|
Name |
Accession |
Description |
Interval |
E-value |
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
3-237 |
4.67e-105 |
|
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: 303.44 E-value: 4.67e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF 82
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:TIGR03864 81 QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 163 VGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHGG-DLGSAFTRLT 237
Cdd:TIGR03864 161 VGLDPASRAAITAHVRALARDQGLSVLWATHLVDEIEASDRLVVLHRGRVLADGAAAELRGATGGaDLEAAFLALT 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-237 |
4.15e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.82 E-value: 4.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 164 GLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEALSLEHggdLGSAFTRLT 237
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLcDRVAIIDKGRIVADGTPDELKARL---LEDVFLELT 231
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-228 |
3.04e-50 |
|
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: 164.26 E-value: 3.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 164 GLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEALSLEHGGD 228
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALcDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-221 |
4.26e-49 |
|
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: 160.61 E-value: 4.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEAL 221
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-212 |
1.24e-40 |
|
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: 137.14 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYhaalhglSrrqtglrvdaelarqalterrrervrelnGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03230 81 EPSLYENLTVRENLKL-------S-----------------------------GGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495290120 164 GLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPR-DDLLILHQGRL 212
Cdd:cd03230 125 GLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLcDRVAILNNGRI 173
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
13-228 |
2.66e-39 |
|
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: 137.91 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 13 YGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQQSTLDLDLS 92
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 93 VEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLA 172
Cdd:TIGR01188 83 GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 173 LNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALSLEHGGD 228
Cdd:TIGR01188 163 IWDYIRAL-KEEGVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPEELKRRLGKD 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-216 |
2.38e-35 |
|
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: 125.31 E-value: 2.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 162 SVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVqprdDLL-----ILHQGRLVASG 216
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEA----EALcdriaIMSDGKLRCIG 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-221 |
2.53e-35 |
|
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: 125.93 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVV 81
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLSVEQNLR-----YHAALHGLSRRqtglrvDAELARQAL-----TERRRERVRELNGGHRRRVEIARALLH 151
Cdd:COG1120 81 PQEPPAPFGLTVRELVAlgrypHLGLFGRPSAE------DREAVEEALertglEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 152 EPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAEAL 221
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-221 |
4.06e-34 |
|
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: 122.06 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRPALKQLGVV 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQStlDLDL---SVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:COG1122 81 FQNP--DDQLfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 159 DEASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEAL 221
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELaDRVIVLDDGRIVADGTPREV 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-216 |
1.90e-33 |
|
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: 119.99 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAaLLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 164 GLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPR-DDLLILHQGRLVASG 216
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-216 |
2.96e-33 |
|
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: 119.55 E-value: 2.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASG 216
Cdd:cd03259 160 ALDAKLREELREELKELQRELGITTIYVTHDQEEaLALADRIAVMNEGRIVQVG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-221 |
3.04e-33 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 120.30 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG---CSL-RTSVRPALKQLG 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLDLDLSVEQN----LRYHAALhglSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:cd03261 81 MLFQSGALFDSLTVFENvafpLREHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEAL 221
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-221 |
3.48e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 120.08 E-value: 3.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQL--- 78
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 -GVVFQQSTL-DlDLSVEQN----LRYHaalHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHE 152
Cdd:COG1127 84 iGMLFQGGALfD-SLTVFENvafpLREH---TDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEAL 221
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-221 |
1.35e-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: 118.44 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQR-----GDIRVGG---CSLRTSVRPAL 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGkdiYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTLdLDLSVEQNLRYHAALHGLSRRqtglRVDAELARQALTE-------RRRERVRELNGGHRRRVEIARA 148
Cdd:cd03260 81 RRVGMVFQKPNP-FPGSIYDNVAYGLRLHGIKLK----EELDERVEEALRKaalwdevKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 149 LLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREhnISVLWTTHLLDEVQpR--DDLLILHQGRLVASGQAEAL 221
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAA-RvaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-229 |
2.71e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslrTSVRPALKQLGV 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLD--LSVEQ----NLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPS 154
Cdd:COG1121 80 VPQRAEVDWDfpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 155 LLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASG------QAEALSLEHGGD 228
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGppeevlTPENLSRAYGGP 238
|
.
gi 495290120 229 L 229
Cdd:COG1121 239 V 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-216 |
5.67e-32 |
|
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: 116.16 E-value: 5.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRqtglRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 164 GLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASG 216
Cdd:cd03268 156 GLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-198 |
1.16e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 115.27 E-value: 1.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLsrRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 495290120 164 GLDPASRLALNQHIRSLCREHNIsVLWTTHLLDEV 198
Cdd:COG4133 161 ALDAAGVALLAELIAAHLARGGA-VLLTTHQPLEL 194
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-216 |
1.22e-31 |
|
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: 115.32 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVrpalKQLGVVFQQ 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 85 STLDLD--LSVEQ----NLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:cd03235 77 RSIDRDfpISVRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 159 DEASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-216 |
5.70e-31 |
|
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: 114.35 E-value: 5.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 13 YGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF-QQSTLDLDL 91
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 92 SVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRL 171
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495290120 172 ALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASG 216
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-197 |
6.51e-31 |
|
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: 113.72 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYG----QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslrTSVRPALKQLG 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 495290120 160 EASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE 197
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDE 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-229 |
9.20e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 114.73 E-value: 9.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRPALKQL 78
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLsEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQ-------STL--DLDLSVEQNlryhaalhGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARAL 149
Cdd:PRK13635 84 GMVFQNpdnqfvgATVqdDVAFGLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 150 LHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALsLEHGGDL 229
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI-FKSGHML 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-216 |
1.69e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 112.37 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRpalKQLGVVFQ 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 164 GLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASG 216
Cdd:cd03269 158 GLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELcDRVLLLNKGRAVLYG 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
1.83e-30 |
|
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: 113.60 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRP-ALKQLG 79
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPhRIARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VV--FQQSTLDLDLSVEQNLR--YHAA-----LHGLSRRQTGLRVDAELARQA--------LTERRRERVRELNGGHRRR 142
Cdd:COG0411 81 IArtFQNPRLFPELTVLENVLvaAHARlgrglLAALLRLPRARREEREARERAeellervgLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 143 VEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVqpR---DDLLILHQGRLVASG 216
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLV--MglaDRIVVLDFGRVIAEG 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
2.01e-30 |
|
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: 111.37 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVFQ 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 qstldldlsveqnlryhaALhglsrRQTGLrvdAELARQALTerrrervrELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03214 81 ------------------AL-----ELLGL---AHLADRPFN--------ELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASG 216
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-220 |
2.20e-30 |
|
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: 112.53 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRP-ALKQLGVV- 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPhEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 -FQQSTLDLDLSVEQNLR--YHAALHGLSRRQTGLRVDAELARQA--------LTERRRERVRELNGGHRRRVEIARALL 150
Cdd:cd03219 80 tFQIPRLFPELTVLENVMvaAQARTGSGLLLARARREEREARERAeellervgLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEA 220
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLaDRVTVLDQGRVIAEGTPDE 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-211 |
5.61e-30 |
|
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: 109.97 E-value: 5.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG---CSLRTSVRPALKQLGV 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedlTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYhaalhGLSrrqtglrvdaelarqalterrrervrelnGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL-----GLS-----------------------------GGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495290120 161 ASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGR 211
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
6.31e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 112.11 E-value: 6.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAY----GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslrTSVRPALK 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQQSTLdLD-LSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:COG1116 81 DRGVVFQEPAL-LPwLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE 197
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDE 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-221 |
6.63e-30 |
|
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: 116.16 E-value: 6.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQ---RGDIRVGGCSLRT-SVRPALK 76
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLElSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQQSTLDLD-LSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:COG1123 84 RIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEAL 221
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-227 |
1.12e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.39 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF 82
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 163 VGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEALSLEHGG 227
Cdd:PRK13536 201 TGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLcDRLCVLEAGRKIAEGRPHALIDEHIG 265
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-216 |
1.70e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 110.15 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY----GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLG 79
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 160 EASVGLDPASRLALNQHIRSLCREHNiSVLWTTHLLDEVQPR-DDLLILHQGRLVASG 216
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLcDRVVVLHRGRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-212 |
2.25e-29 |
|
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: 109.50 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQ----REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-------RTSVR 72
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 73 paLKQLGVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHE 152
Cdd:cd03255 81 --RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRL 212
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-221 |
2.72e-29 |
|
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: 109.94 E-value: 2.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF- 82
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 -QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 162 SVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAEAL 221
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVREtLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-211 |
2.86e-29 |
|
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: 107.85 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYG--QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGV 80
