|
Name |
Accession |
Description |
Interval |
E-value |
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-299 |
8.69e-164 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 456.88 E-value: 8.69e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEER 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:COG4152 81 GLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 161 DPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYLDSHLTKQELEAFA 240
Cdd:COG4152 161 DPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAGWLRALP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 241 GVhTVTQKEDGSFDITLEDPAAGQEIFVQATKDGYIPMFNQQPPTLEEIFKWKAGAVNE 299
Cdd:COG4152 241 GV-TVVEEDGDGAELKLEDGADAQELLRALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-211 |
9.39e-107 |
|
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: 309.21 E-value: 9.39e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEERG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03269 161 PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-237 |
3.70e-87 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 260.38 E-value: 3.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT---IGYLPE 78
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 159 GLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESfgrsklYLDS---HLTKQE 235
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR------LLEDvflELTGEE 234
|
..
gi 498433885 236 LE 237
Cdd:COG1131 235 AR 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-226 |
3.46e-84 |
|
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: 252.86 E-value: 3.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY---NTIGYLP 77
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRearRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 158 SGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLY 226
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLE 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-206 |
4.62e-63 |
|
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: 196.46 E-value: 4.62e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT---IGYLPE 78
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLlffaslrgkskqeiapkidewmekfqvkgkktdkvkSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498433885 159 GLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
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 ... |
1-211 |
5.29e-59 |
|
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: 187.96 E-value: 5.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT---I 73
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEArrrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-217 |
1.04e-50 |
|
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: 166.53 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGS--YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDYNTIGYL 76
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEP 156
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 157 FSGLDPVNAELLKNGIIELKeKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIR 217
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-211 |
1.10e-50 |
|
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: 166.21 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGkILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSG---KDYNTIGYLPE 78
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKqpqKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 159 GLDPVNAELLKNGIIELKEkGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03264 160 GLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-290 |
3.89e-49 |
|
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: 165.26 E-value: 3.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 9 KSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVlwdghTLSGKDY--------NTIGYLPEER 80
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTA-----RVAGYDVvreprkvrRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 161 DPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYLDSHLTKQ-ELEAF 239
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSlKVEVS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 240 AGVHTVTQKEDGSFDITL----------EDPAAGQEIFVQATKDGY-IPMFNQQPPTLEEIF 290
Cdd:TIGR01188 236 MLIAELGETGLGLLAVTVdsdrikilvpDGDETVPEIVEAAIRNGIrIRSISTERPSLDDVF 297
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-211 |
6.12e-49 |
|
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: 161.62 E-value: 6.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG--HTLSGKDYNTIGYLPEE 79
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFFASLRGKSKQEIapkiDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498433885 160 LDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03268 157 LDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-217 |
1.51e-48 |
|
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: 161.45 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDyntigylPEER- 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-------PHEIa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 -----------GLYPKVTI-ENQLL---------FFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQ 139
Cdd:cd03219 74 rlgigrtfqipRLFPELTVlENVMVaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 140 LISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIR 217
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-232 |
3.37e-48 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 160.90 E-value: 3.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGYL 76
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHErarlgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFFASLRGK-SKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 156 PFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYLDSHLT 232
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQFR 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-216 |
1.21e-46 |
|
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: 156.34 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTI----GYL 76
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEerglYPkvtiENQLlFFASLR----------GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIH 146
Cdd:COG1122 81 FQ----NP----DDQL-FAPTVEedvafgpenlGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 147 EPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
2.55e-46 |
|
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: 155.78 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGYL 76
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEP 156
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 157 FSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYL 227
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYL 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-226 |
1.49e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.09 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsGKDYNTIGYLPEER 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-RRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 ----------------GLYPKvtienqLLFFASLRGKSKQeiapKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTL 144
Cdd:COG1121 85 evdwdfpitvrdvvlmGRYGR------RGLFRRPSRADRE----AVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 145 IHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLrNGETVLNGKVHEIRESFGRSK 224
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSR 233
|
..
gi 498433885 225 LY 226
Cdd:COG1121 234 AY 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-217 |
1.43e-44 |
|
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: 152.12 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDyntigylPEER 80
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-------PHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 ---G---------LYPKVT-IENQLL---------FFASLRG-----KSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKG 133
Cdd:COG0411 77 arlGiartfqnprLFPELTvLENVLVaaharlgrgLLAALLRlprarREEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 134 NQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELK-EKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGK 212
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
....*
gi 498433885 213 VHEIR 217
Cdd:COG0411 237 PAEVR 241
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-215 |
5.59e-44 |
|
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: 149.47 E-value: 5.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEERG 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 LYPKVTIENQLLFFASLRGKSKQEIapkiDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHE 215
Cdd:TIGR03740 157 PIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-214 |
2.47e-43 |
|
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: 147.29 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsGKDYNTIGYLPEERGL 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-EKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 83 ---YPkVTIEN--------QLLFFASLRGKSKQeiapKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLV 151
Cdd:cd03235 80 drdFP-ISVRDvvlmglygHKGLFRRLSKADKA----KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 152 ILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMlrngetvLNGKVH 214
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLL-------LNRTVV 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-227 |
9.36e-43 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 146.71 E-value: 9.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLS----------Gkdy 70
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmhkrarlG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 ntIGYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKL 150
Cdd:COG1137 80 --IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 151 VILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYL 227
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYL 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-218 |
1.05e-42 |
|
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: 146.04 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGYL 76
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFFASLRGKSKqeIAPKIDEWMEKFQV-KGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAK--RKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 156 PFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-206 |
1.43e-42 |
|
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: 145.30 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFGSY--KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD----YNTIGYL 76
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 ---PEERGLYPkvTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:cd03225 81 fqnPDDQFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-206 |
2.76e-42 |
|
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: 142.77 E-value: 2.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY----NTIGYLPE 78
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeelrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 erglypkvtienqllffaslrgkskqeiapkidewmekfqvkgkktdkvksLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498433885 159 GLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
1-226 |
7.50e-42 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 144.36 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLS---GKDYNTIGYLP 77
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRrapRAALARLGVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:TIGR03864 81 QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 158 SGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKiCDHLIMLRNGETVLNGKVHEIRESFGRSKLY 226
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALaRDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLADGAAAELRGATGGADLE 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-187 |
5.17e-41 |
|
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: 141.08 E-value: 5.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD---YNTIGYLP 77
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EERGLYPKVTIENQLLFFASLRGKSKQEIApkIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|
gi 498433885 158 SGLDPVNAELLKNGIIELKEKGSCVIFSSH 187
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
7.99e-41 |
|
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: 148.13 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSY-----KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD------ 69
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 70 -YNTIGYL---PeERGLYPKVTIENQLLFFASLRGK-SKQEIAPKIDEWMEKFQVKGKKTDK-VKSLSKGNQQKVQLIST 143
Cdd:COG1123 340 lRRRVQMVfqdP-YSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNA----ELLKngiiELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQaqilNLLR----DLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-219 |
5.25e-40 |
|
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: 139.73 E-value: 5.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDYNT----I 73
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQditGLSEKELYElrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTI-ENqLLFFasLR---GKSKQEIAPKIDEWMEKFQVKGKKtDKVKS-LSKGNQQKVQLISTLIHEP 148
Cdd:COG1127 85 GMLFQGGALFDSLTVfEN-VAFP--LRehtDLSEAEIRELVLEKLELVGLPGAA-DKMPSeLSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 149 KLVILDEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-219 |
6.22e-40 |
|
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: 139.17 E-value: 6.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDY----NTIG 74
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisGLSEAELyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 YLPEERGLYPKVTI-ENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:cd03261 81 MLFQSGALFDSLTVfENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELK-EKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
6.63e-40 |
|
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: 139.79 E-value: 6.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDY-NTIGYL 76
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlASLSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEER--------------GLYPkvtienqllFFASLRGKSKQEIApKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLIS 142
Cdd:COG1120 81 PQEPpapfgltvrelvalGRYP---------HLGLFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 143 TLIHEPKLVILDEPFSGLDPVNA----ELLKngiiEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQlevlELLR----RLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-227 |
6.24e-39 |
|
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: 136.65 E-value: 6.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGY 75
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVTI-ENQLLffASLRGKSKQEIAPKIDEWMEKFQV-KGKKTDKVKSLSKGNQQkvQL-IS-TLIHEPKLV 151
Cdd:COG0410 83 VPEGRRIFPSLTVeENLLL--GAYARRDRAEVRADLERVYELFPRlKERRRQRAGTLSGGEQQ--MLaIGrALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 152 ILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYL 227
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-206 |
1.24e-38 |
|
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: 134.24 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT------IGY 75
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrrIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVTIENQLLFfaslrgkskqeiapkidewmekfqvkgkktdkvkSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 156 PFSGLDPvnaeLLKNGIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:cd03229 127 PTSALDP----ITRREVRALlkslqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-218 |
3.16e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 135.60 E-value: 3.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDyNTIGYL 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-PDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYP-KVTIENqLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:COG1116 86 FQEPALLPwLTVLDN-VALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 156 PFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDnvEKI--CDHLIMLRNGetvlNGKVHEIRE 218
Cdd:COG1116 165 PFGALDALTRERLQDELLRLwQETGKTVLFVTHDVD--EAVflADRVVVLSAR----PGRIVEEID 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-211 |
1.64e-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: 132.26 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSG--KDYNTIGYLPEE 79
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvpPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 160 LDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03259 161 LDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-217 |
1.91e-37 |
|
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: 132.49 E-value: 1.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTL---SGKDYNTIGYLPE 78
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrePREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 159 GLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIR 217
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-206 |
2.67e-37 |
|
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: 131.84 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGS----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY------- 70
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 -NTIGYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPK 149
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 150 LVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDnVEKICDHLIMLRNGE 206
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPE-LAEYADRIIELRDGK 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-227 |
3.74e-37 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 132.32 E-value: 3.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLS-----GKDYNTIGYL 76
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFFASLRGK-SKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 156 PFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYL 227
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-204 |
9.38e-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: 130.67 E-value: 9.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGS----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNtIGYLP 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-RGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 158 SGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDnvEKI--CDHLIMLRN 204
Cdd:cd03293 160 SALDALTREQLQEELLDIwRETGKTVLLVTHDID--EAVflADRVVVLSA 207
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-216 |
9.51e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 131.33 E-value: 9.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDYN----T 72
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtALRGRALRrlrrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 IGYLPEERGLYPKVT-IENQLL-------FFASLRGK-SKQEIApKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLIST 143
Cdd:COG3638 82 IGMIFQQFNLVPRLSvLTNVLAgrlgrtsTWRSLLGLfPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELlkngIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQ----VMDLlrriaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
9.59e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.01 E-value: 9.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT---IGYLPE 78
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHArqrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 159 GLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-216 |
1.28e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 136.30 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGY 75
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaqaagIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVTI-ENqlLFFASLRGK----SKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKL 150
Cdd:COG1129 84 IHQELNLVPNLSVaEN--IFLGREPRRggliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 151 VILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-208 |
3.81e-36 |
|
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: 129.16 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY------ 70
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 -NTIGYLPEE--RGLYPKVTIENQLLffASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKS-----LSKGNQQKVQLIS 142
Cdd:cd03257 81 rKEIQMVFQDpmSSLNPRMTIGEQIA--EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNrypheLSGGQRQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 143 TLIHEPKLVILDEPFSGLDPVnaelLKNGIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVS----VQAQILDLlkklqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-216 |
7.22e-36 |
|
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: 128.96 E-value: 7.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD----YNTIGYL 76
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpvelRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEW-----MEKFQVKGKKTDKvksLSKGNQQKVQLISTLIHEPKLV 151
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlalvgLDPAEFADRYPHE---LSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 152 ILDEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-216 |
1.13e-35 |
|
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: 128.45 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYK-ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDYNT----I 73
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdiNKLKGKALRQlrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVT-IENQLL-------FFASLRGK-SKQEIaPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTL 144
Cdd:cd03256 81 GMIFQQFNLIERLSvLENVLSgrlgrrsTWRSLFGLfPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 145 IHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
1.21e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.04 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGhtlsgKDYNT--------I 73
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-----RDLFTnlpprerrV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 154 DEPFSGLDP-VNAELLKNgIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG1118 158 DEPFGALDAkVRKELRRW-LRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-211 |
1.27e-35 |
|
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: 126.40 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDY-NTIGYLPe 78
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlASLSPKELaRKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 erglypkvtienQLlffaslrgkskqeiapkidewMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03214 80 ------------QA---------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 159 GLDPVNA----ELLKNgiiELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03214 127 HLDIAHQiellELLRR---LARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
1.40e-35 |
|
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: 133.88 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF--GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKD---SGSVLWDGHTLSGKDY----N 71
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEalrgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 72 TIGYLPEE--RGLYPkVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPK 149
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 150 LVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-208 |
4.29e-35 |
|
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: 124.46 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkdyntigylpeerg 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 lypkvtienqllfFASLRGKSKQEIAPkidewmekfqvkgkktdkVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:cd03216 66 -------------FASPRDARRAGIAM------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-259 |
1.19e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 127.90 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYK---------------------ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVL 59
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 60 WDGHTlsgkdyntigylP--EERGLYPKVTI----ENQLLF-------FASLR---GKSKQEIAPKIDEWMEKFQVKGKK 123
Cdd:COG4586 81 VLGYV------------PfkRRKEFARRIGVvfgqRSQLWWdlpaidsFRLLKaiyRIPDAEYKKRLDELVELLDLGELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 124 TDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIML 202
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVI 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 203 RNGETVLNGKVHEIRESFGRSK---LYLDSHLTKQELEAFAgvhTVTQKEDGSFDITLED 259
Cdd:COG4586 229 DHGRIIYDGSLEELKERFGPYKtivLELAEPVPPLELPRGG---EVIEREGNRVRLEVDP 285
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-208 |
3.61e-34 |
|
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: 123.52 E-value: 3.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFG-SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD-YNTIGYLPEE- 79
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKErRKSIGYVMQDv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 -RGLYpKVTIENQLLFFASLRGKSKQeiapKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03226 81 dYQLF-TDSVREELLLGLKELDAGNE----QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 159 GLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:cd03226 156 GLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-290 |
4.04e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 126.87 E-value: 4.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 7 LSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGK---DYNTIGYLPEERGLY 83
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARarlARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 PKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPV 163
Cdd:PRK13536 127 LEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 164 NAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIresfgrsklyLDSHLTKQELEAFAG-- 241
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL----------IDEHIGCQVIEIYGGdp 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 242 --VHTVTQKEDGSFDITLE-------DPAAgqeifVQATKDGYIPM-FNQQPPTLEEIF 290
Cdd:PRK13536 277 heLSSLVKPYARRIEVSGEtlfcyapDPEQ-----VRVQLRGRAGLrLLQRPPNLEDVF 330
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-162 |
1.09e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.98 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKdyntigyLPEER 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-------PPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 G---------LYPKVTI-ENqLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKL 150
Cdd:COG3842 78 NvgmvfqdyaLFPHLTVaEN-VAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170
....*....|..
