELLIKAILTAKQQGTMVIFSTHNMDNVqKLSDYIV 201
Cdd:cd03270 135 APTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI-RAADHVI 209
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
141-196 |
9.06e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.33 E-value: 9.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 951434962 141 LIACLMFKPQLLILDEPFSGLDPVNSELLIKAIL-TAKQQGTMVIFSTHN---MDNVQKL 196
Cdd:COG1106 216 ALLDALAKGGVLLIDEIEASLHPSLLRKLLKLFLdLANKNNAQLIFTTHStelLDAFLEL 275
|
|
| |