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLryhaalhgLSrrqtglrvdaelarqalterrrervrelnGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:cd03228 81 VPQDPFL-FSGTIRENI--------LS-----------------------------GGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495290120 161 ASVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGR 211
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-219 |
6.12e-29 |
|
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: 108.90 E-value: 6.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF- 82
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 -QQSTLDLDLSVEQNLRyhAAL---HGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:TIGR04406 82 pQEASIFRKLTVEENIM--AVLeirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 159 DEASVGLDPASRLALNQHIRSLcREHNISVLWTTH----LLDEVqprDDLLILHQGRLVASGQAE 219
Cdd:TIGR04406 160 DEPFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHnvreTLDIC---DRAYIISDGKVLAEGTPA 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-216 |
3.41e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVV 81
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELaRRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL--- 158
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPprw 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 159 ---DEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLD-EVQPRDDLLILHQGRLVASG 216
Cdd:PRK13548 162 lllDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-211 |
3.74e-28 |
|
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: 104.63 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVFQ 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QStldldlsveqnlryhaalhglsrrqtglrvdaelarqalterrrervrelnGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd00267 81 LS---------------------------------------------------GGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 495290120 164 GLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVQP-RDDLLILHQGR 211
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-226 |
5.00e-28 |
|
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: 111.40 E-value: 5.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLG 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLdLDLSVEQNLRY----------HAALhglsrRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARAL 149
Cdd:COG4987 413 VVPQRPHL-FDTTLRENLRLarpdatdeelWAAL-----ERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 150 LHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-218 |
5.93e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.90 E-value: 5.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT---SVRPAL-KQL 78
Cdd:COG2884 2 IRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrREIPYLrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 159 DEASVGLDPASRLALNQHIRSLCREhNISVLWTTH---LLDEVQPRddLLILHQGRLVASGQA 218
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHdleLVDRMPKR--VLELEDGRLVRDEAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-211 |
8.86e-28 |
|
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: 105.24 E-value: 8.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQLGVV 81
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDL-DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:cd03225 81 FQNPDDQFfGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495290120 161 ASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVQPR-DDLLILHQGR 211
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELaDRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-221 |
2.91e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.84 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE-----ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQL 78
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 ----GVVFQ--QSTLDLDLSVEQNLRYHAALHG-LSRRQTGLRVDAELARQALTERRRERV-RELNGGHRRRVEIARALL 150
Cdd:COG1123 341 rrrvQMVFQdpYSSLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADRYpHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVqpR---DDLLILHQGRLVASGQAEAL 221
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVV--RyiaDRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-148 |
6.52e-27 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 101.19 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVFQQSTLDLDLSVEQNL 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 98 RYHAALHGLSRRQTGLRVDAELARQALTERR----RERVRELNGGHRRRVEIARA 148
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARA 135
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-226 |
7.56e-27 |
|
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: 107.92 E-value: 7.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGV 80
Cdd:COG4988 336 SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWrRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLRY----------HAALhglsrRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:COG4988 416 VPQNPYL-FAGTIRENLRLgrpdasdeelEAAL-----EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-225 |
1.21e-26 |
|
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: 103.03 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQL---- 78
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLDLDLSVEQN-----LRYHAALHGLSRRQTglRVDAELARQALTE-----RRRERVRELNGGHRRRVEIARA 148
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFP--KEEKQRALAALERvglldKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 149 LLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLI-LHQGRLVASGQAEALSLEH 225
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVgLKDGRIVFDGPPAELTDEV 236
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-221 |
2.00e-26 |
|
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: 103.30 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYG-----QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQL 78
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 ----GVVFQQSTLDL-DLSVE-------QNLryhaalhGLSRRQTGLRVDAELARQALTERRRERV-RELNGGHRRRVEI 145
Cdd:TIGR04521 81 rkkvGLVFQFPEHQLfEETVYkdiafgpKNL-------GLSEEEAEERVKEALELVGLDEEYLERSpFELSGGQMRRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 146 ARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEAL 221
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYaDRVIVMHKGKIVLDGTPREV 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-226 |
4.44e-26 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 101.54 E-value: 4.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR----TSVRpalKQL 78
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevtlDSLR---RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLdLDLSVEQNLRYHaalhglsrrqtglRVDA------ELARQALTERRRERV------------RELNGGHR 140
Cdd:cd03253 78 GVVPQDTVL-FNDTIGYNIRYG-------------RPDAtdeeviEAAKAAQIHDKIMRFpdgydtivgergLKLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 141 RRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEA 220
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEE 221
|
....*.
gi 495290120 221 LSLEHG 226
Cdd:cd03253 222 LLAKGG 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-221 |
5.52e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.96 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF 82
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 163 VGLDPASRLALNQHIRSLCREHNiSVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEAL 221
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLcDRLCVIEEGRKIAEGAPHAL 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-219 |
6.26e-26 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.73 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVF 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL---- 158
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGgprw 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 159 ---DEASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLD-EVQPRDDLLILHQGRLVASGQAE 219
Cdd:COG4559 162 lflDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPE 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-221 |
2.03e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.44 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREAlrQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQN--LRYHAALHgLSRRQTgLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:COG3840 79 ENNLFPHLTVAQNigLGLRPGLK-LTAEQR-AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 162 SVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEAL 221
Cdd:COG3840 157 FSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-227 |
3.14e-25 |
|
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: 103.76 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR----TSVRpalK 76
Cdd:COG2274 473 DIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqidpASLR---R 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQQSTLdLDLSVEQNLRYHAALHGLSR-----RQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLH 151
Cdd:COG2274 550 QIGVVLQDVFL-FSGTIRENITLGDPDATDEEiieaaRLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 152 EPSLLLLDEASVGLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALsLEHGG 227
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEEL-LARKG 701
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
6.77e-25 |
|
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: 98.62 E-value: 6.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTR-LYDLQRGDIRVGGCSL-RTSVRPALKQL 78
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRgGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVfqQSTLDLDLSVEQNLR------YHAALhGLSRRQTglRVDAELARQALTE-----RRRERVRELNGGHRRRVEIAR 147
Cdd:COG1119 81 GLV--SPALQLRFPRDETVLdvvlsgFFDSI-GLYREPT--DEQRERARELLELlglahLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 148 ALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEAL 221
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEV 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-227 |
1.08e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.78 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT----SVRpalKQ 77
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDltleSLR---RQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 LGVVFQQSTLdLDLSVEQNLRY---------------HAALHGLSRRQT-GLrvDAELARQALTerrrervreLNGGHRR 141
Cdd:COG1132 416 IGVVPQDTFL-FSGTIRENIRYgrpdatdeeveeaakAAQAHEFIEALPdGY--DTVVGERGVN---------LSGGQRQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 142 RVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
....*.
gi 495290120 222 sLEHGG 227
Cdd:COG1132 562 -LARGG 566
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-221 |
1.18e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.39 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 13 YGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLydLQ--RGDIRVGGC--SLRtsvRPA-LKQLGVVF-QQST 86
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVptSGEVRVLGYvpFKR---RKEfARRIGVVFgQRSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 87 LDLDLSVEQNLRYHAALHGLSRRQTGLRVD--AEL----------ARQalterrrervreLNGGHRRRVEIARALLHEPS 154
Cdd:COG4586 107 LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDelVELldlgelldtpVRQ------------LSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 155 LLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQ---PRddLLILHQGRLVASGQAEAL 221
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEalcDR--VIVIDHGRIIYDGSLEEL 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-216 |
1.25e-24 |
|
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: 96.98 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 20 RQVSFNL-----AAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTS-----VRPALKQLGVVFQQSTLDL 89
Cdd:cd03297 9 RLPDFTLkidfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinLPPQQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 90 DLSVEQNLRYhaALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPAS 169
Cdd:cd03297 89 HLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495290120 170 RLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASG 216
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-227 |
1.35e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 101.63 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR----TSVRpalKQ 77
Cdd:PRK11176 342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdytlASLR---NQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 LGVVFQQSTLDLDlSVEQNLRYhAALHGLSRRQtgLRVDAELA---------RQALTERRRERVRELNGGHRRRVEIARA 148
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAY-ARTEQYSREQ--IEEAARMAyamdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARA 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 149 LLHEPSLLLLDEASVGLDPASRLALNQHIRSLcrEHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALsLEHGG 227
Cdd:PRK11176 495 LLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL-LAQNG 570
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-229 |
1.42e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.65 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQRE---ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRPALK 76
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQQSTLD-LDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:PRK13650 82 KIGMVFQNPDNQfVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALsLEHGGDL 229
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL-FSRGNDL 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-221 |
1.50e-24 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.79 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGV 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 161 ASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEvq-prDDLLILHQGRLVASGQAEAL 221
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEalalaDRIAVMNDGRIEQVGTPEEI 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-221 |
2.72e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG---CSLRTSVRpALKQ 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGediTHLPMHKR-ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 LGVVFQQSTLDLDLSVEQNLRyhAAL--HGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNIL--AVLelRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTH----LLDEVqprDDLLILHQGRLVASGQAEAL 221
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVLITDHnvreTLGIC---DRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-221 |
1.09e-23 |
|
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: 95.45 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQ-LGVV 81
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRkIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERV--RELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRypHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 160 EASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAEAL 221
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEaFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-236 |
1.14e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQ-LGV 80
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRnIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLRY----------------HAALHGLSRRQTGLRVDA-ELARQalterrrervreLNGGHRRRV 143
Cdd:PRK13657 414 VFQDAGL-FNRSIEDNIRVgrpdatdeemraaaerAQAHDFIERKPDGYDTVVgERGRQ------------LSGGERQRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 144 EIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcrEHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSl 223
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV- 557
|
250
....*....|...