gi 498433885 151 VILDEPFSGLDP 162
Cdd:COG3842 157 LLLDEPLSALDA 168
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-231 |
4.71e-33 |
|
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: 122.56 E-value: 4.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEERGL---YP-----KV 86
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLvfqFPehqlfEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 87 TIENQLLFFASLRGKSKQEIAPKIDEWMEKfqVKGKKTDKVKS---LSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPV 163
Cdd:TIGR04521 99 TVYKDIAFGPKNLGLSEEEAEERVKEALEL--VGLDEEYLERSpfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 164 NAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIresFGRSKLYLDSHL 231
Cdd:TIGR04521 177 GRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV---FSDVDELEKIGL 242
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-158 |
7.68e-33 |
|
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: 118.13 E-value: 7.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY----NTIGYLPEERGLYPKVTIENQL 92
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkslrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 93 LFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKV----KSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-218 |
7.78e-33 |
|
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: 120.87 E-value: 7.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS-YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHT---LSGKDYNT---- 72
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitkLRGKKLRKlrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 IGYLPEERGLYPKVT-IENQLL-------FFASLRG---KSKQEIAPKIdewMEKFQVKGKKTDKVKSLSKGNQQKVQLI 141
Cdd:TIGR02315 81 IGMIFQHYNLIERLTvLENVLHgrlgykpTWRSLLGrfsEEDKERALSA---LERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 142 STLIHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
1.09e-32 |
|
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: 119.98 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLI-----LDFLSKDSGSVLWDGHTLSGKDYN----- 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 72 -TIGYLPEERGLYPKvTIENQLLFFASLRGKSKQEIAPKIDEW-MEKFQVKGKKTDKVK--SLSKGNQQKVQLISTLIHE 147
Cdd:cd03260 81 rRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEaLRKAALWDEVKDRLHalGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 148 PKLVILDEPFSGLDPVNAELLKNGIIELKEKGScVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYT-IVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-211 |
6.94e-32 |
|
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: 118.20 E-value: 6.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVlwdghtlsgkdyNTIGYLPEER--GLYPKVTI----E 89
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV------------RVAGLVPWKRrkKFLRRIGVvfgqK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQL----------LFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:cd03267 104 TQLwwdlpvidsfYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 160 LDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03267 184 LDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-218 |
2.87e-31 |
|
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: 116.57 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLwdghtLSGKDYNTIGylPEERG 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL-----LDGKDITNLP--PHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 ---------LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:cd03300 74 vntvfqnyaLFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 153 LDEPFSGLDpvnAELLKNGIIELK----EKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:cd03300 154 LDEPLGALD---LKLRKDMQLELKrlqkELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-216 |
8.96e-31 |
|
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: 115.37 E-value: 8.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIlDFLSK-DSGSVLWDGH---TLSGKDYNT 72
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLERpTSGSVLVDGTdltLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 ----IGYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEP 148
Cdd:cd03258 80 arrrIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 149 KLVILDEPFSGLDPVNAEllknGIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:cd03258 160 KVLLCDEATSALDPETTQ----SILALlrdinRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-216 |
8.99e-31 |
|
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: 115.51 E-value: 8.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKaLDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH--TLSGKDYNTIGYLPEE 79
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKdiTNLPPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 160 LDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:cd03299 160 LDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-208 |
9.47e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 114.76 E-value: 9.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDYN----T 72
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsRLKRREIPylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 IGYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 153 LDEPFSGLDPVNA----ELLKngiiELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:COG2884 161 ADEPTGNLDPETSweimELLE----EINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-208 |
2.42e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 119.36 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGY 75
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaialgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVT-IENQLLFFASLRGK--SKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:COG3845 85 VHQHFMLVPNLTvAENIVLGLEPTKGGrlDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 153 LDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:COG3845 165 LDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-205 |
2.74e-30 |
|
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: 113.50 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDghtlsGKDYNTIGylPEERG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-----GRDVTDLP--PKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 ---------LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:cd03301 74 iamvfqnyaLYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 153 LDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-216 |
1.57e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYK----------------------ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSV 58
Cdd:COG1134 4 MIEVENVSKSYRLYHepsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 59 LWDGHT-----LSGkdyntigylpeerGLYPKVT-IENqLLFFASLRGKSKQEIAPKIDEwMEKFQVKGKKTD-KVKSLS 131
Cdd:COG1134 84 EVNGRVsalleLGA-------------GFHPELTgREN-IYLNGRLLGLSRKEIDEKFDE-IVEFAELGDFIDqPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 132 KGnqQKVQL---ISTLIhEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:COG1134 149 SG--MRARLafaVATAV-DPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
....*...
gi 498433885 209 LNGKVHEI 216
Cdd:COG1134 226 MDGDPEEV 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-206 |
1.90e-28 |
|
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: 107.47 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD----YNTIGYLPEERGLYPKvTIEN 90
Cdd:cd03228 16 PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDleslRKNIAYVPQDPFLFSG-TIRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLlffaslrgkskqeiapkidewmekfqvkgkktdkvksLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKN 170
Cdd:cd03228 95 NI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILE 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 498433885 171 GIIELKeKGSCVIFSSHNMDNVEKiCDHLIMLRNGE 206
Cdd:cd03228 138 ALRALA-KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-216 |
2.00e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.52 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNtIGYLPEERGL---YPKV----- 86
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLvfqYPEYqlfee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 87 TIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKgKKTDKVKS---LSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPV 163
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLD-YEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 164 NAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13637 179 GRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-227 |
2.08e-28 |
|
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: 115.11 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 4 VEKLSKSFGSY--KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLwdghtLSGKDYNT--------I 73
Cdd:TIGR01257 931 VKNLVKIFEPSgrPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL-----VGGKDIETnldavrqsL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELKEkGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGrSKLYL 227
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFG-TGFYL 1157
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-213 |
3.03e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 109.05 E-value: 3.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGylpeER 80
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIA----RL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GL---------YPKVTI-ENQLL-------FFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLIST 143
Cdd:COG4674 86 GIgrkfqkptvFEELTVfENLELalkgdrgVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGML 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 144 LIHEPKLVILDEPFSGLDPV----NAELLKngiiELKEKGScVIFSSHNMDNVEKICDHLimlrngeTVLN-GKV 213
Cdd:COG4674 166 LAQDPKLLLLDEPVAGMTDAeterTAELLK----SLAGKHS-VVVVEHDMEFVRQIARKV-------TVLHqGSV 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-206 |
4.35e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWdGHTLsgkdynTIGYLPEER 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------KIGYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 -GLYPKVTIENQLlffaslrgkskQEIAPKIDE-----WMEKFQVKGKKTDK-VKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:COG0488 388 eELDPDKTVLDEL-----------RDGAPGGTEqevrgYLGRFLFSGDDAFKpVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELkeKGsCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-208 |
5.69e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.42 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSfgsyKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGY 75
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEER---GLYPKVTI-ENqlLFFASLRGKSK---------QEIApkiDEWMEKFQVK-GKKTDKVKSLSKGNQQKVQLI 141
Cdd:COG1129 332 VPEDRkgeGLVLDLSIrEN--ITLASLDRLSRgglldrrreRALA---EEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 142 STLIHEPKLVILDEPFSGLDpVNAellKNGII----ELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:COG1129 407 KWLATDPKVLILDEPTRGID-VGA---KAEIYrlirELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-216 |
1.46e-27 |
|
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: 111.43 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVL------W-----DGHT 64
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdeWvdmtkPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 65 LSGKDYNTIGYLPEERGLYPKVTIENQLLFFASLR-----GKSKQEIAPKIDEWMEKF--QVKGKKTDKvksLSKGNQQK 137
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLElpdelARMKAVITLKMVGFDEEKaeEILDKYPDE---LSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 138 VQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-216 |
1.22e-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: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKalddMTF--TIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG--HTlsgkdyntiGYL 76
Cdd:COG3840 1 MLRLDDLTYRYGDFP----LRFdlTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdLT---------ALP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERglypKVTI---ENQLlfFASL------------RGK-SKQEIApKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQL 140
Cdd:COG3840 68 PAER----PVSMlfqENNL--FPHLtvaqniglglrpGLKlTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 141 ISTLIHEPKLVILDEPFSGLDPVnaelLKNGIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHE 215
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDPA----LRQEMLDLvdelcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
.
gi 498433885 216 I 216
Cdd:COG3840 217 L 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
1.43e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 104.71 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDY-NTIGYL 76
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpisMLSSRQLaRRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERgLYPKVTIENQLLFFA-----SLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLV 151
Cdd:PRK11231 82 PQHH-LTPEGITVRELVAYGrspwlSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 152 ILDEPFSGLDpVN--AELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK11231 161 LLDEPTTYLD-INhqVELMRL-MRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-233 |
1.84e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.09 E-value: 1.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsgkDYNTIGYL---- 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGLLalrq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 --------PEERGLYpkVTIENQLLFfaSLR--GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIH 146
Cdd:PRK13638 78 qvatvfqdPEQQIFY--TDIDSDIAF--SLRnlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 147 EPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIresFGRSKLY 226
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV---FACTEAM 230
|
....*..
gi 498433885 227 LDSHLTK 233
Cdd:PRK13638 231 EQAGLTQ 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-205 |
2.77e-26 |
|
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: 103.57 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYN--TIGYLPEE 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQerNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFfaSLRGK------SKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:cd03296 83 YALFRHMTVFDNVAF--GLRVKprserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-216 |
5.68e-26 |
|
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: 102.86 E-value: 5.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLwdghTLSGKDYNT-------- 72
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFGERRGGedvwelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 -IGYL-PE-ERGLYPKVTIENQLL--FFASL---RGKSKQEIApKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTL 144
Cdd:COG1119 79 rIGLVsPAlQLRFPRDETVLDVVLsgFFDSIglyREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 145 IHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSC-VIFSSHnmdNVEKI--C-DHLIMLRNGETVLNGKVHEI 216
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPtLVLVTH---HVEEIppGiTHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-208 |
6.02e-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: 101.99 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIE---DGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTL--SGKDYNT------IGYLPEERGLY 83
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKINLppqqrkIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 PKVTIENQLLFfaSLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPV 163
Cdd:cd03297 88 PHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498433885 164 NAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-206 |
6.24e-26 |
|
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: 102.10 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEER 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 G-------LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:cd03292 81 GvvfqdfrLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 154 DEPFSGLDPVNAellkNGIIELKEK----GSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:cd03292 161 DEPTGNLDPDTT----WEIMNLLKKinkaGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-219 |
6.35e-26 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 107.15 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD----YNTIGYLPEERGLyPKVTIENQ 91
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDpaswRRQIAWVPQNPYL-FAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 92 LLFFAslRGKSKQEI-----APKIDEWMEKFQvKGKKT---DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPV 163
Cdd:COG4988 431 LRLGR--PDASDEELeaaleAAGLDEFVAALP-DGLDTplgEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 164 NAELLKNGIIELKeKGSCVIFSSHNMDNVeKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:COG4988 508 TEAEILQALRRLA-KGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-221 |
7.42e-26 |
|
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: 107.79 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFG--SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVlwdghTLSGKD--------Y 70
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDA-----TVAGKSiltnisdvH 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 NTIGYLPEERGLYPKVTIENQLLFFASLRGKSKQEIApKIDEWMEKFQVKGKKTDKVK-SLSKGNQQKVQLISTLIHEPK 149
Cdd:TIGR01257 2012 QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIE-KVANWSIQSLGLSLYADRLAgTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 150 LVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFG 221
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-227 |
1.07e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 102.38 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEER 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 G-----LYPKVT-IENQLL---------FFASL------RgKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQ 139
Cdd:PRK11300 85 TfqhvrLFREMTvIENLLVaqhqqlktgLFSGLlktpafR-RAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 140 LISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELK-EKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
....*....
gi 498433885 219 SFGRSKLYL 227
Cdd:PRK11300 244 NPDVIKAYL 252
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-206 |
2.42e-25 |
|
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: 100.30 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT------IGY 75
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVTI-ENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILD 154
Cdd:cd03262 81 VFQQFNLFPHLTVlENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 155 EPFSGLDPvnaELLK---NGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:cd03262 161 EPTSALDP---ELVGevlDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-218 |
2.85e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 103.49 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSG-----KDYNTI--G 74
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaenRHVNTVfqS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 YlpeerGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILD 154
Cdd:PRK09452 95 Y-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 155 EPFSGLDpvnAELLKNGIIELK----EKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:PRK09452 170 ESLSALD---YKLRKQMQNELKalqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-217 |
3.16e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.75 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLS----GKDYNTIGYL 76
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArltpAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 -PEERGLYPKVTIENQLLFfaslRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:PRK15439 91 vPQEPLLFPNLSVKENILF----GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 156 PFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIR 217
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
15-190 |
4.42e-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: 99.03 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsgkDYNTIGYL------------PEERGL 82
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL---DYSRKGLLerrqrvglvfqdPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 83 YPKVtieNQLLFFASLR-GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:TIGR01166 83 AADV---DQDVAFGPLNlGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180
....*....|....*....|....*....
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIFSSHNMD 190
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-209 |
5.69e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 99.95 E-value: 5.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkDYNT-------I 73
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT--DWQTakimreaV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQLL---FFASlrgksKQEIAPKIDEWMEKF-QVKGKKTDKVKSLSKGNQQKVQLISTLIHEPK 149
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAmggFFAE-----RDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 150 LVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVL 209
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVL 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-206 |
1.17e-24 |
|
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: 97.50 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSfgsyKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGY 75
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDairagIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEER---GLYPKVTI-ENqlLFFASLrgkskqeiapkidewmekfqvkgkktdkvksLSKGNQQKVQLISTLIHEPKLV 151
Cdd:cd03215 80 VPEDRkreGLVLDLSVaEN--IALSSL-------------------------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 152 ILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-218 |
2.23e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 102.39 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH--TLSG-KDYNT--IGY 75
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevTFNGpKSSQEagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVTI-ENQLL---FFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLV 151
Cdd:PRK10762 84 IHQELNLIPQLTIaENIFLgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 152 ILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTE 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-197 |
2.73e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.90 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 7 LSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT---IGYLPEERGLY 83
Cdd:NF033858 272 LTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATrrrVGYMSQAFSLY 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 PKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPV 163
Cdd:NF033858 352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498433885 164 nA-----ELLkngiIELKEKGSCVIF-SSHNMDNVEKiCD 197
Cdd:NF033858 432 -ArdmfwRLL----IELSREDGVTIFiSTHFMNEAER-CD 465
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-211 |
3.34e-24 |
|
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: 97.18 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 6 KLSKSFGSYKALDdMTF--TIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG--HTLSGKDYNTIGYLPEERG 81
Cdd:cd03298 2 RLDKIRFSYGEQP-MHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvdVTAAPPADRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:cd03298 81 LFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 162 PVnaelLKNGIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03298 161 PA----LRAEMLDLvldlhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-218 |
4.11e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.29 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSG-KDYN-TIGYLPE 78
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQrPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 159 GLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
14-211 |
4.76e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 4.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 14 YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGhtlsgkdynTIGYLPEER-GLYPKVTIENQL 92
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------RVSSLLGLGgGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 93 LFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGnqQKVQL---ISTLIhEPKLVILDEPFSGLDPVNAELLK 169
Cdd:cd03220 106 YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSG--MKARLafaIATAL-EPDILLIDEVLAVGDAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498433885 170 NGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03220 183 RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
7.93e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.00 E-value: 7.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIlDFLSK-DSGSVLWDGH---TLSGKDynt 72
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLLERpTSGSVLVDGVdltALSERE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 igyLPEER----------GLYPKVTI-ENQLLffaSLR--GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQ 139
Cdd:COG1135 77 ---LRAARrkigmifqhfNLLSSRTVaENVAL---PLEiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 140 LISTLIHEPKLVILDEPFSGLDPVNA----ELLKngiiELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVH 214
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTrsilDLLK----DINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
250 260
....*....|....*....|
gi 498433885 215 EIresFGRSKlyldSHLTKQ 234
Cdd:COG1135 227 DV---FANPQ----SELTRR 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-211 |
1.66e-23 |
|
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: 94.93 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKA-LDDMTFTIEDGKILGLIGQNGAGKTTtfrlILDFLS------KDSGSVLWDGHTLSGKDY-NTI 73
Cdd:cd03213 9 LTVTVKSSPSKSGKQlLKNVSGKAKPGELTAIMGPSGAGKST----LLNALAgrrtglGVSGEVLINGRPLDKRSFrKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQLLFFASLRGkskqeiapkidewmekfqvkgkktdkvksLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHN-MDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
4.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.91 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsgkDYN-------- 71
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI---KYDkksllevr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 72 -TIGYL---PEERGLYPkvTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHE 147
Cdd:PRK13639 78 kTVGIVfqnPDDQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 148 PKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-216 |
5.69e-23 |
|
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: 95.40 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 5 EKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDY-----NTIGYL 76
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELrelrrKKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEP 156
Cdd:cd03294 108 FQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 157 FSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:cd03294 188 FSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-208 |
6.05e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.08 E-value: 6.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTtfrlILDFLS------KDSGSVLWDGHTLSGK-----D 69
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKST----LMKVLSgvyphgTYEGEIIFEGEELQASnirdtE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 70 YNTIGYLPEERGLYPKVTI-ENqlLFFASlrgkskqEIAP-----------KIDEWMEKFQVKGKKTDKVKSLSKGNQQK 137
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVlEN--IFLGN-------EITPggimdydamylRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 138 VQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-222 |
6.10e-23 |
|
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: 98.75 E-value: 6.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFG--SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT----IGY 75
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEErglypkvtienQLLFFASLR--------GKSKQEI--APK---IDEWMEKFQvKGKKT---DKVKSLSKGNQQKVQ 139
Cdd:COG2274 554 VLQD-----------VFLFSGTIRenitlgdpDATDEEIieAARlagLHDFIEALP-MGYDTvvgEGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 140 LISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKeKGSCVIFSSHNMDNVeKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLAR 699
|
...