gi 495290120 224 ehggDLGSAFTRL 236
Cdd:PRK13657 558 ----ARGGRFAAL 566
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-216 |
4.19e-23 |
|
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: 92.94 E-value: 4.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGqrEALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQN--LRYHAALHgLSRRQTGlRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:cd03298 78 ENNLFAHLTVEQNvgLGLSPGLK-LTAEDRQ-AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 162 SVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLI-LHQGRLVASG 216
Cdd:cd03298 156 FAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-216 |
5.62e-23 |
|
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: 92.70 E-value: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcSLRTSVRPALKQLGVVFQ 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-RDVTDLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVD--AELARqaLTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVRevAELLQ--IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 162 SVGLDPASRLALNQHIRSLCREHNISVLWTTHllDEVQPR---DDLLILHQGRLVASG 216
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTH--DQVEAMtmaDRIAVMNDGQIQQIG 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-226 |
6.60e-23 |
|
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: 93.06 E-value: 6.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVF 82
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLdLDLSVEQNLRYH----------------AALHGLSRRQTGLrvDAELARQAlterrrervRELNGGHRRRVEIA 146
Cdd:cd03254 84 QDTFL-FSGTIMENIRLGrpnatdeevieaakeaGAHDFIMKLPNGY--DTVLGENG---------GNLSQGERQLLAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 147 RALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcrEHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-221 |
1.58e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 92.17 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQ----REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQ 77
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 LGVVFQQSTLDLD--LSVEQNLRYHAALHGLSRRQTglRVDAELARQALTERRRERV-RELNGGHRRRVEIARALLHEPS 154
Cdd:COG1124 81 VQMVFQDPYASLHprHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSFLDRYpHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 155 LLLLDEASVGLDPASR---LALNQHIRslcREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEAL 221
Cdd:COG1124 159 LLLLDEPTSALDVSVQaeiLNLLKDLR---EERGLTYLFVSHDLAVVAHLcDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-216 |
2.23e-22 |
|
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: 91.49 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR----EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL----RTSVRPAL 75
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 156 LLLDEASVGLDPA---SRLALnqhIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASG 216
Cdd:cd03258 162 LLCDEATSALDPEttqSILAL---LRDINRELGLTIVLITHEMEVVKRIcDRVAVMEKGEVVEEG 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-216 |
3.59e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.17 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLY---DLQRGDIRVGGCSLRT-SVRPAL 75
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAkTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTLD-LDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPS 154
Cdd:PRK13640 84 EKVGIVFQNPDNQfVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 155 LLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-221 |
5.10e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 92.86 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 21 QVSFNLAAGRFAALLGPNGAGKSTL---IALLTRLydlQRGDIRVGG-----CSLRTSVRPALKQLGVVFQQSTLDLDLS 92
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLlraIAGLERP---DSGRIRLGGevlqdSARGIFLPPHRRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 93 VEQNLRYhaALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLA 172
Cdd:COG4148 94 VRGNLLY--GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495290120 173 LNQHIRSLCREHNISVLWTTHLLDEVQpR--DDLLILHQGRLVASGQAEAL 221
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVA-RlaDHVVLLEQGRVVASGPLAEV 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-227 |
7.83e-22 |
|
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: 89.98 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYG--QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGV 80
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLrRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLRYhaALHGLSRRQtgLRVDAELAR---------QALTERRRERVRELNGGHRRRVEIARALLH 151
Cdd:cd03251 81 VSQDVFL-FNDTVAENIAY--GRPGATREE--VEEAARAANahefimelpEGYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 152 EPSLLLLDEASVGLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALsLEHGG 227
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL-LAQGG 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-221 |
9.70e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.43 E-value: 9.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVV-- 81
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLSVEQNL-----RYHAA--LHGLSRRQTGLRVDAE--------LARQALTERRRERVRELNGGHRRRVEIA 146
Cdd:PRK11300 86 FQHVRLFREMTVIENLlvaqhQQLKTglFSGLLKTPAFRRAESEaldraatwLERVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 147 RALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEAL 221
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-222 |
1.47e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQ----- 77
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAirllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 --LGVVFQQSTLDLDLSVEQNLrYHAALH--GLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEP 153
Cdd:COG4161 82 qkVGMVFQQYNLWPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 154 SLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLD---EVQPRddLLILHQGRLVASGQAEALS 222
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEfarKVASQ--VVYMEKGRIIEQGDASHFT 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-221 |
2.45e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRpalKQLGVVF 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR---RRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 163 VGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVQpR--DDLLILHQGRLVASGQAEAL 221
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVE-ElcDRIVIINKGRKVLSGSVDEI 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-215 |
3.30e-21 |
|
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: 86.71 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQ-LGVV 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAgIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQqstldldlsveqnlryhaalhglsrrqtglrvdaelarqalterrrervreLNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 162 SVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVAS 215
Cdd:cd03216 110 TAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-227 |
3.37e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGV 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYHAALHGLSR-----RQTGLR--------VDA---ELARQalterrrervreLNGGHRRRVE 144
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAAPNASDEAlievlQQVGLEklleddkgLNAwlgEGGRQ------------LSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 145 IARALLHEPSLLLLDEASVGLDPASRlalnQHIRSLCREH--NISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALS 222
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETE----RQILELLAEHaqNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELL 561
|
....*
gi 495290120 223 LEHGG 227
Cdd:PRK11160 562 AQQGR 566
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-224 |
3.83e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.62 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQ-LGV 80
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAAgIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNL---RYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLL 157
Cdd:COG1129 84 IHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 158 LDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQpR--DDLLILHQGRLVASGQAEALSLE 224
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVF-EiaDRVTVLRDGRLVGTGPVAELTED 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
5.40e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.71 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRPALKQL 78
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLDL-DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLL 157
Cdd:PRK13652 81 GLVFQNPDDQIfSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 158 LDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDD-LLILHQGRLVASGQAEALSLE 224
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-168 |
9.36e-21 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 86.69 E-value: 9.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG---CSLRTSVRPALKQ-LGVVFQQSTLDLDLSV 93
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvSDLRGRAIPYLRRkIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 94 EQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPA 168
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-216 |
9.59e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.12 E-value: 9.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRPALKQLG 79
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQStlD---LDLSVEQNLRYhaalhGLSRRqtglRVD--------AELARQA-LTERRRERVRELNGGHRRRVEIAR 147
Cdd:PRK13632 87 IIFQNP--DnqfIGATVEDDIAF-----GLENK----KVPpkkmkdiiDDLAKKVgMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 148 ALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-221 |
1.00e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.98 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcSLRTSVRPALKQLGV 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG-RDVTDLPPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVD--AE-------LARQALTerrrervreLNGGHRRRVEIARALLH 151
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVReaAEllgledlLDRKPKQ---------LSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 152 EPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHllDEVQPR---DDLLILHQGRLVASGQAEAL 221
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTH--DQVEAMtlaDRIAVMNDGRIQQVGTPEEL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-222 |
1.10e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQL---- 78
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAIrelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 ---GVVFQQSTLDLDLSVEQNLrYHAALH--GLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEP 153
Cdd:PRK11124 82 rnvGMVFQQYNLWPHLTVQQNL-IEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 154 SLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLD---EVQPRddLLILHQGRLVASGQAEALS 222
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEvarKTASR--VVYMENGHIVEQGDASCFT 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-227 |
1.21e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 90.16 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYG--QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQLGV 80
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLRYhaalhglSRRQTGLRVDAELARQA-------------LTERRRERVRELNGGHRRRVEIAR 147
Cdd:TIGR02203 411 VSQDVVL-FNDTIANNIAY-------GRTEQADRAEIERALAAayaqdfvdklplgLDTPIGENGVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 148 ALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLwtTHLLDEVQPRDDLLILHQGRLVASGQAEALsLEHGG 227
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI--AHRLSTIEKADRIVVMDDGRIVERGTHNEL-LARNG 559
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
14-235 |
1.37e-20 |
|
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: 87.70 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 14 GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQL-----GVVFQQSTLD 88
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkiSMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 89 LDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPA 168
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 169 SRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAEALSLEHGGDLGSAFTR 235
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEaLRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-216 |
1.48e-20 |
|
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: 85.44 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVV 81
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLdLDLSVEQNLryhaalhglsrrqtGLRvdaelarqalterrrervreLNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:cd03247 81 NQRPYL-FDTTLRNNL--------------GRR--------------------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 162 SVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-216 |
2.16e-20 |
|
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: 85.30 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 14 GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLT--RLYDLQRGDIRVGGCSL-RTSVRpalKQLGVVFQQSTLDLD 90
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLdKRSFR---KIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 91 LSVEQNLRYHAALHGLSrrqtglrvdaelarqalterrrervrelnGGHRRRVEIARALLHEPSLLLLDEASVGLDPASR 170
Cdd:cd03213 97 LTVRETLMFAAKLRGLS-----------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495290120 171 LALNQHIRSLCREhNISVLWTTHlldevQPR-------DDLLILHQGRLVASG 216
Cdd:cd03213 148 LQVMSLLRRLADT-GRTIICSIH-----QPSseifelfDKLLLLSQGRVIYFG 194
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-216 |
2.36e-20 |
|
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: 86.02 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY----GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL----RTSVRPAL 75
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTLDLD--LSVEQN----LRYHAALHGLSRRQTG---LRVDAELARQALTERRRErvreLNGGHRRRVEIA 146
Cdd:cd03257 82 KEIQMVFQDPMSSLNprMTIGEQiaepLRIHGKLSKKEARKEAvllLLVGVGLPEEVLNRYPHE----LSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 147 RALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASG 216
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIaDRVAVMYAGKIVEEG 228
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
3-227 |
3.64e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 88.72 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR----TSVRpalKQ 77
Cdd:COG5265 357 EVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdvtqASLR---AA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 LGVVFQQSTLDLDlSVEQNLRY---------------HAALHGLSRR-----QT-----GLRvdaelarqalterrrerv 132
Cdd:COG5265 434 IGIVPQDTVLFND-TIAYNIAYgrpdaseeeveaaarAAQIHDFIESlpdgyDTrvgerGLK------------------ 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 133 reLNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHnisvlwTT----HLLDEVQPRDDLLILH 208
Cdd:COG5265 495 --LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGR------TTlviaHRLSTIVDADEILVLE 566
|
250
....*....|....*....