gi 498433885 220 FGR 222
Cdd:COG2274 700 KGL 702
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-209 |
6.44e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.15 E-value: 6.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS-----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLwdghtLSGKDyntIGY 75
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL-----IDGKD---VTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEER--------------GLYPKVTI-ENQLLffASLRGKSKQEIAPKIDEWMEKFQVKGKK---------TDKVKSLS 131
Cdd:COG1101 73 LPEYKrakyigrvfqdpmmGTAPSMTIeENLAL--AYRRGKRRGLRRGLTKKRRELFRELLATlglglenrlDTKVGLLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 132 KGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELlkngIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAAL----VLELtekivEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
...
gi 498433885 207 TVL 209
Cdd:COG1101 227 IIL 229
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-213 |
6.57e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.80 E-value: 6.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTlsgkdynTIGYLPEEr 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL-------RIGYVPQK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 gLYPKVTIENQLLFFASLR-GKSKQEIAPKidewMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:PRK09544 76 -LYLDTTLPLTVNRFLRLRpGTKKEDILPA----LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 160 LDpVNAEL-LKNGIIELKEKGSC-VIFSSHNMdnvekicdHLIMLRNGETV-LNGKV 213
Cdd:PRK09544 151 VD-VNGQVaLYDLIDQLRRELDCaVLMVSHDL--------HLVMAKTDEVLcLNHHI 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-268 |
1.33e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYL---- 76
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRvasv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIEN--------QLLFFAslRGKSKQEIApkIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEP 148
Cdd:PRK09536 83 PQDTSLSFEFDVRQvvemgrtpHRSRFD--TWTETDRAA--VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 149 KLVILDEPFSGLDpVN-----AELLKngiiELKEKGSCVIFSSHNMDNVEKICDHLIMLRngetvlNGKVHEIresfGRS 223
Cdd:PRK09536 159 PVLLLDEPTASLD-INhqvrtLELVR----RLVDDGKTAVAAIHDLDLAARYCDELVLLA------DGRVRAA----GPP 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 224 KlyldSHLTKQELEAFAGVHTV--TQKEDGSFDIT------LEDPAAGQEIFV 268
Cdd:PRK09536 224 A----DVLTADTLRAAFDARTAvgTDPATGAPTVTplpdpdRTEAAADTRVHV 272
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.78e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.53 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS-YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsgkDYNTIGYLPEE 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI---DYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFFASLR----------GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPK 149
Cdd:PRK13636 82 ESVGMVFQDPDNQLFSASVYqdvsfgavnlKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 150 LVILDEPFSGLDPVN-AELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13636 162 VLVLDEPTAGLDPMGvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.90e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.52 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYK--ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkdYNTIGYLPE 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGL--------YPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKL 150
Cdd:PRK13632 84 KIGIifqnpdnqFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 151 VILDEPFSGLDPVNAELLKNGIIELKEKGS-CVIFSSHNMDNVEKiCDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEI 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-208 |
6.46e-22 |
|
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: 95.28 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDS--GSVLWDGHTLSGKDYNT-----I 73
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDteragI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTI-ENqlLFFA---SLRGK--SKQEIAPKIDEWMEKFQVKGKK-TDKVKSLSKGNQQKVQLISTLIH 146
Cdd:TIGR02633 81 VIIHQELTLVPELSVaEN--IFLGneiTLPGGrmAYNAMYLRAKNLLRELQLDADNvTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 147 EPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
6.59e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYN----TIGY 75
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRevrkFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 L---PEERGLYPkvTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:PRK13652 83 VfqnPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 153 LDEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIresFGRSKLYLDSHL 231
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLLARVHL 237
|
.
gi 498433885 232 T 232
Cdd:PRK13652 238 D 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-206 |
6.63e-22 |
|
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: 89.97 E-value: 6.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKA--LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT----IGY 75
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVTIENqllffaslrgkskqeIapkidewmekfqvkgkktdkvksLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:cd03246 81 LPQDDELFSGSIAEN---------------I-----------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498433885 156 PFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMdNVEKICDHLIMLRNGE 206
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGR 172
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
7.93e-22 |
|
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: 95.25 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLI--LDFLSKDSGSVLWD------------------ 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 62 -----GHTLSGKDYNTIGYL-PEERGLYPKVTIENQLLFfaSLRG---------KSKQEIAPKIDEWM-------EKFQV 119
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNLSdKLRRRIRKRIAIMLQRTF--ALYGddtvldnvlEALEEIGYEGKEAVgravdliEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 120 KGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDH 198
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDK 238
|
250 260
....*....|....*....|..
gi 498433885 199 LIMLRNGETVLNGKVHEIRESF 220
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVF 260
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-216 |
1.15e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.31 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGK--DYNTI----G 74
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvDERLIrqeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 YLPEERGLYPKVT-IENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:PRK09493 81 MVFQQFYLFPHLTaLENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 154 DEPFSGLDP-VNAELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK09493 161 DEPTSALDPeLRHEVLKV-MQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-187 |
1.74e-21 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.86 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLS--GKDYNT----IG 74
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqRDEYHQdllyLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 YLPeerGLYPKVTIENQLLFFASLRGKSKQEIAPKIdewMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILD 154
Cdd:PRK13538 81 HQP---GIKTELTALENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|...
gi 498433885 155 EPFSGLDPVNAELLKNGIIELKEKGSCVIFSSH 187
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-211 |
1.78e-21 |
|
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: 90.41 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLI---LDFLSKDSGSVLWDGHTLSGKDY-NTIGYLPEERGLYPKVTIEN 90
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKPDQFqKCVAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLLFFASLRG--KSKQEIAPKIDEWMEKFQVKGKKT--DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAE 166
Cdd:cd03234 101 TLTYTAILRLprKSSDAIRKKRVEDVLLRDLALTRIggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498433885 167 LLKNGIIELKEKGSCVIFSSHN-MDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03234 181 NLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-211 |
3.63e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.22 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkdyntiGYLPEE- 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA-------DWSPAEl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 ---RGLYPKVTienQLLF-F---------ASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQL------ 140
Cdd:PRK13548 75 arrRAVLPQHS---SLSFpFtveevvamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLarvlaq 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 141 ISTLIHEPKLVILDEPFSGLDPVN----AELLKNgiieL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:PRK13548 152 LWEPDGPPRWLLLDEPTSALDLAHqhhvLRLARQ----LaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-237 |
4.98e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 14 YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSG--KDYNTIGYLPEERGL---YPKV-- 86
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLRKEIGLvfqFPEYql 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 87 ---TIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVK-SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDP 162
Cdd:PRK13645 104 fqeTIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 163 VNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIresFGRSKLyldshLTKQELE 237
Cdd:PRK13645 184 KGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI---FSNQEL-----LTKIEID 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-206 |
5.11e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLS-KSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGY 75
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErrrlgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEER---GLYPKVTI-ENQLL------FFAS---LRGKSKQEIApkiDEWMEKFQVKGKKTD-KVKSLSKGNQQKVQLI 141
Cdd:COG3845 338 IPEDRlgrGLVPDMSVaENLILgryrrpPFSRggfLDRKAIRAFA---EELIEEFDVRTPGPDtPARSLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 142 STLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-206 |
5.17e-21 |
|
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: 86.73 E-value: 5.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTlsgkdynTIGYLPEerg 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------KIGYFEQ--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 lypkvtienqllffaslrgkskqeiapkidewmekfqvkgkktdkvksLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498433885 162 PVNAELLKNGiieLKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:cd03221 103 LESIEALEEA---LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-216 |
5.50e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.45 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLI-----LDFLSKDSGSVLWDGHTLSGKDYNT--- 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSPRTDTvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 ---IGYLPEERGLYPKVTIENqLLFFASLRG-KSKQeiapKIDEWMEKF--------QVKGKKTDKVKSLSKGNQQKVQL 140
Cdd:PRK14239 85 rkeIGMVFQQPNPFPMSIYEN-VVYGLRLKGiKDKQ----VLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 141 ISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFsSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLV-TRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
5.80e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVlwdghTLSGKDYNTIGY-LPEE 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----TINNINYNKLDHkLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGL---YPKVTIENQLLFFASL---RGKSKQEIAPKIDEWMEKFQVK-------GKKTD---KVKSLSKGNQQKVQLIST 143
Cdd:PRK09700 80 LGIgiiYQELSVIDELTVLENLyigRHLTKKVCGVNIIDWREMRVRAammllrvGLKVDldeKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-222 |
6.37e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 6.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTiGYLPEER 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-GVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 161 DPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGEtvlnGKVHE-IRESFGR 222
Cdd:PRK11248 160 DAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPGP----GRVVErLPLNFAR 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-219 |
2.33e-20 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 87.36 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIlDFLSK-DSGSVLWDGHTLSGKDYN------TI 73
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLEEpDSGTITVDGEDLTDSKKDinklrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVT-IENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:COG1126 80 GMVFQQFNLFPHLTvLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 153 LDEPFSGLDPVN-AELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:COG1126 160 FDEPTSALDPELvGEVLDV-MRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-216 |
4.26e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLwdghtLSGKDYNTIGYLPEE 79
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-----VSGIDTGDFSKLQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKV-----------TIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEP 148
Cdd:PRK13644 76 RKLVGIVfqnpetqfvgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 149 KLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEkICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENV 222
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-222 |
9.69e-20 |
|
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: 89.05 E-value: 9.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSF--GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKD-YNTIGY 75
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrDLDEDDlRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEErglyPKV---TIENQLL----------------------FFASLRGKskqeiapkIDEWMEkfqvkgkktDKVKSL 130
Cdd:COG4987 414 VPQR----PHLfdtTLRENLRlarpdatdeelwaalervglgdWLAALPDG--------LDTWLG---------EGGRRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 131 SKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELkEKGSCVIFSSHNMDNVEKiCDHLIMLRNGETVLN 210
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQ 550
|
250
....*....|..
gi 498433885 211 GKVHEIRESFGR 222
Cdd:COG4987 551 GTHEELLAQNGR 562
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-221 |
1.25e-19 |
|
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: 85.35 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDY-NTIGYLPEERGLYPKVTIENq 91
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidiRDISRKSLrSMIGVVLQDTFLFSGTIMEN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 92 LLFFASLRGKSKQEIAPK---IDEWMEKFQvKGKKT---DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNA 165
Cdd:cd03254 97 IRLGRPNATDEEVIEAAKeagAHDFIMKLP-NGYDTvlgENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 166 ELLKNGIIELKEKGSCVIFsSHNMDNVEKiCDHLIMLRNGETVLNGKVHEIRESFG 221
Cdd:cd03254 176 KLIQEALEKLMKGRTSIII-AHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-208 |
1.57e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.43 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKdyNT-------IG 74
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--STtaalaagVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 YLPEERGLYPKVTI-ENQLL-FFASLRGKSKQEIApkIDEWMEKFQVKGKKTD---KVKSLSKGNQQKVQLISTLIHEPK 149
Cdd:PRK11288 83 IIYQELHLVPEMTVaENLYLgQLPHKGGIVNRRLL--NYEAREQLEHLGVDIDpdtPLKYLSIGQRQMVEIAKALARNAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 150 LVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-208 |
1.60e-19 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.30 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 10 SFgSY----KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsgKDYNT------IGYLPEE 79
Cdd:COG1132 346 SF-SYpgdrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI--RDLTLeslrrqIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKvTIENQLLFfaslrGK---SKQEI--APK---IDEWMEKF------QV--KGKKtdkvksLSKGnqQKvQLIS- 142
Cdd:COG1132 423 TFLFSG-TIRENIRY-----GRpdaTDEEVeeAAKaaqAHEFIEALpdgydtVVgeRGVN------LSGG--QR-QRIAi 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 143 --TLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKeKGSCVIFSSHNMDNVEKiCDHLIMLRNGETV 208
Cdd:COG1132 488 arALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIV 553
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
3.39e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGS---VLWDGHTL--SGKDYNTI-- 73
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVqrEGRLARDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 -----GYLPEERGLYPKVTI-ENQLL--------------FFASLRGKSKQEIAPKIDewMEKFQVKgkktdKVKSLSKG 133
Cdd:PRK09984 84 srantGYIFQQFNLVNRLSVlENVLIgalgstpfwrtcfsWFTREQKQRALQALTRVG--MVHFAHQ-----RVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 134 NQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGK 212
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
...
gi 498433885 213 VHE 215
Cdd:PRK09984 237 SQQ 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-211 |
3.56e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRlILDFL-SKDSGSVLWDGHT--LSGK-DYNTIGYLP 77
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLeMPRSGTLNIAGNHfdFSKTpSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EERG-------LYPKVT-IENqlLFFASLR--GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHE 147
Cdd:PRK11124 82 RNVGmvfqqynLWPHLTvQQN--LIEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 148 PKLVILDEPFSGLDP-VNAELLKngII-ELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:PRK11124 160 PQVLLFDEPTAALDPeITAQIVS--IIrELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
15-211 |
3.88e-19 |
|
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: 83.79 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT----IGYLPEERGlypkvtien 90
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADlrrnIGYVPQDVT--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 qlLFFASLRgkskQEIA---PKID--EWMEKFQVKGkKTDKVK---------------SLSKGNQQKVQLISTLIHEPKL 150
Cdd:cd03245 89 --LFYGTLR----DNITlgaPLADdeRILRAAELAG-VTDFVNkhpngldlqigergrGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 151 VILDEPFSGLDPVNAELLKNGIIELKEkGSCVIFSSHNMdNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-226 |
4.19e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.58 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFL-----SKDSGSVLWDGHTLSGKDY------ 70
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVielrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 -NTIGYLPEErglYPKVTI-ENQLLFFASLR-GKSKQEIAPKIDEWMEKFQ----VKGKKTDKVKSLSKGNQQKVQLIST 143
Cdd:PRK14247 84 vQMVFQIPNP---IPNLSIfENVALGLKLNRlVKSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELLKNGIIELKeKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKV--------HE 215
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTrevftnprHE 239
|
250
....*....|.
gi 498433885 216 IRESFGRSKLY 226
Cdd:PRK14247 240 LTEKYVTGRLY 250
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-208 |
4.77e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 86.71 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 7 LSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY-----NTIGYLPEERG 81
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSkealeNGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 LYPKVTI-ENQLLFFASLRG------KSKQEIAPKIDEwmekFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILD 154
Cdd:PRK10982 84 LVLQRSVmDNMWLGRYPTKGmfvdqdKMYRDTKAIFDE----LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 155 EPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-216 |
5.65e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.98 E-value: 5.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDY-NTIGYL 76
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGldvATTPSRELaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIEnQLLFFA----SlRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:COG4604 81 RQENHINSRLTVR-ELVAFGrfpyS-KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 153 LDEPFSGLDPVNA-ELLKNgiieLK----EKGSCVI-------FSSHnmdnvekICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG4604 159 LDEPLNNLDMKHSvQMMKL----LRrladELGKTVVivlhdinFASC-------YADHIVAMKDGRVVAQGTPEEI 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-206 |
6.46e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 4 VEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTlsgkdynTIGYLPEERGLY 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-------RIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 PKVTIENQLL-----FFASLRGKSKQEIAP--------KIDEWMEKFQVKG-----------------KKTD---KVKSL 130
Cdd:COG0488 74 DDLTVLDTVLdgdaeLRALEAELEELEAKLaepdedleRLAELQEEFEALGgweaearaeeilsglgfPEEDldrPVSEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 131 SKGNQQKVQLISTLIHEPKLVILDEPFSGLDpVNAellkngiIE-----LKEKGSCVIFSSHN---MDNVekiCDHLIML 202
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD-LES-------IEwleefLKNYPGTVLVVSHDryfLDRV---ATRILEL 222
|
....
gi 498433885 203 RNGE 206
Cdd:COG0488 223 DRGK 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-219 |
8.00e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 8.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRL------ILDFLSKDSGSVLWDGHTLSGKD----YNTIGYLPEERGLYPKV 86
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDaiklRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 87 TIENQLLFFASLRG-KSKQEIAPKIDEWMEKFQVKGKKTDKVKS----LSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:PRK14246 106 SIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLWKEVYDRLNSpasqLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIFsSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:PRK14246 186 IVNSQAIEKLITELKNEIAIVIV-SHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-202 |
8.15e-19 |
|
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: 86.19 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD----YNTIGYL 76
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADadswRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLffaSLRGKSKQEIAPKID--EWMEKFQVKGKKTDKV-----KSLSKGNQQKVQLISTLIHEPK 149
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRL---ARPDASDAEIREALEraGLDEFVAALPQGLDTPigeggAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 150 LVILDEPFSGLDPVNAELLKNGIIELKEkGSCVIFSSHNmDNVEKICDHLIML 202
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHR-LALAALADRIVVL 529
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-216 |
8.96e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.11 E-value: 8.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYN-TIGYLPEERGL---YPKVTI-E 89
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNkNLKKLRKKVSLvfqFPEAQLfE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLL---FFASLR-GKSKQEIAPKIDEWMEKFQVKGKKTDKVK-SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVN 164
Cdd:PRK13641 101 NTVLkdvEFGPKNfGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498433885 165 AELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
1.14e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.85 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYK----ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIlDFLSK-DSGSVLWDGH---TLSGKDynt 72
Cdd:PRK11153 1 MIELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLLERpTSGRVLVDGQdltALSEKE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 igyLPEER----------GLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLIS 142
Cdd:PRK11153 77 ---LRKARrqigmifqhfNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 143 TLIHEPKLVILDEPFSGLDPVNA----ELLKNgiIElKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTrsilELLKD--IN-RELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-216 |
1.30e-18 |
|
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: 85.51 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYK----ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFL----SKDSGSVLWDGHTLSGkdynt 72
Cdd:COG4172 6 LLSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLpdpaAHPSGSILFDGQDLLG----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 igyLPEE-----RG-------------LYPKVTIENQLlfFASL---RGKSKQEIAPKIDEWMEKFQVKGKKTdKVKS-- 129
Cdd:COG4172 81 ---LSERelrriRGnriamifqepmtsLNPLHTIGKQI--AEVLrlhRGLSGAAARARALELLERVGIPDPER-RLDAyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 130 --LSKGNQQKVQLISTLIHEPKLVILDEPFSGLDP-VNA---ELLKngiiELKEK-GSCVIFSSHNMDNVEKICDHLIML 202
Cdd:COG4172 155 hqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtVQAqilDLLK----DLQRElGMALLLITHDLGVVRRFADRVAVM 230
|
250
....*....|....
gi 498433885 203 RNGETVLNGKVHEI 216
Cdd:COG4172 231 RQGEIVEQGPTAEL 244
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-211 |
1.35e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 82.75 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRlILDFLS-KDSGSVLWDGHTLS---GKDYNTIGYLP 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAGHQFDfsqKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EERG-------LYPKVTIENQLLFfASLR--GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEP 148
Cdd:COG4161 82 QKVGmvfqqynLWPHLTVMENLIE-APCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 149 KLVILDEPFSGLDP-VNAELLKngII-ELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:COG4161 161 QVLLFDEPTAALDPeITAQVVE--IIrELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-208 |
1.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.60 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF---GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY----NTI 73
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlrRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYL---PEERglYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKL 150
Cdd:PRK13642 84 GMVfqnPDNQ--FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 151 VILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFS-SHNMDNVEKiCDHLIMLRNGETV 208
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEAAS-SDRILVMKAGEII 219
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-161 |
1.52e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.39 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH--TLSGKDYNTIGYLPEE 79
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvTHRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
..
gi 498433885 160 LD 161
Cdd:PRK11432 167 LD 168
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-208 |
1.74e-18 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 82.93 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDyntigylPEERGLY------------- 83
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD-------RKQRRAFrrdvqlvfqdsps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 ---PKVTIE----NQLLFFASLRGKSKQEiapKIDEWMEKFQVKGKKTDKV-KSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:TIGR02769 100 avnPRMTVRqiigEPLRHLTSLDESEQKA---RIAELLDMVGLRSEDADKLpRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 156 PFSGLDPVnaelLKNGIIELKEK-----GSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:TIGR02769 177 AVSNLDMV----LQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-205 |
1.76e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSfgsykALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD-----YNTIGYL 76
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqdglANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEER---GLYPKVTI-ENQLL----FFASLRG--KSKQEIApKIDEWMEKFQVKGKKTDK-VKSLSKGNQQKVQLISTLI 145
Cdd:PRK10762 333 SEDRkrdGLVLGMSVkENMSLtalrYFSRAGGslKHADEQQ-AVSDFIRLFNIKTPSMEQaIGLLSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 146 HEPKLVILDEPFSGLDpVNAellKNGIIEL----KEKGSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:PRK10762 412 TRPKVLILDEPTRGVD-VGA---KKEIYQLinqfKAEGLSIILVSSEMPEVLGMSDRILVMHEG 471
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-205 |
1.84e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.37 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSG---KDYNtIGYLPE 78
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhaRDRK-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASL--RGK--SKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILD 154
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVlpRRErpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 155 EPFSGLDP-VNAEL---LKNGIIELKEKGscvIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:PRK10851 162 EPFGALDAqVRKELrrwLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQG 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-206 |
1.92e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.24 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY----NTIGYL---PEERglYPKVTIE 89
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdirHKIGMVfqnPDNQ--FVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLK 169
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 498433885 170 NGIIELKEK-GSCVIFSSHNMDNVeKICDHLIMLRNGE 206
Cdd:PRK13650 181 KTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQ 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-225 |
2.90e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.79 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIldflskdSGS-VLWDGH-TLSGKD----------Y 70
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGArKIQQGRvEVLGGDmadarhrravC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 NTIGYLPEERG--LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWME-----KFQVK--GKktdkvksLSKGNQQKVQLI 141
Cdd:NF033858 76 PRIAYMPQGLGknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRatglaPFADRpaGK-------LSGGMKQKLGLC 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 142 STLIHEPKLVILDEPFSGLDPVNA----ELLKNgiIELKEKGSCVIFSSHNMDNVEKiCDHLIMLRNGETVLNGKVHEIR 217
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRrqfwELIDR--IRAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELL 225
|
....*...
gi 498433885 218 ESFGRSKL 225
Cdd:NF033858 226 ARTGADTL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-215 |
3.92e-18 |
|
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: 81.51 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT----IGYLPEERGLYpKVTIEN 90
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlrraIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLLFfaslrGK---SKQEI-----APKIDEWMEKFQvKGKKTdKVKS----LSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03253 94 NIRY-----GRpdaTDEEVieaakAAQIHDKIMRFP-DGYDT-IVGErglkLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 159 GLDPVNAELLKNGIIELKeKGSCVIFSSHNMDNVEKiCDHLIMLRNGETVLNGKVHE 215
Cdd:cd03253 167 ALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
14-209 |
4.31e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.24 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 14 YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH-TLSGKDYNTIGYLP--EERGLYPKVTIEN 90
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQpTRQALQKNLVAYVPqsEEVDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLLF-----FASLRgKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNA 165
Cdd:PRK15056 100 VVMMgryghMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498433885 166 ELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNgeTVL 209
Cdd:PRK15056 179 ARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKG--TVL 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
6.16e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 81.51 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGyLPEER 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS-EAERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 ----------------GLYPKVT----IENQLL-----FFASLRGKSKQeiapkideWMEKFQVKGKKTDKV-KSLSKGN 134
Cdd:PRK11701 85 rllrtewgfvhqhprdGLRMQVSaggnIGERLMavgarHYGDIRATAGD--------WLERVEIDAARIDDLpTTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 135 QQKVQLISTLIHEPKLVILDEPFSGLD-PVNA---ELLKNGIIELkekGSCVIFSSHNMDNVEKICDHLIMLRNGETVLN 210
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDvSVQArllDLLRGLVREL---GLAVVIVTHDLAVARLLAHRLLVMKQGRVVES 233
|
.
gi 498433885 211 G 211
Cdd:PRK11701 234 G 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-226 |
6.16e-18 |
|
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: 80.99 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYN----TIGYLPEERGLYPKVTIEN- 90
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlrrQVGVVLQENVLFNRSIRDNi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 ----------QLLFFASLRGksKQEIAPKIDEWMEkfQVKGKKTdkvKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:cd03252 97 aladpgmsmeRVIEAAKLAG--AHDFISELPEGYD--TIVGEQG---AGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 161 DPVNAELLKNGIIELKeKGSCVIFSSHNMDNVeKICDHLIMLRNGETVLNGKVHEIRESFGR-SKLY 226
Cdd:cd03252 170 DYESEHAIMRNMHDIC-AGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAENGLyAYLY 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-195 |
6.89e-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: 80.10 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDYNTIGYLPE 78
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASLRGKSKQEiapkIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498433885 159 GLDPVNAELLKNGIIELKEKGSCVIFSSH---NMDNVEKI 195
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTHqdlGLVEAREL 196
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-216 |
7.68e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG--------HTLSGKDYNTI 73
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdAELREVRRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 154 DEPFSGLDPVNAELLKNGIIELKEKGS-CVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-187 |
1.07e-17 |
|
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: 79.46 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG---HTLSGKDYNTIGYLPE 78
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgplDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLYPKVTIENQLLFFASLRGKSkqeiapKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 498433885 159 GLDPVNAELLKNGIIELKEKGSCVIFSSH 187
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-216 |
1.17e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG----HTLSGKDYNTIGYLP 77
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EE--------------RGLYPkvtieNQLLFfaslrGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLIST 143
Cdd:PRK10253 88 QNattpgditvqelvaRGRYP-----HQPLF-----TRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-233 |
1.24e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.56 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSV-----LWDGHTLSGKDYNTIGY 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERG-------LYPKVT-IENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHE 147
Cdd:PRK11264 83 LRQHVGfvfqnfnLFPHRTvLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 148 PKLVILDEPFSGLDP-VNAELLkNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGkvhEIRESFG----- 221
Cdd:PRK11264 163 PEVILFDEPTSALDPeLVGEVL-NTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG---PAKALFAdpqqp 238
|
250
....*....|..
gi 498433885 222 RSKLYLDSHLTK 233
Cdd:PRK11264 239 RTRQFLEKFLLQ 250
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-216 |
1.56e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 81.29 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSG----------KDYNTIGYLPEErGLYP 84
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddewravrSDIQMIFQDPLA-SLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 85 KVTI-----ENQLLFFASLrgkSKQEIAPKIDEWMEKFQVKGKKTDKV-KSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:PRK15079 114 RMTIgeiiaEPLRTYHPKL---SRQEVKDRVKAMMLKVGLLPNLINRYpHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 159 GLDP------VNaeLLKngiiEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK15079 191 ALDVsiqaqvVN--LLQ----QLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-227 |
1.58e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 81.71 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTfRLILDFLSKDSGSVLWDGHTLSGKDY---NTIG-YLP 77
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRalrRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 78 EERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 158 SGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFGRSKLYL 227
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQI 242
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-216 |
2.80e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.39 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTigylpeERGLYPKVtienQLLF 94
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEA------QKLLRQKI----QIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 95 ---FASL--RGK---------------SKQEIAPKIDEWMEKFQVKGKKTDKVKSL-SKGNQQKVQLISTLIHEPKLVIL 153
Cdd:PRK11308 99 qnpYGSLnpRKKvgqileepllintslSAAERREKALAMMAKVGLRPEHYDRYPHMfSGGQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 154 DEPFSGLD-PVNAELLkNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK11308 179 DEPVSALDvSVQAQVL-NLMMDLqQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
2.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.28 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS-----YKALDDMTFTIEDGKILGLIGQNGAGKTTtfrLILDF--LSKDSGSVLWDGHTLSGKDYN-- 71
Cdd:PRK13631 21 ILRVKNLYCVFDEkqeneLVALNNISYTFEKNKIYFIIGNSGSGKST---LVTHFngLIKSKYGTIQVGDIYIGDKKNnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 72 --TIGYLPE-------------------ERGLYpKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVK-S 129
Cdd:PRK13631 98 elITNPYSKkiknfkelrrrvsmvfqfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPfG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 130 LSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVL 209
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
....*..
gi 498433885 210 NGKVHEI 216
Cdd:PRK13631 257 TGTPYEI 263
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-197 |
3.26e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.44 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFR-------LILDFlsKDSGSVLWDGHTLSGKDYNT-- 72
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGF--RVEGKVTFHGKNLYAPDVDPve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 ----IGYLPEERGLYPKVTIENqLLFFASLRGKSKQeiapkIDEWMEKF--------QVKGKKTDKVKSLSKGNQQKVQL 140
Cdd:PRK14243 89 vrrrIGMVFQKPNPFPKSIYDN-IAYGARINGYKGD-----MDELVERSlrqaalwdEVKDKLKQSGLSLSGGQQQRLCI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 141 ISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFsSHNMDNVEKICD 197
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV-THNMQQAARVSD 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-216 |
3.29e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.45 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYK-----ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYn 71
Cdd:PRK15112 4 LLEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 72 tiGYLPEE---------RGLYPKVTIeNQLLFFaSLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVK----SLSKGNQQKV 138
Cdd:PRK15112 83 --SYRSQRirmifqdpsTSLNPRQRI-SQILDF-PLRLNTDLEPEQREKQIIETLRQVGLLPDHASyyphMLAPGQKQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 139 QLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-211 |
3.59e-17 |
|
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: 77.35 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFG--SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDYNTIGYL 76
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYpKVTIENQLlffaslrgkskqeiapkidewmekfqvkGKKtdkvksLSKGNQQKVQLISTLIHEPKLVILDEP 156
Cdd:cd03247 81 NQRPYLF-DTTLRNNL----------------------------GRR------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 157 FSGLDPVNAELLKNGIIE-LKEKgsCVIFSSHNMDNVEKIcDHLIMLRNGETVLNG 211
Cdd:cd03247 126 TVGLDPITERQLLSLIFEvLKDK--TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-216 |
5.12e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.29 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKdynTIGYLPEERGL--------YPKVT 87
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE---TVWDVRRQVGMvfqnpdnqFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 88 IENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAEL 167
Cdd:PRK13635 99 VQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 168 LKNGIIELKEKGSCVIFS-SHNMDNVEKiCDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13635 179 VLETVRQLKEQKGITVLSiTHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-206 |
7.88e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 7.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKsfgsyKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-----IGYL 76
Cdd:PRK15439 269 LTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlargLVYL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEER---GLYPKVTI--------ENQLLFFAslrgKSKQEIApKIDEWMEKFQVKGKKTDK-VKSLSKGNQQKVQLISTL 144
Cdd:PRK15439 344 PEDRqssGLYLDAPLawnvcaltHNRRGFWI----KPARENA-VLERYRRALNIKFNHAEQaARTLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 145 IHEPKLVILDEPFSGLDpVNA-----ELLKNgiieLKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:PRK15439 419 EASPQLLIVDEPTRGVD-VSArndiyQLIRS----IAAQNVAVLFISSDLEEIEQMADRVLVMHQGE 480
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-216 |
1.23e-16 |
|
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: 79.73 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSF-----------GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDfLSKDSGSVLWDGHTLSGKDY 70
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 NtigylpEERGLYPKVtienQLLF---FASL------------------RGKSKQEIAPKIDEWMEK------------- 116
Cdd:COG4172 355 R------ALRPLRRRM----QVVFqdpFGSLsprmtvgqiiaeglrvhgPGLSAAERRARVAEALEEvgldpaarhryph 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 117 -FqvkgkktdkvkslSKGNQQKVQLISTLIHEPKLVILDEPFSGLD-PVNA---ELLKngiiEL-KEKGSCVIFSSHNMD 190
Cdd:COG4172 425 eF-------------SGGQRQRIAIARALILEPKLLVLDEPTSALDvSVQAqilDLLR----DLqREHGLAYLFISHDLA 487
|
250 260
....*....|....*....|....*.
gi 498433885 191 NVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:COG4172 488 VVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-208 |
1.39e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.75 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKD-----SGSVLWDGH-------- 63
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGEsllhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 64 TLSGKDYNTIGYLPEER--GLYPKVTIENQLLFFASL-RGKSKQEIAPKIDEWMEKF---QVKGKKTDKVKSLSKGNQQK 137
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVgirQAAKRLTDYPHQLSGGERQR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 138 VQLISTLIHEPKLVILDEPFSGLD-PVNAELLKNgIIELK-EKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDvSVQAQILQL-LRELQqELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-223 |
1.48e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.45 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTtfrlILDFLS------KDSGSVLWDGHTLSGKDYNTig 74
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKST----LMKVLSgvyphgSYEGEILFDGEVCRFKDIRD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 ylPEERG---------LYPKVTI-ENqlLFFASLRGKSK----QEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQL 140
Cdd:NF040905 75 --SEALGiviihqelaLIPYLSIaEN--IFLGNERAKRGvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 141 ISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKG-SCVIFsSHNMDNVEKICDHLIMLRNGETV-----LNGKVH 214
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIII-SHKLNEIRRVADSITVLRDGRTIetldcRADEVT 229
|
250
....*....|..