gi 495290120 209 QGRLVASGQAEALsLEHGG 227
Cdd:COG5265 567 AGRIVERGTHAEL-LAQGG 584
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-221 |
3.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQ---VSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQLG 79
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLD-LDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:PRK13642 85 MVFQNPDNQfVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 159 DEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-216 |
4.36e-20 |
|
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: 85.37 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASG 216
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEaLTMSDRIAVMNKGKIQQIG 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-221 |
9.04e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.35 E-value: 9.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEAL 221
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-167 |
1.08e-19 |
|
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: 84.12 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL---KQLGV 80
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYhaAL---HGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLL 157
Cdd:cd03262 81 VFQQFNLFPHLTVLENITL--APikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170
....*....|
gi 495290120 158 LDEASVGLDP 167
Cdd:cd03262 159 FDEPTSALDP 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
1.09e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.17 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTS----VRpalK 76
Cdd:PRK13647 3 NIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnekwVR---S 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQqstlDLD-----LSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLH 151
Cdd:PRK13647 80 KVGLVFQ----DPDdqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 152 EPSLLLLDEASVGLDPASRLALNQHIRSLCREHNiSVLWTTHLLD-EVQPRDDLLILHQGRLVASGQAEALS 222
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-216 |
1.40e-19 |
|
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: 87.38 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 16 REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQQSTLDLDLSVEQ 95
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 96 NLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQ 175
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495290120 176 HIrsLCREHNISVLWTTHLLDEVQPRDD-LLILHQGRLVASG 216
Cdd:TIGR01257 1103 LL--LKYRSGRTIIMSTHHMDEADLLGDrIAIISQGRLYCSG 1142
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-193 |
1.43e-19 |
|
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: 83.18 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQtglrVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLwTTH 193
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLL-TTH 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-212 |
1.47e-19 |
|
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: 84.06 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 8 DLSFAYGQREA---LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVFQ 83
Cdd:cd03248 16 NVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLhSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLdLDLSVEQNLRYhaalhGLSRRQTGLRVDAELARQALTERRRERV----------RELNGGHRRRVEIARALLHEP 153
Cdd:cd03248 96 EPVL-FARSLQDNIAY-----GLQSCSFECVKEAAQKAHAHSFISELASgydtevgekgSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 154 SLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLwtTHLLDEVQPRDDLLILHQGRL 212
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVI--AHRLSTVERADQILVLDGGRI 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-221 |
2.56e-19 |
|
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: 83.54 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVF 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQN----LRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:cd03296 81 QHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 159 DEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAEAL 221
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEaLEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-207 |
3.48e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.84 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQLGVVF 82
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDlSVEQNLRYHAALHGLSRRQTGLRVDaeLARQALTERRRERV-RELNGGHRRRVEIARALLHEPSLLLLDEA 161
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495290120 162 SVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLIL 207
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-219 |
9.97e-19 |
|
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: 82.00 E-value: 9.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREaLRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVD--AE-------LARQALTerrrervreLNGGHRRRVEIARALLHEPS 154
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLeiAEmlgidhlLNRKPET---------LSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 155 LLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAE 219
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPE 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
1.13e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.49 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREA--LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDI-----RVGGCSLRtSVRpa 74
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFE-KLR-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 75 lKQLGVVFQQ-------STLDLDLS--VEQNLRYHAALHGlsrrqtglRVDAELARQALTERRRERVRELNGGHRRRVEI 145
Cdd:PRK13648 83 -KHIGIVFQNpdnqfvgSIVKYDVAfgLENHAVPYDEMHR--------RVSEALKQVDMLERADYEPNALSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 146 ARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAE 219
Cdd:PRK13648 154 AGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
1.47e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL---KQLG 79
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevrKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQStlDLDL---SVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLL 156
Cdd:PRK13639 82 IVFQNP--DDQLfapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 157 LLDEASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVqP--RDDLLILHQGRLVASG 216
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLV-PvyADKVYVMSDGKIIKEG 219
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-221 |
2.00e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.09 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVG--GCSLRTSVRPALKQL 78
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLDLDLSVEQNLRyhAAL---HGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLM--AVLqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVREtLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
9-226 |
2.18e-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: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 9 LSFAYG--QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALK-QLGVVFQQS 85
Cdd:cd03252 6 VRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRrQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 86 TLdLDLSVEQNLRyhAALHGLSRRQtgLRVDAELA---------RQALTERRRERVRELNGGHRRRVEIARALLHEPSLL 156
Cdd:cd03252 86 VL-FNRSIRDNIA--LADPGMSMER--VIEAAKLAgahdfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 157 LLDEASVGLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-216 |
2.46e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.63 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQ-----REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL---RTSVRPAL 75
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTLDL-DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVR--ELNGGHRRRVEIARALLHE 152
Cdd:PRK13637 83 KKVGLVFQYPEYQLfEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASG 216
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQG 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-219 |
3.48e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 9 LSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG---CSLRTSVRPALK-QLGVVFQ 83
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiTRLKNREVPFLRrQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 164 GLDPasrlALNQHIRSLCREHN---ISVLWTTHLLDEVQPRD-DLLILHQGRLVASGQAE 219
Cdd:PRK10908 167 NLDD----ALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSyRMLTLSDGHLHGGVGGE 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-226 |
7.37e-18 |
|
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: 79.51 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQR---EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQLGV 80
Cdd:cd03249 2 EFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLRYhaalhGLSRRQTGLRVDAelARQA------------LTERRRERVRELNGGHRRRVEIARA 148
Cdd:cd03249 82 VSQEPVL-FDGTIAENIRY-----GKPDATDEEVEEA--AKKAnihdfimslpdgYDTLVGERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 149 LLHEPSLLLLDEASVGLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-193 |
8.91e-18 |
|
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: 81.95 E-value: 8.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGV 80
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWrDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLRYH---AALHGLSR--RQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:TIGR02857 401 VPQHPFL-FAGTIAENIRLArpdASDAEIREalERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*...
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHniSVLWTTH 193
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTH 515
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-221 |
1.06e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.37 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR---TSVRPALKQLGV 80
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYHAA-LHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 160 EASVGLDPASRLALNQHIRSLCREhNISVLWTTH---LLDEVQPRddLLILHQGRLVASGQAEAL 221
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHeigFAEKVASR--LIFIDKGRIAEDGDPQVL 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-219 |
1.17e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 79.31 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQR-----GDIRVGGCSLR------TSV 71
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPgarveGEILLDGEDIYdpdvdvVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 72 RpalKQLGVVFQQSTLdLDLSVEQNLRYHAALHGLSRRQ-------TGLR-------VDAELARQALterrrervrELNG 137
Cdd:COG1117 91 R---RRVGMVFQKPNP-FPKSIYDNVAYGLRLHGIKSKSeldeiveESLRkaalwdeVKDRLKKSAL---------GLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 138 GHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDevQPR---DDLLILHQGRLVA 214
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQ--QAArvsDYTAFFYLGELVE 233
|
....*
gi 495290120 215 SGQAE 219
Cdd:COG1117 234 FGPTE 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-236 |
1.29e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-----RTSVRPA--- 74
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhRRAVCPRiay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 75 LKQ-LGvvfqqSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEP 153
Cdd:NF033858 81 MPQgLG-----KNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 154 SLLLLDEASVGLDPASR---LALNQHIRSlcREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALsLEHGG--D 228
Cdd:NF033858 156 DLLILDEPTTGVDPLSRrqfWELIDRIRA--ERPGMSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAEL-LARTGadT 232
|
....*...
gi 495290120 229 LGSAFTRL 236
Cdd:NF033858 233 LEAAFIAL 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-210 |
1.29e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.31 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQrGDIRVGG---------CSLRTSVRP 73
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqniYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 74 ALKQLGVVFQQSTLdLDLSVEQNLRYHAALHGLSRR-------QTGLRvDAELARQaLTERRRERVRELNGGHRRRVEIA 146
Cdd:PRK14258 86 LRRQVSMVHPKPNL-FPMSVYDNVAYGVKIVGWRPKleiddivESALK-DADLWDE-IKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 147 RALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQG 210
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-216 |
1.31e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.89 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL---KQ 77
Cdd:PRK13636 4 YILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMklrES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 LGVVFQQSTLDL-DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLL 156
Cdd:PRK13636 84 VGMVFQDPDNQLfSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 157 LLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASG 216
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYcDNVFVMKEGRVILQG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-221 |
1.45e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQ-REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGC-SLRTSVRPALKQL-GV 80
Cdd:PRK13644 2 IRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdTGDFSKLQGIRKLvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQ-STLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:PRK13644 82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 160 EASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-221 |
1.51e-17 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 78.24 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRP-ALKQLGVVF 82
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPhERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDL--DLSVEQNLRyhAALHGLSRRQTGLRVDAELAR-QALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:cd03224 80 VPEGRRIfpELTVEENLL--LGAYARRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 160 EASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEAL 221
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIaDRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-216 |
2.34e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.01 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVG-----GCSLRTSVRPALKQLGVVFQ--QSTLdLD 90
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvsSTSKQKEIKPVRKKVGVVFQfpESQL-FE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 91 LSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERR-RERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPAS 169
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495290120 170 RLALNQHIRSLcREHNISVLWTTHLLDEVQPRDD-LLILHQGRLVASG 216
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADyVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
8-221 |
2.61e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.91 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 8 DLSFAYG-----QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVR-----PALKQ 77
Cdd:PRK13634 7 KVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklkPLRKK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 78 LGVVFQ--QSTLdLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERV-RELNGGHRRRVEIARALLHEPS 154
Cdd:PRK13634 87 VGIVFQfpEHQL-FEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSpFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 155 LLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-207 |
3.64e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 12 AYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslrtSVRPALkqlgvVFQQSTLD--L 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----GARVAY-----VPQRSEVPdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 90 DLSVEQNLRY----HAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGL 165
Cdd:NF040873 71 PLTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 495290120 166 DPASRLALNQHIRSLCREhNISVLWTTHLLDEVQPRDDLLIL 207
Cdd:NF040873 151 DAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-194 |
5.47e-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: 76.38 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL---RTSVRPALKQLGv 80
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqRDSIARGLLYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 vfQQSTLDLDLSVEQNLRYHAALHGLSrrqtglRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:cd03231 80 --HAPGIKTTLSVLENLRFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 495290120 161 ASVGLDPASRLALNQHIRSLCREHNISVLwTTHL 194
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVL-TTHQ 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-223 |
5.88e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 5.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRvggcslrtsvRPALKQLGV 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLD--LDLSVEQNLRYHAA------LHGLSRRQTGLRVDAELARqalterrrervreLNGGHRRRVEIARALLHE 152
Cdd:PRK09544 72 VPQKLYLDttLPLTVNRFLRLRPGtkkediLPALKRVQAGHLIDAPMQK-------------LSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSL 223
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPEVVSL 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-221 |
8.86e-17 |
|
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: 76.56 E-value: 8.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRP-ALKQLG 79
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPPhRIARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 V--------VFQqstldlDLSVEQNLRYhAALHGLSRRQTGLRVD---------AELARQalterrreRVRELNGGHRRR 142
Cdd:COG0410 80 IgyvpegrrIFP------SLTVEENLLL-GAYARRDRAEVRADLErvyelfprlKERRRQ--------RAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 143 VEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREhNISVlwtthLLDEVQPR------DDLLILHQGRLVASG 216
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTI-----LLVEQNARfaleiaDRAYVLERGRIVLEG 218
|
....*
gi 495290120 217 QAEAL 221
Cdd:COG0410 219 TAAEL 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-169 |
1.13e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQ-----RGDIRVGGCSL---RTSVRPAL 75
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTlDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQA-----LTERRRERVRELNGGHRRRVEIARALL 150
Cdd:PRK14239 86 KEIGMVFQQPN-PFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGAsiwdeVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170
....*....|....*....
gi 495290120 151 HEPSLLLLDEASVGLDPAS 169
Cdd:PRK14239 165 TSPKIILLDEPTSALDPIS 183
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-217 |
1.19e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.09 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYG-----QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTS-----VR 72
Cdd:PRK13649 2 GINLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 73 PALKQLGVVFQ--QSTLdLDLSVEQNLRYHAALHGLSRRqtglrvDAE-LARQALTERRRERVR------ELNGGHRRRV 143
Cdd:PRK13649 82 QIRKKVGLVFQfpESQL-FEETVLKDVAFGPQNFGVSQE------EAEaLAREKLALVGISESLfeknpfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 144 EIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDDLL-ILHQGRLVASGQ 217
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVyVLEKGKLVLSGK 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-219 |
1.35e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.42 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQ-----RGDIRVGGCSLRT-SVRP- 73
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpDVDPi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 74 -ALKQLGVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGL--RVDAELARQAL----TERRRERVRELNGGHRRRVEIA 146
Cdd:PRK14267 82 eVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELdeRVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 147 RALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNIsVLWTTHLLDEVQPRDDLLILHQGRLVASGQAE 219
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI-VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-216 |
2.04e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 75.39 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 16 REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYD---LQRGDIRVGGCSLRtsvrPAL--KQLGVVFQQSTLDLD 90
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEgggTTSGQILFNGQPRK----PDQfqKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 91 LSVEQNLRYHAALHG---LSRRQTGLRVDAELARQ-ALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLD 166
Cdd:cd03234 96 LTVRETLTYTAILRLprkSSDAIRKKRVEDVLLRDlALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 167 PASRLALNQHIRSLCREHNIsVLWTTHlldevQPR-------DDLLILHQGRLVASG 216
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRI-VILTIH-----QPRsdlfrlfDRILLLSSGEIVYSG 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-196 |
2.12e-16 |
|
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: 74.77 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 17 EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL---RTSVRPALKQLGVVFQQSTLDL-DLS 92
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDPDDQLfAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 93 VEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLA 172
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|....
gi 495290120 173 LNQHIRSLcREHNISVLWTTHLLD 196
Cdd:TIGR01166 166 MLAILRRL-RAEGMTVVISTHDVD 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-216 |
2.48e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.79 E-value: 2.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 9 LSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRPALKQLGVVFQQSTL 87
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 88 DLDLSVEQNL---RY-HAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK10253 93 PGDITVQELVargRYpHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASG 216
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQG 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-150 |
3.03e-16 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 75.03 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL---RTSVRPALKQLGV 80
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdsKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 81 VFQQSTLDLDLSVEQNLRYhaAL---HGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTL--APikvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-224 |
3.05e-16 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 74.87 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRP---ALKQLGV 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI-TKLPPherARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYHAALHGLSRRqtglRVDAELAR--QALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSR----KIPDEIYElfPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 159 DEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALSLE 224
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFArELADRYYVMERGRVVASGAGDELDED 222
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-95 |
3.06e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVFQ 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLAILRQ 82
|
90
....*....|..
gi 495290120 84 QSTLDLDLSVEQ 95
Cdd:COG4604 83 ENHINSRLTVRE 94
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-221 |
3.08e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL----RTSVRPALK 76
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQQSTLDLDLSVEQN----LRYHAALHGLSRRQT--------GLRVDAELarqalterrreRVRELNGGHRRRVE 144
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNvaypLREHTQLPAPLLHSTvmmkleavGLRGAAKL-----------MPSELSGGMARRAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 145 IARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEAL 221
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-119 |
3.51e-16 |
|
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: 74.88 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 13 YGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslrtSVRPALkQLGVVFqqstlDLDLS 92
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSSLL-GLGGGF-----NPELT 100
|
90 100 110
....*....|....*....|....*....|..
gi 495290120 93 VEQNLRYHAALHGLSRRQTGLRVD-----AEL 119
Cdd:cd03220 101 GRENIYLNGRLLGLSRKEIDEKIDeiiefSEL 132
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-119 |
3.94e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.12 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 13 YGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslRTSvrpALKQLGVVFQQstldlDLS 92
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVS---ALLELGAGFHP-----ELT 104
|
90 100 110
....*....|....*....|....*....|..