gi 498433885 215 E---IRESFGRS 223
Cdd:NF040905 230 EdriIRGMVGRD 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.53e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.20 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGS-----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLW---DGHTLSGKDYNTI 73
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 gYLPE----------------------------ERGLYpKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTD 125
Cdd:PRK13651 83 -VLEKlviqktrfkkikkikeirrrvgvvfqfaEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 126 KVK-SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRN 204
Cdd:PRK13651 161 RSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|..
gi 498433885 205 GETVLNGKVHEI 216
Cdd:PRK13651 241 GKIIKDGDTYDI 252
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-215 |
1.55e-16 |
|
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: 76.89 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT----IGYLPEERGLYPKvTIEN 90
Cdd:cd03251 16 PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrrqIGLVSQDVFLFND-TVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLLFfaSLRGKSKQEI--APKI---DEWMEKFQvKGKKT---DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDP 162
Cdd:cd03251 95 NIAY--GRPGATREEVeeAARAanaHEFIMELP-EGYDTvigERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 163 VNAELLKNGIIEL-KEKGSCVIfsSHNMDNVEKIcDHLIMLRNGETVLNGKvHE 215
Cdd:cd03251 172 ESERLVQAALERLmKNRTTFVI--AHRLSTIENA-DRIVVLEDGKIVERGT-HE 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-162 |
1.56e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.37 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKD---SGSVLWDGHTLSGKDYNT--IGY 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQrrIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEERGLYPKVTI-ENqlLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILD 154
Cdd:COG4136 81 LFQDDLLFPHLSVgEN--LAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLD 158
|
....*...
gi 498433885 155 EPFSGLDP 162
Cdd:COG4136 159 EPFSKLDA 166
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-216 |
2.51e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.54 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 21 TFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDG--HTLSGKDYNTIGYLPEERGLYPKVTIENQL------ 92
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTTPPSRRPVSMLFQENNLFSHLTVAQNIglglnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 93 -LFFASLRGKSKQEIAPK--IDEWMEKFQVKgkktdkvksLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVnaelLK 169
Cdd:PRK10771 99 gLKLNAAQREKLHAIARQmgIEDLLARLPGQ---------LSGGQRQRVALARCLVREQPILLLDEPFSALDPA----LR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498433885 170 NGIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK10771 166 QEMLTLvsqvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-188 |
2.85e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-IGYLPEE 79
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEaCHYLGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFFASLRGKSKQEIAPKIdewmEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:PRK13539 82 NAMKPALTVAENLEFWAAFLGGEELDIAAAL----EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*....
gi 498433885 160 LDPVNAELLKNGIIELKEKGSCVIFSSHN 188
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-202 |
4.22e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.52 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSGKDY-NTIGYL 76
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdisTLKPEIYrQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKvTIENQLLFFASLRGKSKQEIAPKIDewMEKFQVKGKKTDK-VKSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTILTKnIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498433885 156 PFSGLDPVNAELLkNGIIE--LKEKGSCVIFSSHNMDNVeKICDHLIML 202
Cdd:PRK10247 164 ITSALDESNKHNV-NEIIHryVREQNIAVLWVTHDKDEI-NHADKVITL 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
16-216 |
4.51e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.38 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGS---VLWDGHTLSGKdynTIGYLPEERGL--------YP 84
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAK---TVWDIREKVGIvfqnpdnqFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 85 KVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVN 164
Cdd:PRK13640 99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 165 AELLKNGIIELKEKGSCVIFS-SHNMDNVEkICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSPVEI 230
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-212 |
8.60e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.61 E-value: 8.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 8 SKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLwdghtLSGKDYNTIGylPEERG------ 81
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF-----IGEKRMNDVP--PAERGvgmvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 ---LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:PRK11000 83 syaLYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 159 GLDpvnAELLKNGIIEL----KEKGSCVIFSSHnmDNVE--KICDHLIMLRNGETVLNGK 212
Cdd:PRK11000 163 NLD---AALRVQMRIEIsrlhKRLGRTMIYVTH--DQVEamTLADKIVVLDAGRVAQVGK 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
17-215 |
9.03e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.39 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTT-----TFRLILDflSKDSGSVLWDGHTLSGKDYNTI-GYLPEERGLYPKVTIEN 90
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLLFFASLRGK---SKQEIAPKIDEWMEKFQ-VKGKKT-----DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:TIGR00955 119 HLMFQAHLRMPrrvTKKEKRERVDEVLQALGlRKCANTrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIF-----SSHNMDNVekicDHLIMLRNGETVLNGKVHE 215
Cdd:TIGR00955 199 SFMAYSVVQVLKGLAQKGKTIICtihqpSSELFELF----DKIILMAEGRVAYLGSPDQ 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-206 |
1.12e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.89 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILD-FLSKDSGSVLWDGHTLSGKD-----YNTIGYLPEER---GLYPK 85
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKPVKIRNpqqaiAQGIAMVPEDRkrdGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 86 VTI-ENQLLffASLRGKSKQEIAPK------IDEWMEKFQVKGKKTD-KVKSLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:PRK13549 356 MGVgKNITL--AALDRFTGGSRIDDaaelktILESIQRLKVKTASPElAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498433885 158 SGLDpVNA--ELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:PRK13549 434 RGID-VGAkyEIYKL-INQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-200 |
1.13e-15 |
|
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: 76.90 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWdGHTLSgkdyntIGYLPEER- 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK------LAYVDQSRd 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GLYPKVTIEnqllffaslrgkskQEIAPKIDE------------WMEKFQVKGKKTDK-VKSLSKGNQQKVQLISTLIHE 147
Cdd:TIGR03719 396 ALDPNKTVW--------------EEISGGLDIiklgkreipsraYVGRFNFKGSDQQKkVGQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498433885 148 PKLVILDEPFSGLDPVNAELLKNGIIELkekGSCVIFSSHNMDNVEKICDHLI 200
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVISHDRWFLDRIATHIL 511
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-216 |
1.13e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.05 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-----------GSYKALDDMTFTIEDGKILGLIGQNGAGKTTT----FRLIldflsKDSGSVLWDGHTL 65
Cdd:PRK15134 275 LLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 66 SGkdYNTIGYLPEER-----------GLYPKVTIENqlLFFASLR----GKSKQEIAPKIDEWMEKFQVKGKKTDKVKS- 129
Cdd:PRK15134 350 HN--LNRRQLLPVRHriqvvfqdpnsSLNPRLNVLQ--IIEEGLRvhqpTLSAAQREQQVIAVMEEVGLDPETRHRYPAe 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 130 LSKGNQQKVQLISTLIHEPKLVILDEPFSGLD-PVNAE---LLKNgiieLKEK-GSCVIFSSHNMDNVEKICDHLIMLRN 204
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDkTVQAQilaLLKS----LQQKhQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
250
....*....|..
gi 498433885 205 GETVLNGKVHEI 216
Cdd:PRK15134 502 GEVVEQGDCERV 513
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-219 |
1.87e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.44 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT----IGYLPEER------------ 80
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfarkVAYLPQQLpaaegmtvrelv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 --GLYPkvtienqllFFASLrGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:PRK10575 107 aiGRYP---------WHGAL-GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 159 GLDPVN-AELLknGIIEL--KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:PRK10575 177 ALDIAHqVDVL--ALVHRlsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRG 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-218 |
2.25e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkDYNtigylpeERGLYPKVTIENQ--LLF 94
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV--QYD-------HHYLHRQVALVGQepVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 95 FAS--------LRGKSKQEI-----APKIDEWMEKFQvKGKKTD---KVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:TIGR00958 568 SGSvreniaygLTDTPDEEImaaakAANAHDFIMEFP-NGYDTEvgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 159 GLDPVNAELLKngiiELKEKGS-CVIFSSHNMDNVEKiCDHLIMLRNGETVLNGKVHEIRE 218
Cdd:TIGR00958 647 ALDAECEQLLQ----ESRSRASrTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-205 |
2.38e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 2.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIlDFLSKDS-GSVLWDGHTLS------GK----DY 70
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSeGSIVVNGQTINlvrdkdGQlkvaDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 NTIGYLP-------EERGLYPKVTI-ENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKS-LSKGNQQKVQLI 141
Cdd:PRK10619 85 NQLRLLRtrltmvfQHFNLWSHMTVlENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 142 STLIHEPKLVILDEPFSGLDP-VNAELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPeLVGEVLRI-MQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-206 |
2.39e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 73.66 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkDYntigylpEERGLYPKVTIENQ--LLF 94
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS--QY-------EHKYLHSKVSLVGQepVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 95 FASLR--------GKSKQEI-----APKIDEWMEKFQvKGKKTD---KVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03248 101 ARSLQdniayglqSCSFECVkeaaqKAHAHSFISELA-SGYDTEvgeKGSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498433885 159 GLDpVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKiCDHLIMLRNGE 206
Cdd:cd03248 180 ALD-AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-208 |
2.60e-15 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 73.73 E-value: 2.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsgKDYNT------IGYLPEERGLYPkVTI 88
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI--RDLNLrwlrsqIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 89 ENQLLFFASLRGKSKQEIAPK-------IDEWMEKFQ-VKGKKTdkvKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:cd03249 94 AENIRYGKPDATDEEVEEAAKkanihdfIMSLPDGYDtLVGERG---SQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498433885 161 DPVNAELLKNGIIELKeKGSCVIFSSHNMDNVEKiCDHLIMLRNGETV 208
Cdd:cd03249 171 DAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-189 |
2.67e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 73.92 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTT---TFRLILDFLS--KDSGSVLWDGHTLSGKDYNtigyL 76
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgaRVEGEILLDGEDIYDPDVD----V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEER---GL-------YPKvTIENQLLFFASLRG-KSKQEiapkIDE-----------WMEkfqVKgkktDKVK----SL 130
Cdd:COG1117 88 VELRrrvGMvfqkpnpFPK-SIYDNVAYGLRLHGiKSKSE----LDEiveeslrkaalWDE---VK----DRLKksalGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 131 SKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKgSCVIFSSHNM 189
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNM 213
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
3.16e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.68 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgKDYNT----IGYL 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLCTyqkqLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENQLLFfaSLRGKSKqeiAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEP 156
Cdd:PRK13540 80 GHRSGINPYLTLRENCLY--DIHFSPG---AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 498433885 157 FSGLDPVNAELLKNGIIELKEKGSCVIFSSH 187
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-216 |
3.53e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.01 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-IGYLPEERGL---YPkvtiEN 90
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIKQIRKKVGLvfqFP----ES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLLFFASLR---------GKSKQEiAPKIDEwmEKFQVKGKKTDKVK----SLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:PRK13649 97 QLFEETVLKdvafgpqnfGVSQEE-AEALAR--EKLALVGISESLFEknpfELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 158 SGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-205 |
5.55e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.60 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEE 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RG-------LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVI 152
Cdd:PRK10908 81 IGmifqdhhLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 153 LDEPFSGLDpvnaELLKNGIIELKEK----GSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:PRK10908 161 ADEPTGNLD----DALSEGILRLFEEfnrvGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-206 |
6.61e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 21 TFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTL---SGKDYNTIGYL--PEER---GLYPKVTIE--- 89
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirSPRDAIRAGIMlcPEDRkaeGIIPVHSVAdni 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 ------NQLLFFASLRGKSKQEIApkiDEWMEKFQVKGKKTD-KVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDp 162
Cdd:PRK11288 353 nisarrHHLRAGCLINNRWEAENA---DRFIRSLNIKTPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID- 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498433885 163 VNAellKNGI----IELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:PRK11288 429 VGA---KHEIynviYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-208 |
8.53e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 72.80 E-value: 8.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSY---------KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDyn 71
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 72 tigylPEERGLYPKvtiENQLLFFAS--------------------LRGKSKQEIAPKIDEWMEKFQVKGKKTDKV-KSL 130
Cdd:PRK10419 81 -----RAQRKAFRR---DIQMVFQDSisavnprktvreiireplrhLLSLDKAERLARASEMLRAVDLDDSVLDKRpPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 131 SKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVnaelLKNGIIELKEK-----GSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLV----LQAGVIRLLKKlqqqfGTACLFITHDLRLVERFCQRVMVMDNG 228
|
...
gi 498433885 206 ETV 208
Cdd:PRK10419 229 QIV 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-206 |
9.27e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.09 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILD-FLSKDSGSVLWDGHTLSGKD-----YNTIGYLPEER---GLYPK 85
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNpaqaiRAGIAMVPEDRkrhGIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 86 VTIENQ--LLFFASLRGKSKQEIAPK---IDEWMEKFQVKGKKTD-KVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:TIGR02633 354 LGVGKNitLSVLKSFCFKMRIDAAAElqiIGSAIQRLKVKTASPFlPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498433885 160 LD-PVNAELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:TIGR02633 434 VDvGAKYEIYKL-INQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| DUF4162 |
pfam13732 |
Domain of unknown function (DUF4162); This domain is found at the C-terminus of bacterial ABC ... |
211-294 |
1.07e-14 |
|
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: 68.01 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 211 GKVHEIRESFGRSKLYLDShLTKQELEAFAGVHTVTQKeDGSFDITLEDPAAGQEIFVQATKDGYIPMFNQQPPTLEEIF 290
Cdd:pfam13732 1 GTLEEIKRSYGRNRIEVET-ADAEELLELPGVEEVEEE-GGGLELKLEDEEAANELLAALLSGGEIRSFEEEEPSLNDIF 78
|
....
gi 498433885 291 KWKA 294
Cdd:pfam13732 79 IEKV 82
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-216 |
1.17e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.22 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKD---SGSVLWDGH---TLSGKDY 70
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGReilNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 NTIgyLPEE---------RGLYPKVTIENQLLFFASL-RGKSKQEiapkidewmeKFQVKGKKTDKVK------------ 128
Cdd:PRK09473 92 NKL--RAEQismifqdpmTSLNPYMRVGEQLMEVLMLhKGMSKAE----------AFEESVRMLDAVKmpearkrmkmyp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 129 -SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD-PVNAEL--LKNgiiELK-EKGSCVIFSSHNMDNVEKICDHLIMLR 203
Cdd:PRK09473 160 hEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDvTVQAQImtLLN---ELKrEFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250
....*....|...
gi 498433885 204 NGETVLNGKVHEI 216
Cdd:PRK09473 237 AGRTMEYGNARDV 249
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-218 |
1.25e-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: 71.02 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSK--DSGSVLWDGHtlsgkdyNTIGYLPEE 79
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGE-------DITDLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 R---GLY---------PKVTIENqllfFasLRGkskqeiapkIDEwmekfqvkgkktdkvkSLSKGNQQKVQLISTLIHE 147
Cdd:cd03217 74 RarlGIFlafqyppeiPGVKNAD----F--LRY---------VNE----------------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 148 PKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNmdnvEKICDHLI-----MLRNGETVLNGK---VHEIRE 218
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY----QRLLDYIKpdrvhVLYDGRIVKSGDkelALEIEK 197
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-216 |
3.36e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGhtLSGKDYNTIGYLPEERGLYPK-------VTI 88
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIRNKAGMVFQnpdnqivATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 89 -ENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAEL 167
Cdd:PRK13633 103 vEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRRE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 168 LKNGIIEL-KEKGSCVIFSSHNMDNVEKiCDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13633 183 VVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-243 |
3.55e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 71.20 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTigylpEERGLYPKVTI-----E 89
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNK-----KLKPLRKKVGIvfqfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLL---------FFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVK-SLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:PRK13634 96 HQLFeetvekdicFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 160 LDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI-RESFGRSKLYLDSHLT---KQ 234
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIfADPDELEAIGLDLPETvkfKR 255
|
....*....