gi 495290120 93 VEQNLRYHAALHGLSRRQTGLRVD-----AEL 119
Cdd:COG1134 105 GRENIYLNGRLLGLSRKEIDEKFDeivefAEL 136
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-197 |
5.80e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslrTSVRPALKQLGVVF 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGPGAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|....*
gi 495290120 163 VGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE 197
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLWQETGKQVLLITHDIEE 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-219 |
6.34e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.67 E-value: 6.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQLGVVF 82
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRY----HAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARAllhepslLLL 158
Cdd:PRK11231 83 QHHLTPEGITVRELVAYgrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV-------LAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 159 DEASVGLD-PASRLALNQHIR--SLCREHN------ISVLwttHLLDEVQpR--DDLLILHQGRLVASGQAE 219
Cdd:PRK11231 156 DTPVVLLDePTTYLDINHQVElmRLMRELNtqgktvVTVL---HDLNQAS-RycDHLVVLANGHVMAQGTPE 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-169 |
7.53e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 7.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRV-GGCSLRTSVRPALKQLGvvf 82
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPDVAEACHYLG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGlsrrQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:PRK13539 80 HRNAMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
....*..
gi 495290120 163 VGLDPAS 169
Cdd:PRK13539 156 AALDAAA 162
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-195 |
8.45e-16 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 75.86 E-value: 8.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRY---HAALHGLSR--RQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLL 157
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLarpDATDEELWAalERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*...
gi 495290120 158 LDEASVGLDPASRLALNQHIRSLCREHniSVLWTTHLL 195
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-197 |
1.07e-15 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 73.65 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcslRTSVRPALKQLgVVFQQSTLDLDLSVEQN-- 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEPGPDRM-VVFQNYSLLPWLTVRENia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 97 LRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQH 176
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180
....*....|....*....|.
gi 495290120 177 IRSLCREHNISVLWTTHLLDE 197
Cdd:TIGR01184 157 LMQIWEEHRVTVLMVTHDVDE 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
3-219 |
1.43e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.76 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVggcsLRTSVRPALKQLGVV 81
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLS----VEQNL---RY-HAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEP 153
Cdd:PRK15056 82 YVPQSEEVDWSfpvlVEDVVmmgRYgHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 154 SLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAE 219
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-216 |
1.46e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 74.73 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR----EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG---CSLRTS-VRPAL 75
Cdd:COG1135 2 IELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSEReLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTLdldLS---VEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHE 152
Cdd:COG1135 82 RKIGMIFQHFNL---LSsrtVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 153 PSLLLLDEASVGLDP---ASRLALNQHIRslcREHNISVLWTTHLLDEVQpR--DDLLILHQGRLVASG 216
Cdd:COG1135 159 PKVLLCDEATSALDPettRSILDLLKDIN---RELGLTIVLITHEMDVVR-RicDRVAVLENGRIVEQG 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-217 |
1.57e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.89 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL---KQLGV 80
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLalrQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQST-----LDLDLSVEQNLRYHaalhGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:PRK13638 82 VFQDPEqqifyTDIDSDIAFSLRNL----GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHNiSVLWTTHLLDEV-QPRDDLLILHQGRLVASGQ 217
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIyEISDAVYVLRQGQILTHGA 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-214 |
2.04e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.15 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNA-LEVSDLSFAY----GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL 75
Cdd:PRK10535 1 MTAlLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQL-----GVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:PRK10535 81 AQLrrehfGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDDLLILHQGRLVA 214
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-242 |
2.09e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLialLTRLYDLQRGDIRVGG------------CSLRTSV 71
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTL---LRHLSGLITGDKSAGShiellgrtvqreGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 72 RPALKQLGVVFQQSTLDLDLSVEQNLR---------YHAALHGLSRRQTGLRVDAeLARQALTERRRERVRELNGGHRRR 142
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLigalgstpfWRTCFSWFTREQKQRALQA-LTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 143 VEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLD-EVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
250 260
....*....|....*....|.
gi 495290120 222 SLEHGGDLGSAFTRLTTSGAA 242
Cdd:PRK09984 241 DNERFDHLYRSINRVEENAKA 261
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-212 |
2.52e-15 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 71.09 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREA--LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGV 80
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNLryhaalhglsrrqtglrvdaelarqalterrrervreLNGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:cd03246 81 LPQDDEL-FSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 495290120 161 ASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDDLLILHQGRL 212
Cdd:cd03246 123 PNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
4-221 |
2.86e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.31 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYgQREALRqVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcSLRTSVRPALKQLGVVFQ 83
Cdd:PRK10771 2 LKLTDITWLY-HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG-QDHTTTPPSRRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLryhaALhGLSrrqTGLRVDAE-------LARQ-ALTERRRERVRELNGGHRRRVEIARALLHEPSL 155
Cdd:PRK10771 79 ENNLFSHLTVAQNI----GL-GLN---PGLKLNAAqreklhaIARQmGIEDLLARLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE---VQPRdDLLILhQGRLVASGQAEAL 221
Cdd:PRK10771 151 LLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDaarIAPR-SLVVA-DGRIAWDGPTDEL 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-193 |
3.49e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDL-----QRGDIRVGGCSLRTS-VRPA--L 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPdVDPVevR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTlDLDLSVEQNLRYHAALHGL----------SRRQTGL--RVDAELARQALTerrrervreLNGGHRRRV 143
Cdd:PRK14243 91 RRIGMVFQKPN-PFPKSIYDNIAYGARINGYkgdmdelverSLRQAALwdEVKDKLKQSGLS---------LSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495290120 144 EIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLwtTH 193
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIV--TH 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-221 |
4.19e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQLG 79
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLDLDLSVEQNLRYHAALHgLSR----RQTGLR-VDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPS 154
Cdd:PRK09536 81 SVPQDTSLSFEFDVRQVVEMGRTPH-RSRfdtwTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 155 LLLLDEASVGLDpasrlaLNQHIRSL-----CREHNISVLWTTHLLDeVQPR--DDLLILHQGRLVASGQAEAL 221
Cdd:PRK09536 160 VLLLDEPTASLD------INHQVRTLelvrrLVDDGKTAVAAIHDLD-LAARycDELVLLADGRVRAAGPPADV 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
4.44e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 72.25 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQ-----RGDIRVGGCSL-RTSVRPA 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIfKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 75 LKQLGVVFQQSTLDLDLSVEQNLRYHAALHGL--SRRQTGLRVDAELARQAL----TERRRERVRELNGGHRRRVEIARA 148
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 149 LLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNIsVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI-VLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-221 |
5.12e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 72.09 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTS---------V 71
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 72 RPALKQLGVVFQQSTLDLDLSVEQN-LRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-227 |
5.20e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 73.23 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAG--KSTLIALLTRLyDLQRGDIRVGG-CSLRTSVRPALKQL 78
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GP-DAGRRPWRF*TwCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVfqQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:NF000106 91 RPV--R*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 159 DEASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALSLEHGG 227
Cdd:NF000106 169 DEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGG 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-216 |
5.25e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQRE------ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcsLRTSVRPAL 75
Cdd:PRK13633 3 EMIKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 ----KQLGVVFQQSTLDLDLS-VEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:PRK13633 81 wdirNKAGMVFQNPDNQIVATiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-216 |
5.37e-15 |
|
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: 71.47 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTsVRPAL--KQL 78
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQ-LDPADlrRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLdLDLSVEQNLRYHAALHGLSR-----RQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEP 153
Cdd:cd03245 81 GYVPQDVTL-FYGTLRDNITLGAPLADDERilraaELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 154 SLLLLDEASVGLDPASRLALNQHIRSLCREhnISVLWTTH---LLDEVqprDDLLILHQGRLVASG 216
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHrpsLLDLV---DRIIVMDSGRIVADG 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-242 |
6.31e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 6.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPAL-KQLGV-- 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKaHQLGIyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLryhaaLHGLSRRQTGL-RVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:PRK15439 91 VPQEPLLFPNLSVKENI-----LFGLPKRQASMqKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 160 EASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALSLEhggDLGSAFTRLTT 238
Cdd:PRK15439 166 EPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADLSTD---DIIQAITPAAR 241
|
....
gi 495290120 239 SGAA 242
Cdd:PRK15439 242 EKSL 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-227 |
6.44e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 70.63 E-value: 6.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRL--YDLQRGDIRVGGCSLrTSVRP---ALKQL 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDI-TDLPPeerARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQqstldldlsveqnlrYHAALHGLSRRQTgLR-VDAelarqalterrrervrELNGGHRRRVEIARALLHEPSLLL 157
Cdd:cd03217 80 FLAFQ---------------YPPEIPGVKNADF-LRyVNE----------------GFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 158 LDEASVGLD-PASRLALNQhIRSLcREHNISVLWTTH---LLDEVQPrDDLLILHQGRLVASGQAE-ALSLEHGG 227
Cdd:cd03217 128 LDEPDSGLDiDALRLVAEV-INKL-REEGKSVLIITHyqrLLDYIKP-DRVHVLYDGRIVKSGDKElALEIEKKG 199
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
7-221 |
7.49e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 72.12 E-value: 7.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 7 SDLSFAYGQ-----REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTS-----VRPALK 76
Cdd:PRK13646 6 DNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQ--QSTLDLDlSVEQNL-----RYHAALHGLSRRQTGLRVDAELARQALTERRRErvreLNGGHRRRVEIARAL 149
Cdd:PRK13646 86 RIGMVFQfpESQLFED-TVEREIifgpkNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQ----MSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 150 LHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
4-216 |
9.68e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.22 E-value: 9.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR---EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG--------CSLRTSVR 72
Cdd:TIGR00958 479 IEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 73 pALKQLGVVFQQSTLD-----LDLSVEQNLRYHAALHGLSRRQTGLrvdaelaRQALTERRRERVRELNGGHRRRVEIAR 147
Cdd:TIGR00958 559 -LVGQEPVLFSGSVREniaygLTDTPDEEIMAAAKAANAHDFIMEF-------PNGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 148 ALLHEPSLLLLDEASVGLDPASRLALNQhirSLCREhNISVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQE---SRSRA-SRTVLLIAHRLSTVERADQILVLKKGSVVEMG 695
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-213 |
1.08e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.78 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 15 QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG--CSLRTSVRpALKQL----GVVFQQSTLD 88
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNK-NLKKLrkkvSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 89 L-DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQAL-TERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLD 166
Cdd:PRK13641 98 LfENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495290120 167 PASRLALNQHIRSLCREHNiSVLWTTHLLDEV-QPRDDLLILHQGRLV 213
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVaEYADDVLVLEHGKLI 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-193 |
1.08e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 72.29 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190
....*....|....*....|....*....|
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTH 193
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTH 203
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-193 |
1.64e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQ 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHaaLHGLSrrqTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK13540 82 RSGINPYLTLRENCLYD--IHFSP---GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|
gi 495290120 164 GLDPASRLALNQHIRSLcREHNISVLWTTH 193
Cdd:PRK13540 157 ALDELSLLTIITKIQEH-RAKGGAVLLTSH 185
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-225 |
1.69e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcSLRTSVRPALKQLGV 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-KRMNDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 161 ASVGLDPASRLALNQHIRSLCREHNISVLWTTHllDEVQPR---DDLLILHQGRLVASGQaeALSLEH 225
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH--DQVEAMtlaDKIVVLDAGRVAQVGK--PLELYH 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-221 |
2.23e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-------RTSVRPA 74
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdifQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 75 LKQLGVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQA-----LTERRRERVRELNGGHRRRVEIARAL 149
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVglwkeVYDRLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 150 LHEPSLLLLDEASVGLDPASRLALNQHIRSLCREhnISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-225 |
2.27e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.40 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALKQLGVVFQ 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 164 GLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQAEALsLEH 225
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMaGRIAIMNRGKFVQIGEPEEI-YEH 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-215 |
2.41e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQ-LGVVFQQSTLDLDLSVEQ 95
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAgVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 96 NL---RYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEasvgldPASRLA 172
Cdd:PRK11288 99 NLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE------PTSSLS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495290120 173 ------LNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVAS 215
Cdd:PRK11288 173 areieqLFRVIREL-RAEGRVILYVSHRMEEIfALCDAITVFKDGRYVAT 221
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-226 |
3.71e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 71.29 E-value: 3.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVV 81
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQ------STLDLDLSVEQNLRYHAALHGLSRRQTglrvdAELAR---QALTERRRERVRELNGGHRRRVEIARALLHE 152
Cdd:PRK10790 420 VQQdpvvlaDTFLANVTLGRDISEEQVWQALETVQL-----AELARslpDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRsLCREHNISVLwTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALA-AVREHTTLVV-IAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQG 566
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-235 |
5.45e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.45 E-value: 5.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-----KQLGVVFQQSTLDLDLS 92
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 93 VEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLA 172
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495290120 173 LNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAEALSLEHGGDLGSAFTR 235
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-101 |
8.28e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 8.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGgcslrTSVRPA-LKQlgvvf 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG-----ETVKIGyFDQ----- 385
|
90
....*....|....*....
gi 495290120 83 QQSTLDLDLSVEQNLRYHA 101
Cdd:COG0488 386 HQEELDPDKTVLDELRDGA 404
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-216 |
9.50e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.44 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQR----EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL----RTSVRPALK 76
Cdd:PRK11153 3 ELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQQSTLdldLS---VEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEP 153
Cdd:PRK11153 83 QIGMIFQHFNL---LSsrtVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 154 SLLLLDEASVGLDPA---SRLALnqhIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASG 216
Cdd:PRK11153 160 KVLLCDEATSALDPAttrSILEL---LKDINRELGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-219 |
1.78e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 68.75 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 21 QVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG-----CSLRTSVRPALKQLGVVFQQSTLDLDLSVEQ 95
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 96 NLRYhaalhGLSRRQTG--------LRVDAELARQALTerrrervreLNGGHRRRVEIARALLHEPSLLLLDEASVGLDP 167
Cdd:PRK11144 96 NLRY-----GMAKSMVAqfdkivalLGIEPLLDRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 495290120 168 ASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAE 219
Cdd:PRK11144 162 PRKRELLPYLERLAREINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLE 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
3-226 |
2.56e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.59 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQ--REALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALK-QLG 79
Cdd:PRK10789 313 ELDVNIRQFTYPQtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRsRLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLDLDlSVEQNLryhaALHGLSRRQTGLRVDAELAR---------QALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:PRK10789 393 VVSQTPFLFSD-TVANNI----ALGRPDATQQEIEHVARLASvhddilrlpQGYDTEVGERGVMLSGGQKQRISIARALL 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-199 |
4.67e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.50 E-value: 4.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQQSTLDLDLSVEQNL 97
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 98 RYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHI 177
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|..
gi 495290120 178 RSLCREHNISVLwTTHLLDEVQ 199
Cdd:TIGR01257 2114 VSIIREGRAVVL-TSHSMEECE 2134
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
3-210 |
7.27e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.03 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRPalKQLGVV 81
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsRLHARD--RKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLSVEQNLRYhaALHGLSRRQtglRVDAELARQALTERRRERV---------RELNGGHRRRVEIARALLHE 152
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAF--GLTVLPRRE---RPNAAAIKAKVTQLLEMVQlahladrypAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQG 210
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEaMEVADRVVVMSQG 213
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-224 |
7.66e-13 |
|
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: 67.16 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLY--DLQRGDIRVGGCSLRTSVRPALKQLGVV 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 F--QQSTLDLDLSVEQNL-------------RYHAALHGLSRRQTGLRVDAelarqaltERRRERVRELNGGHRRRVEIA 146
Cdd:TIGR02633 82 IihQELTLVPELSVAENIflgneitlpggrmAYNAMYLRAKNLLRELQLDA--------DNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 147 RALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEALSLE 224
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSED 231
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-224 |
8.06e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.36 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQ-LGV 80
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNL---------------RYHAALHGLSRRqTGLRVDAElAR-QALTErrrervrelngGHRRRVE 144
Cdd:COG3845 85 VHQHFMLVPNLTVAENIvlgleptkggrldrkAARARIRELSER-YGLDVDPD-AKvEDLSV-----------GEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 145 IARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEVqpR---DDLLILHQGRLVASGQAEAL 221
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREV--MaiaDRVTVLRRGKVVGTVDTAET 228
|
...
gi 495290120 222 SLE 224
Cdd:COG3845 229 SEE 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-221 |
8.97e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.76 E-value: 8.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTsVRPALKQLGV- 80
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINL-VRDKDGQLKVa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 --------------VFQQSTLDLDLSVEQN-LRYHAALHGLSRRQTGLRVDAELARQALTERRRERV-RELNGGHRRRVE 144
Cdd:PRK10619 83 dknqlrllrtrltmVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 145 IARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-193 |
9.22e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTsVRPALKQ----LG 79
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRDEYHQdllyLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 vvfQQSTLDLDLSVEQNLRYHAALHGLSRRQTglRVDAeLARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:PRK13538 81 ---HQPGIKTELTALENLRFYQRLHGPGDDEA--LWEA-LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|....
gi 495290120 160 EASVGLDPASRLALNQHIRSLCREHNISVLwTTH 193
Cdd:PRK13538 155 EPFTAIDKQGVARLEALLAQHAEQGGMVIL-TTH 187
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-212 |
9.57e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.85 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTsvrpALKQLGVVFQ 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE----AREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLryhaalhGLsrrqtGLRVD-AELARQALTERRRERVRE-----LNGGHRRRVEIARALLHEPSLLL 157
Cdd:PRK11247 89 DARLLPWKKVIDNV-------GL-----GLKGQwRDAALQALAAVGLADRANewpaaLSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 158 LDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDE-VQPRDDLLILHQGRL 212
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-221 |
1.43e-12 |
|
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: 66.63 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR-----------EALRQVSFNLAAGRFAALLGPNGAGKSTL-IALLtRLYDlQRGDIRVGGCSL---- 67
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDLdgls 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 68 RTSVRPALKQLGVVFQQ--STLDLDLSVEQ----NLRYHAalHGLSRRQTGLRVDAELARQALTERRrervreLN----- 136
Cdd:COG4172 354 RRALRPLRRRMQVVFQDpfGSLSPRMTVGQiiaeGLRVHG--PGLSAAERRARVAEALEEVGLDPAA------RHryphe 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 137 --GGHRRRVEIARALLHEPSLLLLDEASVGLD---PASRLALnqhIRSLCREHNISVLWTTHLLDEVqpR---DDLLILH 208
Cdd:COG4172 426 fsGGQRQRIAIARALILEPKLLVLDEPTSALDvsvQAQILDL---LRDLQREHGLAYLFISHDLAVV--RalaHRVMVMK 500
|
250
....*....|...