gi 498433885 235 ELEAFAGVH 243
Cdd:PRK13634 256 ALEEKFGIS 264
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-215 |
4.69e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDS--GSVLWDGHTLSGKDYNTIGYLPEERGLYPKVTIENQLLF 94
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 95 FASLR---GKSKQEIAPKIDEWMEKFQV-KGKKT----DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAE 166
Cdd:PLN03211 164 CSLLRlpkSLTKQEKILVAESVISELGLtKCENTiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 167 LLKNGIIELKEKGSCVIFSSHNMDN-VEKICDHLIMLRNGETVLNGKVHE 215
Cdd:PLN03211 244 RLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-206 |
5.76e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 5.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEERG 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 LYPKVTIENQLLffaSLRGKSKqeiaPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:PRK11247 93 LPWKKVIDNVGL---GLKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498433885 162 PVnAELLKNGIIE--LKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:PRK11247 166 AL-TRIEMQDLIEslWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-231 |
7.56e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 14 YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYN--------TIGYL---PEERgL 82
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirpvrkRIGMVfqfPESQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 83 YPKvTIENQLLFfaslrgkskqeiAPKiDEWMEKFQVKGKKTDKVKSL--------------SKGNQQKVQLISTLIHEP 148
Cdd:PRK13646 99 FED-TVEREIIF------------GPK-NFKMNLDEVKNYAHRLLMDLgfsrdvmsqspfqmSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 149 KLVILDEPFSGLDPVNAELLKNGIIELK-EKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVheiRESFGRSKLYL 227
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP---KELFKDKKKLA 241
|
....
gi 498433885 228 DSHL 231
Cdd:PRK13646 242 DWHI 245
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-206 |
7.70e-14 |
|
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: 68.65 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYK-----ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGhtlsgkdynTIGYL 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---------SIAYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKvTIENQLLFFASLRgkskqeiapkiDEWMEK----------FQV--KGKKT---DKVKSLSKGNQQKVQLI 141
Cdd:cd03250 72 SQEPWIQNG-TIRENILFGKPFD-----------EERYEKvikacalepdLEIlpDGDLTeigEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 142 STLIHEPKLVILDEPFSGLDP-VNAELLKNGIIELKEKGSCVIFSSHNMDNVEKiCDHLIMLRNGE 206
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAhVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-218 |
1.27e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.41 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLS-GKDYNT---I 73
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipAMSrSRLYTVrkrM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQLLFfaSLRGKSK---QEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKL 150
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAY--PLREHTQlpaPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 151 VILDEPFSGLDPVNAELLKNGIIELKEK-GSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-211 |
1.34e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.38 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTtfrLILDF---LSKDSGSVlwdghTLSGKDYN--TIGYLPEERGLY---P-- 84
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKST---LLLHLngiYLPQRGRV-----KVMGREVNaeNEKWVRSKVGLVfqdPdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 85 ---KVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:PRK13647 91 qvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-219 |
2.03e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.55 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 12 GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLsKDSGSVLWDGHTLSGKDYntIGYLPEER----------- 80
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGIT-KDNWHVTADRFRWNGIDL--LKLSPRERrkiigreiami 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 ------GLYPKVTIENQLL-----------FFASLRGKSKQEIapkidEWMEKFQVKGKKtDKVKS----LSKGNQQKVQ 139
Cdd:COG4170 95 fqepssCLDPSAKIGDQLIeaipswtfkgkWWQRFKWRKKRAI-----ELLHRVGIKDHK-DIMNSypheLTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 140 LISTLIHEPKLVILDEPFSGLDPVNaellKNGIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVH 214
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTT----QAQIFRLlarlnQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTE 244
|
....*
gi 498433885 215 EIRES 219
Cdd:COG4170 245 QILKS 249
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-208 |
3.74e-13 |
|
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: 66.50 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTtfrlILDFLS--KDSGSV----LWDGHTLsGKDYN-TIGYLPEERGLYPKVTIE 89
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTT----LLDVLAgrKTAGVItgeiLINGRPL-DKNFQrSTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLLFFASLRGKSKQEiapkidewmekfqvkgkktdkVKSLSKGnqqkVQLIStlihEPKLVILDEPFSGLDPVNAELLK 169
Cdd:cd03232 98 EALRFSALLRGLSVEQ---------------------RKRLTIG----VELAA----KPSILFLDEPTSGLDSQAAYNIV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498433885 170 NGIIELKEKGSCVIFSSH--NMDNVEKIcDHLIML-RNGETV 208
Cdd:cd03232 149 RFLKKLADSGQAILCTIHqpSASIFEKF-DRLLLLkRGGKTV 189
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-219 |
3.76e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.94 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFR-----LILDFLSKDSGSVLWDGHTLSGKDYNTI--- 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPIevr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 ---GYLPEERGLYPKVTIENQLLFFASLRG--KSKQEIaPKIDEWMEKF-----QVKGKKTDKVKSLSKGNQQKVQLIST 143
Cdd:PRK14267 85 revGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKEL-DERVEWALKKaalwdEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFsSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLV-THSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-211 |
4.02e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 69.28 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLsgKDYnTIGYLPEERGLYPKV------TIE 89
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL--RDY-TLASLRNQVALVSQNvhlfndTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLLfFASLRGKSKQEI--APKIDEWMEKFQVKGKKTDKV-----KSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDP 162
Cdd:PRK11176 435 NNIA-YARTEQYSREQIeeAARMAYAMDFINKMDNGLDTVigengVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 163 VNAELLKNGIIEL-KEKGSCVIfsSHNMDNVEKiCDHLIMLRNGETVLNG 211
Cdd:PRK11176 514 ESERAIQAALDELqKNRTSLVI--AHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-206 |
4.04e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD-----YNTIGYLPEER---GLYPKV 86
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavKKGMAYITESRrdnGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 87 TIENQLLFFASLR------------GKSKQEIApkiDEWMEKFQVKGKKTDK-VKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:PRK09700 357 SIAQNMAISRSLKdggykgamglfhEVDEQRTA---ENQRELLALKCHSVNQnITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 154 DEPFSGLD-PVNAELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:PRK09700 434 DEPTRGIDvGAKAEIYKV-MRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-205 |
4.37e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFG----SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDY------ 70
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 71 --NTIGYLPEERGLYPKVT-IEN---QLLffasLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTL 144
Cdd:PRK11629 85 rnQKLGFIYQFHHLLPDFTaLENvamPLL----IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 145 IHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMlRNG 205
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEM-RDG 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-161 |
7.79e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.61 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWdGHTLSgkdyntIGYLPEER- 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK------LAYVDQSRd 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GLYPKVTIEnqllffaslrgkskQEIAPKIDE-WMEKFQVKG---------KKTD---KVKSLSKGNQQKVQLISTLIHE 147
Cdd:PRK11819 398 ALDPNKTVW--------------EEISGGLDIiKVGNREIPSrayvgrfnfKGGDqqkKVGVLSGGERNRLHLAKTLKQG 463
|
170
....*....|....
gi 498433885 148 PKLVILDEPFSGLD 161
Cdd:PRK11819 464 GNVLLLDEPTNDLD 477
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
16-216 |
8.55e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.08 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT----IGYL---PEERGLYPKVT- 87
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkhIGIVfqnPDNQFVGSIVKy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 88 -----IENQLLffaslrgkSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDP 162
Cdd:PRK13648 104 dvafgLENHAV--------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 163 VNAELLKNGIIELKEKGSCVIFS-SHNMDNVEKiCDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-168 |
1.15e-12 |
|
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: 67.77 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYN----TIGYL 76
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDevrrRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYpKVTIENQLLFFASlrGKSKQEI-----APKIDEWMEKFQvKGKKTDKV---KSLSKGNQQKVQLISTLIHEP 148
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRLARP--DATDEELwaaleRVGLADWLRALP-DGLDTVLGeggARLSGGERQRLALARALLADA 490
|
170 180
....*....|....*....|.
gi 498433885 149 KLVILDEPFSGLDP-VNAELL 168
Cdd:TIGR02868 491 PILLLDEPTEHLDAeTADELL 511
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6-214 |
3.23e-12 |
|
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: 65.12 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 6 KLSKSFGSYKaLDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkdyntigYLPEErgLYPK 85
Cdd:cd03237 5 TMKKTLGEFT-LEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQY--IKAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 86 VTIENQLLFFASLRGKS-----KQEIA-P-KIDEWMEKfqvkgkktdKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03237 74 YEGTVRDLLSSITKDFYthpyfKTEIAkPlQIEQILDR---------EVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 159 GLDpVNAELLKNGII----ELKEKGSCVIfsSHNMDNVEKICDHLIMLrNGETVLNGKVH 214
Cdd:cd03237 145 YLD-VEQRLMASKVIrrfaENNEKTAFVV--EHDIIMIDYLADRLIVF-EGEPSVNGVAN 200
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-219 |
3.99e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.70 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTtfrlildfLSK----------DSGSVLWDGHTLSGKDyn 71
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKST--------LAKvlmghpkyevTSGSILLDGEDILELS-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 72 tigylPEER---GLY---------PKVTIENqLLFFASlrgKSKQEIAPKIDEWMEKFQvkgKKTDKVK----------- 128
Cdd:COG0396 71 -----PDERaraGIFlafqypveiPGVSVSN-FLRTAL---NARRGEELSAREFLKLLK---EKMKELGldedfldryvn 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 129 -SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNmdnvEKI-----CDHLIML 202
Cdd:COG0396 139 eGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY----QRIldyikPDFVHVL 214
|
250 260
....*....|....*....|
gi 498433885 203 RNGETVLNGK---VHEIRES 219
Cdd:COG0396 215 VDGRIVKSGGkelALELEEE 234
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-187 |
4.37e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.19 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 10 SFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIL-DF---LSKD---------SGSVLWD--GHtlsgkdyntIG 74
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgDHpqgYSNDltlfgrrrgSGETIWDikKH---------IG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 YLPEERGLYPKV--TIENQLL--FFASLrG-----KSKQEIapKIDEWMEKFQVKGKKTDK-VKSLSKGnQQKVQLIS-T 143
Cdd:PRK10938 340 YVSSSLHLDYRVstSVRNVILsgFFDSI-GiyqavSDRQQK--LAQQWLDILGIDKRTADApFHSLSWG-QQRLALIVrA 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSC-VIFSSH 187
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-187 |
4.61e-12 |
|
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: 62.94 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKAL-DDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSV--LWDGHTLsgkdyntigYLPE 78
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgmPEGEDLL---------FLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 eRGLYPKVTIENQLLFfaslrgkskqeiaPkideWMEKfqvkgkktdkvksLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:cd03223 72 -RPYLPLGTLREQLIY-------------P----WDDV-------------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180
....*....|....*....|....*....
gi 498433885 159 GLDPVNAELLKNgiiELKEKGSCVIFSSH 187
Cdd:cd03223 121 ALDEESEDRLYQ---LLKELGITVISVGH 146
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-216 |
1.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.60 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFG-----SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSV-LWDGHTLSGKDYNTIG 74
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtVGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 75 YLPEERGL---YPKV-----TIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVK-SLSKGNQQKVQLISTLI 145
Cdd:PRK13643 81 PVRKKVGVvfqFPESqlfeeTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 146 HEPKLVILDEPFSGLDP-VNAELLKngIIE-LKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPkARIEMMQ--LFEsIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-203 |
1.77e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.53 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWdghtlsgKDYNTIGYLPEERG 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-------SENANIGYYAQDHA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 LYpkvtIENQLLFFaslrgkskqeiapkidEWMEKFQ--------VKG------------KKtdKVKSLSKGNQQKVQLI 141
Cdd:PRK15064 393 YD----FENDLTLF----------------DWMSQWRqegddeqaVRGtlgrllfsqddiKK--SVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498433885 142 STLIHEPKLVILDEPFSGLDPVNAELLKNGiieLKEKGSCVIFSSHNMDNVEKICDHLIMLR 203
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMA---LEKYEGTLIFVSHDREFVSSLATRIIEIT 509
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-205 |
1.80e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSfgSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD-----YNTIGY 75
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneaiNHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 76 LPEER---GLYPKVTIEnqllfFASLrgkskqeIApKIDEWMEKFQV---KGKKTD--------KVK---------SLSK 132
Cdd:PRK10982 328 VTEERrstGIYAYLDIG-----FNSL-------IS-NIRNYKNKVGLldnSRMKSDtqwvidsmRVKtpghrtqigSLSG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 133 GNQQKVQLISTLIHEPKLVILDEPFSGLDpVNAEL-LKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGID-VGAKFeIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-219 |
1.94e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 63.19 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 7 LSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIL---DFLS--KDSGSVLWDGHTL-SGKDY----NTIGYL 76
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmnDKVSgyRYSGDVLLGGRSIfNYRDVlefrRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIEN--------QLLFFASLRGKSKQEIApKIDEWMekfQVKGKKTDKVKSLSKGNQQKVQLISTLIHEP 148
Cdd:PRK14271 107 FQRPNPFPMSIMDNvlagvrahKLVPRKEFRGVAQARLT-EVGLWD---AVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498433885 149 KLVILDEPFSGLDPVNAELLKNGIIELKEKGScVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-206 |
2.34e-11 |
|
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: 62.04 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSY--KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDghtlsGKDYNTIGYlpee 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID-----GIDISTIPL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQ--LLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDkvksLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:cd03369 78 EDLRSSLTIIPQdpTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498433885 158 SGLDpVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKiCDHLIMLRNGE 206
Cdd:cd03369 154 ASID-YATDALIQKTIREEFTNSTILTIAHRLRTIID-YDKILVMDAGE 200
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-216 |
2.67e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIL---DFlskdSGSVLWDGHTLSGKDYNTI 73
Cdd:PRK11022 3 LLNVDKLSVHFGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMgliDY----PGRVMAEKLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYlPEERGLypkVTIENQLLF---FASLrgKSKQEIAPKIDEWMEKFQVKGKKTDKVKS--------------------- 129
Cdd:PRK11022 79 SE-KERRNL---VGAEVAMIFqdpMTSL--NPCYTVGFQIMEAIKVHQGGNKKTRRQRAidllnqvgipdpasrldvyph 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 130 -LSKGNQQKVQLISTLIHEPKLVILDEPFSGLD-PVNAEllkngIIEL-----KEKGSCVIFSSHNMDNVEKICDHLIML 202
Cdd:PRK11022 153 qLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQ-----IIELllelqQKENMALVLITHDLALVAEAAHKIIVM 227
|
250
....*....|....
gi 498433885 203 RNGETVLNGKVHEI 216
Cdd:PRK11022 228 YAGQVVETGKAHDI 241
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-216 |
3.45e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGyL 76
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIE-L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEE--------RG-------------LYPKVTIENQLLffASLR---GKSKQEIAPKIDEWMEkfQVKGKKTDKVKS--- 129
Cdd:PRK10261 91 SEQsaaqmrhvRGadmamifqepmtsLNPVFTVGEQIA--ESIRlhqGASREEAMVEAKRMLD--QVRIPEAQTILSryp 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 130 --LSKGNQQKVQLISTLIHEPKLVILDEPFSGLD-PVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGE 206
Cdd:PRK10261 167 hqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|
gi 498433885 207 TVLNGKVHEI 216
Cdd:PRK10261 247 AVETGSVEQI 256
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-205 |
3.85e-11 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 62.13 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIlDFLSK-DSGSVLWDGHTLSGKDYNTIGYLPEE 79
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCI-NLLETpDSGEIRVGGEEIRLKPDRDGELVPAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 R-----------------GLYPKVTI-ENqlLFFASLR--GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQ 139
Cdd:COG4598 87 RrqlqrirtrlgmvfqsfNLWSHMTVlEN--VIEAPVHvlGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 140 LISTLIHEPKLVILDEPFSGLDP--VNaELLKNgIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPelVG-EVLKV-MRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQG 230
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-205 |
4.51e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.14 E-value: 4.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 13 SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGhtlsgkDYNTIGYlpeERGLYPKVTIENQL 92
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAI---SAGLSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 93 LFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGI 172
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190
....*....|....*....|....*....|...
gi 498433885 173 IELKEKGSCVIFSSHNMDNVEKICDHLIMLRNG 205
Cdd:PRK13546 187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-207 |
6.79e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.59 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 2 LQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLI-----LDFLSKDSGSVLWDGHTLSGKDYNTIGYL 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPK-----VTIENQLLFFASLRG-KSKQEIAPKI-------DEWMEkfqVKGKKTDKVKSLSKGNQQKVQLIST 143
Cdd:PRK14258 88 RQVSMVHPKpnlfpMSVYDNVAYGVKIVGwRPKLEIDDIVesalkdaDLWDE---IKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGS-CVIFSSHNMDNVEKICDHLIMLRNGET 207
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDFTAFFKGNEN 229
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-213 |
7.58e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKD--SGSVLWDGHTLSGKDyntigylPE 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLE-------PE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ER---GL-----YPkVTI---ENQLLFFASLRGKSKQEIAPKIDEwMEKFQVKGKKTDKVK------------SLSKGNQ 135
Cdd:CHL00131 80 ERahlGIflafqYP-IEIpgvSNADFLRLAYNSKRKFQGLPELDP-LEFLEIINEKLKLVGmdpsflsrnvneGFSGGEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498433885 136 QKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKIC-DHLIMLRNGETVLNGKV 213
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-248 |
1.33e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.17 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTtfrlILDFLS-KDSGSVLWDGHTLSG--KDYNTI----GYLPEERGLYPKVTIE 89
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTT----LMDVLAgRKTGGYIEGDIRISGfpKKQETFarisGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLLFFASLR---GKSKQEIAPKIDEWMEKFQVKGKKT-----DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD 161
Cdd:PLN03140 972 ESLIYSAFLRlpkEVSKEEKMMFVDEVMELVELDNLKDaivglPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 162 PVNAELLKNGIIELKEKGSCVIFSSH--NMDNVEKICDHLIMLRNGETVLNGkvheireSFGRsklylDSHLTKQELEAF 239
Cdd:PLN03140 1052 ARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSG-------PLGR-----NSHKIIEYFEAI 1119
|
....*....
gi 498433885 240 AGVHTVTQK 248
Cdd:PLN03140 1120 PGVPKIKEK 1128
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-173 |
1.57e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT-IGYLPEE 79
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRfMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKV-TIENqLLFFASLRGKSKQEIAPKIdewMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:PRK13543 91 PGLKADLsTLEN-LHFLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170
....*....|....*
gi 498433885 159 GLDPVNAELLkNGII 173
Cdd:PRK13543 167 NLDLEGITLV-NRMI 180
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
1.64e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 59.50 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSyKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNTIGYLPEER 80
Cdd:PRK13541 1 MLSLHQLQFNIEQ-KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GLYPKVTIENQLLFFASLRGKskqeiAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:PRK13541 80 GLKLEMTVFENLKFWSEIYNS-----AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL 154
|
170 180
....*....|....*....|....*..
gi 498433885 161 DPVNAELLKNGIIELKEKGSCVIFSSH 187
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-221 |
1.67e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 61.44 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSF-----GSYK-ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGhtlsgkdynTIGYL 76
Cdd:PRK13545 20 PFDKLKDLFfrskdGEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------SAALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVT-IENQLL--FFASLRGKSKQEIAPKIDEWME--KFQvkgkkTDKVKSLSKGNQQKVQLISTLIHEPKLV 151
Cdd:PRK13545 91 AISSGLNGQLTgIENIELkgLMMGLTKEKIKEIIPEIIEFADigKFI-----YQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 152 ILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRESFG 221
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-216 |
1.99e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 21 TFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKdSGSVLWDGHTLSGKDYNTI----GYLPEERGLYPKVTIENQL-LFF 95
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELarhrAYLSQQQTPPFAMPVFQYLtLHQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 96 ASlrGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTL--IH-----EPKLVILDEPFSGLDPVNAELL 168
Cdd:PRK03695 95 PD--KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdinpAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498433885 169 KNGIIELKEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-206 |
2.08e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 22 FTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNtigylpEERGLYPKVTIENQLlfFASLRGK 101
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE------DYRKLFSAVFTDFHL--FDQLLGP 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 102 SKQEIAPKI-DEWMEKFQVKgkktDKVK---------SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPV-----NAE 166
Cdd:PRK10522 416 EGKPANPALvEKWLERLKMA----HKLEledgrisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHfrrefYQV 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498433885 167 LLKngiiELKEKGSCVIFSSHNmDNVEKICDHLIMLRNGE 206
Cdd:PRK10522 492 LLP----LLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQ 526
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-222 |
2.48e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKaLDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDghtlsgkdyNTIGYLPEER 80
Cdd:PRK13409 340 LVEYPDLTKKLGDFS-LEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---------LKISYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 81 GLYPKVTIEnQLLFFASLRGKS---KQEIAPK--IDEWMEKfqvkgkktdKVKSLSKGNQQKVQLISTLIHEPKLVILDE 155
Cdd:PRK13409 410 KPDYDGTVE-DLLRSITDDLGSsyyKSEIIKPlqLERLLDK---------NVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 156 PFSGLDpVN-----AELLKNgIIELKEKGSCVIfsSHNMDNVEKICDHlIMLRNGETVLNGKVH---EIRESFGR 222
Cdd:PRK13409 480 PSAHLD-VEqrlavAKAIRR-IAEEREATALVV--DHDIYMIDYISDR-LMVFEGEPGKHGHASgpmDMREGMNR 549
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-197 |
3.84e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIL--DFLSKDSGSVLWDG-----HTLSGKDYNTIGYLPEER---GLYP 84
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgrSYGRNISGTVFKDGkevdvSTVSDAIDAGLAYVTEDRkgyGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 85 KVTI-ENQLLffASLRGKSKQEIapkIDEWME---------KFQVKGKKTD-KVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:NF040905 354 IDDIkRNITL--ANLGKVSRRGV---IDENEEikvaeeyrkKMNIKTPSVFqKVGNLSGGNQQKVVLSKWLFTDPDVLIL 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498433885 154 DEPFSGLDpVNAELLKNGII-ELKEKGSCVIFSSHNMDNVEKICD 197
Cdd:NF040905 429 DEPTRGID-VGAKYEIYTIInELAAEGKGVIVISSELPELLGMCD 472
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-208 |
4.54e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH---TLSG-------KDYNTIGYLPEErGLYPK 85
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPgklqalrRDIQFIFQDPYA-SLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 86 VT----IENQLLFFASLRGKSKQEiapKIDEWMEKFQVKGKKTDKV-KSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:PRK10261 418 QTvgdsIMEPLRVHGLLPGKAAAA---RVAWLLERVGLLPEHAWRYpHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 161 D-PVNAELLkNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:PRK10261 495 DvSIRGQII-NLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-215 |
5.12e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 19 DMTFTIEDGKILGLIGQNGAGKTTTFRLILDF------------------------------------------------ 50
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkegg 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 51 ------LSKDSGSVLWDGHTLSgkDYNtigyLPEERGLYPKVTIEnQLLFFASLRGKSK--QEIAPK-----------ID 111
Cdd:PTZ00265 1266 sgedstVFKNSGKILLDGVDIC--DYN----LKDLRNLFSIVSQE-PMLFNMSIYENIKfgKEDATRedvkrackfaaID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 112 EWMEkfQVKGKKTDKV----KSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFS-S 186
Cdd:PTZ00265 1339 EFIE--SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITiA 1416
|
250 260 270
....*....|....*....|....*....|...
gi 498433885 187 HNMDNVEKiCDHLIML----RNGETVLNGKVHE 215
Cdd:PTZ00265 1417 HRIASIKR-SDKIVVFnnpdRTGSFVQAHGTHE 1448
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-221 |
5.88e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.86 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 21 TFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKdSGSVLWDGHTLSGKD----YNTIGYLPEERGLyPKVTI-ENQLLff 95
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDpeswRKHLSWVGQNPQL-PHGTLrDNVLL-- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 96 aslrGK---SKQEI-----APKIDEWMEKfQVKGKKT---DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVN 164
Cdd:PRK11174 446 ----GNpdaSDEQLqqaleNAWVSEFLPL-LPQGLDTpigDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 165 AELLKNGIIELKeKGSCVIFSSHNMDNVEKiCDHLIMLRNGETVLNGKVHEIRESFG 221
Cdd:PRK11174 521 EQLVMQALNAAS-RRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-215 |
1.37e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.68 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 15 KALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSgkDYNtigylpeERGLYPKVTIENQL-- 92
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA--DYS-------EAALRQAISVVSQRvh 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 93 LFFASLRGKSKQEIAPKIDEWMEKF--QVK-GKKTDKVKSL-----------SKGNQQKVQLISTLIHEPKLVILDEPFS 158
Cdd:PRK11160 425 LFSATLRDNLLLAAPNASDEALIEVlqQVGlEKLLEDDKGLnawlgeggrqlSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 159 GLDPVNA-ELLKNgiieLKE--KGSCVIFSSHNMDNVEKIcDHLIMLRNGETVLNGKVHE 215
Cdd:PRK11160 505 GLDAETErQILEL----LAEhaQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-205 |
3.16e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.19 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYN--------TIGYLPEERGLYpKVTI 88
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrsrnrySVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 89 ENQLLF---FASLRGKSKQE---IAPKIDewMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD- 161
Cdd:cd03290 96 EENITFgspFNKQRYKAVTDacsLQPDID--LLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDi 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498433885 162 PVNAELLKNGIIE-LKEKGSCVIFSSHNMDNVEKiCDHLIMLRNG 205
Cdd:cd03290 174 HLSDHLMQEGILKfLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-206 |
4.81e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.56 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGS----YKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKD------- 69
Cdd:PRK10584 6 IVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 70 -YNTIGYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVkGKKTDKVKS-LSKGNQQKVQLISTLIHE 147
Cdd:PRK10584 86 rAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGL-GKRLDHLPAqLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 148 PKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNmDNVEKICDHLIMLRNGE 206
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQ 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-218 |
1.01e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRlILDFLSKDSGSVlwdgHTLSGKDYNTI--- 73
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKPTSGT----YRVAGQDVATLdad 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 ----------GYLPEERGLYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLIST 143
Cdd:PRK10535 79 alaqlrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498433885 144 LIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDnVEKICDHLIMLRNGETVLNGKVHEIRE 218
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVRNPPAQEKVN 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-231 |
1.23e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.07 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDS----GSVLWDGHTLSgKDYNTIGYLPEE---------RGLY 83
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGeiqiDGVSWNSVTLQ-TWRKAFGVIPQKvfifsgtfrKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 PKVTIENQLLFfaslrgKSKQEIAPK--IDEWMEK--FQVkgkkTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:TIGR01271 1314 PYEQWSDEEIW------KVAEEVGLKsvIEQFPDKldFVL----VDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 160 LDPVNAELLKNgiiELKEKGS-C-VIFSSHNMDNVEKiCDHLIMLRNG--------ETVLNGKVHeIRESFG---RSKLY 226
Cdd:TIGR01271 1384 LDPVTLQIIRK---TLKQSFSnCtVILSEHRVEALLE-CQQFLVIEGSsvkqydsiQKLLNETSL-FKQAMSaadRLKLF 1458
|
....*
gi 498433885 227 LDSHL 231
Cdd:TIGR01271 1459 PLHRR 1463
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-208 |
1.68e-08 |
|
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: 54.04 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTT----FRLIldflSKDSGSVLWDGHtlsgkDYNTIGyLPEERGlypKVTIENQ 91
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGV-----DISKIG-LHDLRS---RISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 92 --LLFFASLRgkskQEIAP-------KIDEWMEKFQVK-------GKKTDKVKS----LSKGNQQKVQLISTLIHEPKLV 151
Cdd:cd03244 86 dpVLFSGTIR----SNLDPfgeysdeELWQALERVGLKefveslpGGLDTVVEEggenLSVGQRQLLCLARALLRKSKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 152 ILDEPFSGLDPVNAELLKNgIIELKEKGSCVIFSSHNMDNVEKiCDHLIMLRNGETV 208
Cdd:cd03244 162 VLDEATASVDPETDALIQK-TIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-183 |
2.64e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 6 KLSKSFGSYKaLDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDghtlsgkdyNTIGYLPEerglYPK 85
Cdd:COG1245 346 DLTKSYGGFS-LEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---------LKISYKPQ----YIS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 86 VTIENQLLFFasLRGKSKQEIAPKI--DEWMEKFQVKgKKTDK-VKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDp 162
Cdd:COG1245 412 PDYDGTVEEF--LRSANTDDFGSSYykTEIIKPLGLE-KLLDKnVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD- 487
|
170 180
....*....|....*....|....*.
gi 498433885 163 VN-----AELLKNgIIELKEKGSCVI 183
Cdd:COG1245 488 VEqrlavAKAIRR-FAENRGKTAMVV 512
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-222 |
2.84e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.58 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGH-----TLSGKDYNtIGYL 76
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvTRASLRRN-IAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 77 PEERGLYPKVTIENqllffasLR-GK---SKQEI--APKIDEWMEKFQVKGKKTDKV-----KSLSKGNQQKVQLISTLI 145
Cdd:PRK13657 415 FQDAGLFNRSIEDN-------IRvGRpdaTDEEMraAAERAQAHDFIERKPDGYDTVvgergRQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498433885 146 HEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIfsSHNMDNVEKiCDHLIMLRNGETVLNGKVHEIRESFGR 222
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELmKGRTTFII--AHRLSTVRN-ADRILVFDNGRVVESGSFDELVARGGR 562
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
29-219 |
6.02e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 29 ILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGKDYNT--------IGYLPEERGLYPKVTIENQLLFfaSLRG 100
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppekrrIGYVFQDARLFPHYKVRGNLRY--GMAK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 101 KSKQEIAP-----KIDEWMEKFQVkgkktdkvkSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD-PVNAELLkNGIIE 174
Cdd:PRK11144 104 SMVAQFDKivallGIEPLLDRYPG---------SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELL-PYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498433885 175 L-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNGKVHEIRES 219
Cdd:PRK11144 174 LaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWAS 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-168 |
6.23e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWdGHTLSgkdyntIGYLPEERG- 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE------VAYFDQHRAe 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 82 LYPKVTIENQLlffaslrGKSKQEIapkidewmekfQVKGKK-----------------TDKVKSLSKGNQQKVQLISTL 144
Cdd:PRK11147 394 LDPEKTVMDNL-------AEGKQEV-----------MVNGRPrhvlgylqdflfhpkraMTPVKALSGGERNRLLLARLF 455
|
170 180
....*....|....*....|....
gi 498433885 145 IHEPKLVILDEPFSGLDPVNAELL 168
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETLELL 479
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-206 |
6.84e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSV-LWDGHTLsgkdyntiGYLPEE 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL--------GYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTiENQLLFFASLrgkSKQEIAPKIDEWMEKFQVKGKK-TDKVKSLSKGnqQKVQLISTLI--HEPKLVILDEP 156
Cdd:PRK10636 384 QLEFLRAD-ESPLQHLARL---APQELEQKLRDYLGGFGFQGDKvTEETRRFSGG--EKARLVLALIvwQRPNLLLLDEP 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498433885 157 FSGLDPVNAELLKNGIIELkeKGSCVIFsSHNMDNVEKICDHLIMLRNGE 206
Cdd:PRK10636 458 TNHLDLDMRQALTEALIDF--EGALVVV-SHDRHLLRSTTDDLYLVHDGK 504
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
6-211 |
7.37e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 7.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 6 KLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLI---LDFLSKDSGSVLWDGHTLSG---KDYNTIGYLPEE 79
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEfaeKYPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RGLYPKVTIENQLLFFASLRGkskqeiapkidewmekfqvkgkkTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSG 159
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 160 LDPVNAELLKNGIIEL--KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETVLNG 211
Cdd:cd03233 149 LDSSTALEILKCIRTMadVLKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-192 |
1.05e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 6 KLSKSFGSYKA-LDDMTFTIEDGKILGLIGQNGAGKTTTFRlILDFLSKDSgsvlwDGHTLSGKDYnTIGYLPEERGLYP 84
Cdd:TIGR03719 9 RVSKVVPPKKEiLKDISLSFFPGAKIGVLGLNGAGKSTLLR-IMAGVDKDF-----NGEARPQPGI-KVGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 85 KVTI-ENQLLFFASLRGKSKQ--EIAPK-----------IDEwMEKFQVKGKKTD----------------------KVK 128
Cdd:TIGR03719 82 TKTVrENVEEGVAEIKDALDRfnEISAKyaepdadfdklAAE-QAELQEIIDAADawdldsqleiamdalrcppwdaDVT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 129 SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNgiiELKEKGSCVIFSSHN---MDNV 192
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEYPGTVVAVTHDryfLDNV 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-200 |
1.35e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.44 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 11 FGSYKALDDMTFTieDGKILGLIGQNGAGKTTTFRlildflskdsgSVLWdghTLSGKDYNTIGYLPEERGLYpKVTIEN 90
Cdd:cd03227 7 FPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILD-----------AIGL---ALGGAQSATRRRSGVKAGCI-VAAVSA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 91 QLLFFaslrgkskqeiapkidewmekfqvkgkktdkVKSLSKGNQQKVQLISTLIHEPK----LVILDEPFSGLDPVNAE 166
Cdd:cd03227 70 ELIFT-------------------------------RLQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....
gi 498433885 167 LLKNGIIELKEKGSCVIFSSHNMDnVEKICDHLI 200
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLPE-LAELADKLI 151
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-161 |
1.42e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF-GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLwdghtLSGKDYNTIGylPEE 79
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW-----IGGRVVNELE--PAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 80 RG---------LYPKVTIENQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKL 150
Cdd:PRK11650 76 RDiamvfqnyaLYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170
....*....|.
gi 498433885 151 VILDEPFSGLD 161
Cdd:PRK11650 156 FLFDEPLSNLD 166
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-216 |
1.55e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.73 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSF----GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDfLSKDSGSVLWDG-------------- 62
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRmrfddidllrlspr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 63 --HTLSGKDYNTIGYLPEErGLYPKVTIENQLL-----------FFASLRGKSKQEIapkidEWMEKFQVKGKKtDKVKS 129
Cdd:PRK15093 82 erRKLVGHNVSMIFQEPQS-CLDPSERVGRQLMqnipgwtykgrWWQRFGWRKRRAI-----ELLHRVGIKDHK-DAMRS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 130 ----LSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRN 204
Cdd:PRK15093 155 fpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|..
gi 498433885 205 GETVLNGKVHEI 216
Cdd:PRK15093 235 GQTVETAPSKEL 246
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-217 |
1.66e-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: 52.61 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHtlsgkdyntIGYLPEERGLYPKvTIENQLLF-- 94
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---------ISFSPQTSWIMPG-TIKDNIIFgl 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 95 -FASLRGKSKQEiAPKIDEWMEKFQVKGKKT--DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVN-AELLKN 170
Cdd:TIGR01271 512 sYDEYRYTSVIK-ACQLEEDIALFPEKDKTVlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEIFES 590
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498433885 171 GIIELKEKGSCVIFSShNMDNVEKiCDHLIMLRNGETVLNGKVHEIR 217
Cdd:TIGR01271 591 CLCKLMSNKTRILVTS-KLEHLKK-ADKILLLHEGVCYFYGTFSELQ 635
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-190 |
1.00e-06 |
|
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: 49.08 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 12 GSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDS----GSVLWDGHTLSgKDYNTIGYLPEerglypKVT 87
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGdiqiDGVSWNSVPLQ-KWRKAFGVIPQ------KVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 88 IenqllFFASLR------GK-SKQEIAPKIDE-----WMEKF--QVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVIL 153
Cdd:cd03289 88 I-----FSGTFRknldpyGKwSDEEIWKVAEEvglksVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 498433885 154 DEPFSGLDPVNAELLKNgiiELKE--KGSCVIFSSHNMD 190
Cdd:cd03289 163 DEPSAHLDPITYQVIRK---TLKQafADCTVILSEHRIE 198
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
3-190 |
1.08e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 3 QVEKLSKSFG------SYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGS---VLWDGHtlSGKDYNTI 73
Cdd:COG2401 26 RVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAgcvDVPDNQ--FGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 74 GYLPEERGLYPKVTIENQL------LFFAslrgkskqeiapkidewmekfqvkgkktdKVKSLSKGNQQKVQLISTLIHE 147
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAVglsdavLWLR-----------------------------RFKELSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498433885 148 PKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMD 190
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYD 198
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-211 |
1.27e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTtfrlILDFLSK-------DSGSVLWDGHTLSGKDYNTIGYLPEERGLYPKVTIE 89
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTT----LLNVLAErvttgviTGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLLFFASLRGKSKQEIAPK---IDEWMEKFQVK------------GKKTDKVKSLSKGnqqkVQLIStlihEPKLVI-L 153
Cdd:TIGR00956 855 ESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEMEsyadavvgvpgeGLNVEQRKRLTIG----VELVA----KPKLLLfL 926
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 154 DEPFSGLDPVNA----ELLKNgiieLKEKGSCVIFSSHN-----MDNVEKIcdhLIMLRNGETVLNG 211
Cdd:TIGR00956 927 DEPTSGLDSQTAwsicKLMRK----LADHGQAILCTIHQpsailFEEFDRL---LLLQKGGQTVYFG 986
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-168 |
1.48e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 49.42 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKAL-DDMTFTIEDGKILGLIGQNGAGKTTTFRLIldflskdSGsvLWD-GhtlSGkdynTIGYLPE 78
Cdd:COG4178 362 ALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAI-------AG--LWPyG---SG----RIARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERGLY-------PKVTIENQLLFFASLRGKSKQEI------------APKIDE---WmekfqvkgkktDKVksLSKGNQQ 136
Cdd:COG4178 426 ARVLFlpqrpylPLGTLREALLYPATAEAFSDAELrealeavglghlAERLDEeadW-----------DQV--LSLGEQQ 492
|
170 180 190
....*....|....*....|....*....|..
gi 498433885 137 KVQLISTLIHEPKLVILDEPFSGLDPVNAELL 168
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-217 |
3.21e-06 |
|
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: 47.54 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHtlsgkdyntIGYLPEERGLYPKvTIENQLLF-- 94
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---------ISFSSQFSWIMPG-TIKENIIFgv 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 95 -FASLRGKSKQEiAPKIDEWMEKFQVKGKKT--DKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD-PVNAELLKN 170
Cdd:cd03291 123 sYDEYRYKSVVK-ACQLEEDITKFPEKDNTVlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvFTEKEIFES 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498433885 171 GIIELKEKGSCVIFSShNMDNVeKICDHLIMLRNGETVLNGKVHEIR 217
Cdd:cd03291 202 CVCKLMANKTRILVTS-KMEHL-KKADKILILHEGSSYFYGTFSELQ 246
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
115-216 |
4.47e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 115 EKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEK 194
Cdd:PRK10938 121 QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPD 200
|
90 100
....*....|....*....|..
gi 498433885 195 ICDHLIMLRNGETVLNGKVHEI 216
Cdd:PRK10938 201 FVQFAGVLADCTLAETGEREEI 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-187 |
5.91e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 10 SFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFR------------------LILDFLSKD-----SGSVlWD----- 61
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKilngevllddgriiyeqdLIVARLQQDpprnvEGTV-YDfvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 62 ----GHTLsgKDYNTIGYL----PEERGLypkvtieNQLlffASLrgkskQEI---------APKIDEWMEKFQVKGKKt 124
Cdd:PRK11147 91 ieeqAEYL--KRYHDISHLvetdPSEKNL-------NEL---AKL-----QEQldhhnlwqlENRINEVLAQLGLDPDA- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498433885 125 dKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGiieLKEKGSCVIFSSH 187
Cdd:PRK11147 153 -ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGF---LKTFQGSIIFISH 211
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
129-202 |
1.21e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 1.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 129 SLSKGNQQKVQLISTLIH---EPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMdNVEKICDHLIML 202
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVADYVLEL 884
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-189 |
1.28e-05 |
|
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: 45.82 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 25 EDGKILGLIGQNGAGKTTTFRLILD----FLSKDSGSVLWDGHTLSGKDYNTIGYLPEERGLYPKVTIENQL--LFFASL 98
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpNLGKFDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYvdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 99 RGK-----SKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLD---PVNAELLkn 170
Cdd:cd03236 104 KGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqRLNAARL-- 181
|
170
....*....|....*....
gi 498433885 171 gIIELKEKGSCVIFSSHNM 189
Cdd:cd03236 182 -IRELAEDDNYVLVVEHDL 199
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-200 |
2.69e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSV--------LWDGHTLSGKDYNTIGYL----PEERGLYP 84
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtfpgnwqlAWVNQETPALPQPALEYVidgdREYRQLEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 85 KVTIENQL---LFFASLRGKskqeiAPKIDEWMEKFQVKG----------KKTDKVKSLSKGNQQKVQLISTLIHEPKLV 151
Cdd:PRK10636 97 QLHDANERndgHAIATIHGK-----LDAIDAWTIRSRAASllhglgfsneQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498433885 152 ILDEPFSGLDPVNAELLKNGiieLKEKGSCVIFSSHNMDNVEKICDHLI 200
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKW---LKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
90-188 |
3.01e-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: 44.69 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 90 NQLLFFASLRGKSKQEIAPKIDEWMEKFQVKGKKTDKVK----SLSKGNQQKVQLISTLI---HEPKLVILDEPFSGLDP 162
Cdd:pfam13304 193 KLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElpafELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHP 272
|
90 100
....*....|....*....|....*.
gi 498433885 163 VNAELLKNGIIELKEKGSCVIFSSHN 188
Cdd:pfam13304 273 KLLRRLLELLKELSRNGAQLILTTHS 298
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
126-209 |
4.27e-05 |
|
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: 43.08 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 126 KVKSLSKGNQQKVQLISTLIHEPK--LVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDnVEKICDHLIML- 202
Cdd:cd03238 84 KLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD-VLSSADWIIDFg 162
|
90
....*....|.
gi 498433885 203 ----RNGETVL 209
Cdd:cd03238 163 pgsgKSGGKVV 173
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-203 |
4.41e-05 |
|
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: 42.75 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 27 GKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLW-DGHTLSGKDYNTIGYLPEERGLYPKVTIENQLLFFASLRGkskqe 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 106 iapkidewmekfqvkgkktdkvkslskgnqqkvqlistliHEPKLVILDEPFSGLDPVNAELL------KNGIIELKEKG 179
Cdd:smart00382 77 ----------------------------------------LKPDVLILDEITSLLDAEQEALLllleelRLLLLLKSEKN 116
|
170 180
....*....|....*....|....
gi 498433885 180 SCVIFSSHnmdNVEKICDHLIMLR 203
Cdd:smart00382 117 LTVILTTN---DEKDLGPALLRRR 137
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-216 |
1.49e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.51 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKD--------SGSVLWDGHTLSGKDYNT 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 73 IGYLpeeRGLYPKVTienQLLFFASLR--------------GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKV 138
Cdd:PRK13547 81 LARL---RAVLPQAA---QPAFAFSAReivllgrypharraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 139 QLISTL---------IHEPKLVILDEPFSGLDPVNAELLKNGIIEL-KEKGSCVIFSSHNMDNVEKICDHLIMLRNGETV 208
Cdd:PRK13547 155 QFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
....*...
gi 498433885 209 LNGKVHEI 216
Cdd:PRK13547 235 AHGAPADV 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-206 |
1.58e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 19 DMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLW-DGHTLsgKDYN------TIGYLPEERGLYPKvTIENQ 91
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNL--KDINlkwwrsKIGVVSQDPLLFSN-SIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 92 LLF-------------------FASLRGKSKQ-----EIAPKIDEWM------EKFQVK--------------GKKT--- 124
Cdd:PTZ00265 480 IKYslyslkdlealsnyynedgNDSQENKNKRnscraKCAGDLNDMSnttdsnELIEMRknyqtikdsevvdvSKKVlih 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 125 -------DKVKS--------LSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELK-EKGSCVIFSSHN 188
Cdd:PTZ00265 560 dfvsalpDKYETlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHR 639
|
250
....*....|....*...
gi 498433885 189 MDNVeKICDHLIMLRNGE 206
Cdd:PTZ00265 640 LSTI-RYANTIFVLSNRE 656
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-216 |
1.89e-04 |
|
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: 43.01 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGhtlsgkdynTIGYLPEERGLYPKVTIENqLLFFA 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------SVAYVPQQAWIQNDSLREN-ILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 97 SLRGKSKQ------------EIAPKIDewmekfqvKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVN 164
Cdd:TIGR00957 724 ALNEKYYQqvleacallpdlEILPSGD--------RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498433885 165 AELLKNGIIELKE--KGSCVIFSSHNMDNVEKIcDHLIMLRNGETVLNGKVHEI 216
Cdd:TIGR00957 796 GKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQEL 848
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
5-68 |
2.39e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 2.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498433885 5 EKLSKSFGSYKALDDMTfTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLSGK 68
Cdd:cd03222 4 PDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK 66
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
129-202 |
2.69e-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: 42.31 E-value: 2.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498433885 129 SLSKGNQQKVQLISTLIHE---PKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDnVEKICDHLIML 202
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD-VIKTADYIIDL 904
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-66 |
3.52e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.01 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 498433885 16 ALDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSKDSGSVLWDGHTLS 66
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT 380
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-161 |
3.61e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 23 TIEDGKILGLIGQNGAGKTTTFRlIL---------DFLSKDS---------GSVLWDGHT-LSGKDYNTIgYLPEERGLY 83
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVK-ILsgelipnlgDYEEEPSwdevlkrfrGTELQNYFKkLYNGEIKVV-HKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 PKV---TIEnQLLFFASLRGkskqeiapKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGL 160
Cdd:PRK13409 173 PKVfkgKVR-ELLKKVDERG--------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
.
gi 498433885 161 D 161
Cdd:PRK13409 244 D 244
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-161 |
3.61e-04 |
|
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: 42.08 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 23 TIEDGKILGLIGQNGAGKTTTFRlIL------------------DFLSKDSGSVLWDgH--TLSGKDYNTIgYLPEERGL 82
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALK-ILsgelkpnlgdydeepswdEVLKRFRGTELQD-YfkKLANGEIKVA-HKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 83 YPKV---TIeNQLLFFASLRGKSKqEIAPK--IDEWMEKfqvkgkktdKVKSLSKGNQQKVQLISTLIHEPKLVILDEPF 157
Cdd:COG1245 172 IPKVfkgTV-RELLEKVDERGKLD-ELAEKlgLENILDR---------DISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
....
gi 498433885 158 SGLD 161
Cdd:COG1245 241 SYLD 244
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
129-213 |
5.75e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 129 SLSKGNQQKVQLISTLihEPKLV----ILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVeKICDHLIMLRN 204
Cdd:cd03270 137 TLSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI-RAADHVIDIGP 213
|
....*....
gi 498433885 205 GETVLNGKV 213
Cdd:cd03270 214 GAGVHGGEI 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-166 |
6.02e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 6 KLSKSFGSYKA-LDDMTFTIEDG-KIlGLIGQNGAGKTTTFRlILDFLSKDSgsvlwDGHTLSGKDYnTIGYLPEERGLY 83
Cdd:PRK11819 11 RVSKVVPPKKQiLKDISLSFFPGaKI-GVLGLNGAGKSTLLR-IMAGVDKEF-----EGEARPAPGI-KVGYLPQEPQLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 84 PKVTI-ENQLLFFASLRGKSKQ--EIAPKIDEWMEKFQV----KGKKTDK----------------------------VK 128
Cdd:PRK11819 83 PEKTVrENVEEGVAEVKAALDRfnEIYAAYAEPDADFDAlaaeQGELQEIidaadawdldsqleiamdalrcppwdakVT 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 498433885 129 SLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDpvnAE 166
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AE 197
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-211 |
1.41e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 1 MLQVEKLSKSFGSYKALDDMTFTIEDGKILGLIGQNGAGKTTTFRLIL--DFLSKDSGSVLWDGHTLSGKDyntigylPE 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELS-------PE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 79 ERG--------LYPkVTI---ENQLLFFASLRGKSKQEIAPKIDewmeKFQVKGKKTDKVKSL---------------SK 132
Cdd:PRK09580 74 DRAgegifmafQYP-VEIpgvSNQFFLQTALNAVRSYRGQEPLD----RFDFQDLMEEKIALLkmpedlltrsvnvgfSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 133 GNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNMDNVEKI-CDHLIMLRNGETVLNG 211
Cdd:PRK09580 149 GEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-250 |
1.66e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 17 LDDMTFTIEDGKILGLIGQNGAGKTTTFRLILDFLSK-DSGSVLWDGhtlsgkdynTIGYLPEERGLYpKVTIENQLLF- 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRG---------SVAYVPQVSWIF-NATVRENILFg 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 95 --FASLR-GKSKQEIAPKIDEWMEKFQVKGKKTDKVKSLSKGNQQKVQLISTLIHEPKLVILDEPFSGLDPVNAELLKNG 171
Cdd:PLN03232 703 sdFESERyWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDS 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 172 II--ELKEKGSCVIFSS-HNMDNVEKIcdhlIMLRNGetvlngkvhEIRESFGRSKLYLDSHLTKQELEAfAGVHTVTQK 248
Cdd:PLN03232 783 CMkdELKGKTRVLVTNQlHFLPLMDRI----ILVSEG---------MIKEEGTFAELSKSGSLFKKLMEN-AGKMDATQE 848
|
..
gi 498433885 249 ED 250
Cdd:PLN03232 849 VN 850
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-215 |
7.07e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498433885 127 VKSLSKGNQQKVQLISTLIHEPKLV--ILDEPFSGLDPVNAELLKNGIIELKEKGSCVIFSSHNmDNVEKICDHLI---- 200
Cdd:PRK00635 474 LATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIdigp 552
|
90
....*....|....*..
gi 498433885 201 --MLRNGETVLNGKVHE 215
Cdd:PRK00635 553 gaGIFGGEVLFNGSPRE 569
|
|
| |