gi 495290120 209 QGRLVASGQAEAL 221
Cdd:COG4172 501 DGKVVEQGPTEQV 513
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-219 |
1.57e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 66.31 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQ-LGV 80
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNL-RY-------------HAALHGLSRR-----QTglRVDAELARqalterrrervreLNGGHRR 141
Cdd:COG4618 411 LPQDVEL-FDGTIAENIaRFgdadpekvvaaakLAGVHEMILRlpdgyDT--RIGEGGAR-------------LSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 142 RVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTH---LLDEVqprDDLLILHQGRLVASGQA 218
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHrpsLLAAV---DKLLVLRDGRVQAFGPR 550
|
.
gi 495290120 219 E 219
Cdd:COG4618 551 D 551
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-221 |
1.72e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.50 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYD-----LQRGDIRVGGCSLRT--SVRPAL 75
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFNyrDVLEFR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVFQQSTlDLDLSVEQNLRYHAALHGLSRRQTGLRV-DAELAR----QALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:PRK14271 101 RRVGMLFQRPN-PFPMSIMDNVLAGVRAHKLVPRKEFRGVaQARLTEvglwDAVKDRLSDSPFRLSGGQQQLLCLARTLA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLCreHNISVLWTTH-LLDEVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLA--DRLTVIIVTHnLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-193 |
1.85e-12 |
|
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: 64.20 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYG-QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRpaLKQLGVVFQ 83
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDL-DLSVEQNLRYhaALHGLSRRQTglRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:cd03226 79 DVDYQLfTDSVREELLL--GLKELDAGNE--QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190
....*....|....*....|....*....|.
gi 495290120 163 VGLDPASRLALNQHIRSLCREHNISVLwTTH 193
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIV-ITH 184
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-227 |
2.50e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 64.32 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLT--RLYDLQRGDIRVGGCSLrTSVRP---ALKQL 78
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDI-LELSPderARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQ-------STLDL-----------DLSVEQnlrYHAALHGLSRRqtgLRVDAELARQALterrrervrelN---- 136
Cdd:COG0396 80 FLAFQYpveipgvSVSNFlrtalnarrgeELSARE---FLKLLKEKMKE---LGLDEDFLDRYV-----------Negfs 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 137 GGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTH---LLDEVQPrDDLLILHQGRLV 213
Cdd:COG0396 143 GGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITHyqrILDYIKP-DFVHVLVDGRIV 220
|
250
....*....|....*
gi 495290120 214 ASGQAE-ALSLEHGG 227
Cdd:COG0396 221 KSGGKElALELEEEG 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-226 |
2.77e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 22 VSFNLAAGRFAALLGPNGAGKSTLI-ALLTRL-YdlqRGDIRVGGCSLRTSVRPA-LKQLGVVFQQSTL----------- 87
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLnALLGFLpY---QGSLKINGIELRELDPESwRKHLSWVGQNPQLphgtlrdnvll 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 88 -DLDLS---VEQNLRYHAALHGLSRRQTGLrvDAELARQALTerrrervreLNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK11174 446 gNPDASdeqLQQALENAWVSEFLPLLPQGL--DTPIGDQAAG---------LSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 164 GLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHG 226
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-221 |
3.42e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.13 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSvrpALKQ--LG 79
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHR---SIQQrdIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 160 EASVGLDPASRLALNQHIRSLCREHNISVLWTTHllDEVQP---RDDLLILHQGRLVASGQAEAL 221
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTH--DQSEAfavSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-193 |
5.43e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.26 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREA----LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT---SVRPA 74
Cdd:PRK10584 5 NIVEVHHLKKSVGQGEHelsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 75 L--KQLGVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHE 152
Cdd:PRK10584 85 LraKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTH 193
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-216 |
8.28e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 63.49 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 6 VSDLSFAYGQR-----EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVG------GCSLRTSVRPA 74
Cdd:PRK13645 9 LDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 75 LKQLGVVFQQSTLDL-DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERV-RELNGGHRRRVEIARALLHE 152
Cdd:PRK13645 89 RKEIGLVFQFPEYQLfQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 153 PSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASG 216
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-148 |
1.07e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 6 VSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIrvggcslrtSVRPALKqLGVVFQQS 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV---------SIPKGLR-IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 86 TLDLDLSVEQNL------------RYHAALHGLSRRQTGLRVDAEL---------------ARQALT------ERRRERV 132
Cdd:COG0488 71 PLDDDLTVLDTVldgdaelraleaELEELEAKLAEPDEDLERLAELqeefealggweaearAEEILSglgfpeEDLDRPV 150
|
170
....*....|....*.
gi 495290120 133 RELNGGHRRRVEIARA 148
Cdd:COG0488 151 SELSGGWRRRVALARA 166
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-221 |
2.60e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 6 VSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGVVFQQ 84
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 85 STLDLDLSVEQNL---RY--HAAL--HGLSRRQtglRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLL 157
Cdd:PRK10575 94 LPAAEGMTVRELVaigRYpwHGALgrFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 158 LDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDeVQPR--DDLLILHQGRLVASGQAEAL 221
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDIN-MAARycDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-221 |
3.50e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY-----------GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQrGDIRVGGCSL----R 68
Cdd:PRK15134 276 LDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLhnlnR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 69 TSVRPALKQLGVVFQ--QSTLDLDLSVEQ----NLRYH-AALHGLSRRQTGLRVDAELARQALTERRRERVreLNGGHRR 141
Cdd:PRK15134 355 RQLLPVRHRIQVVFQdpNSSLNPRLNVLQiieeGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE--FSGGQRQ 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 142 RVEIARALLHEPSLLLLDEASVGLD---PASRLALnqhIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQ 217
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDktvQAQILAL---LKSLQQKHQLAYLFISHDLHVVRALcHQVIVLRQGEVVEQGD 509
|
....
gi 495290120 218 AEAL 221
Cdd:PRK15134 510 CERV 513
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-227 |
5.53e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.74 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLT--RLYDLQRGDIRVGGCSLrTSVRP---ALKQL 78
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDL-LELEPderARAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDA-----ELARQALTERRRERVRELN----GGHRRRVEIARAL 149
Cdd:TIGR01978 80 FLAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDfekllKEKLALLDMDEEFLNRSVNegfsGGEKKRNEILQMA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 150 LHEPSLLLLDEASVGLD-PASRLALNQhIRSLcREHNISVLWTTH---LLDEVQPrDDLLILHQGRLVASGQAE-ALSLE 224
Cdd:TIGR01978 160 LLEPKLAILDEIDSGLDiDALKIVAEG-INRL-REPDRSFLIITHyqrLLNYIKP-DYVHVLLDGRIVKSGDVElAKELE 236
|
...
gi 495290120 225 HGG 227
Cdd:TIGR01978 237 AKG 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-222 |
6.06e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 6.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLY---DLQrGDIRVGGCSLR-TSVRPAlKQLG 79
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYE-GEIIFEGEELQaSNIRDT-ERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VV--FQQSTLDLDLSVEQNLRY-HAALHG--LSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPS 154
Cdd:PRK13549 84 IAiiHQELALVKELSVLENIFLgNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 155 LLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEALS 222
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAiSDTICVIRDGRHIGTRPAAGMT 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
15-195 |
9.80e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.83 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 15 QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT---SVRPALK--QLGVVFQQSTLDL 89
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssAAKAELRnqKLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 90 DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPAS 169
Cdd:PRK11629 101 DFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180
....*....|....*....|....*.
gi 495290120 170 RLALNQHIRSLCREHNISVLWTTHLL 195
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDL 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-221 |
1.50e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.49 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQV----SFNLAAGRFAALLGPNGAGKSTLIALLTRLYD-----LQRGDIRVGGCSLRTSVRPA 74
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVvndvSLQIEAGETLALVGESGSGKSVTALSILRLLPsppvvYPSGDIRFHGESLLHASEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 75 LK-----QLGVVFQQSTLDLD--LSVEQNLRYHAALHGLSRRQTGL--------RVDAELARQALTERRRErvreLNGGH 139
Cdd:PRK15134 86 LRgvrgnKIAMIFQEPMVSLNplHTLEKQLYEVLSLHRGMRREAARgeilncldRVGIRQAAKRLTDYPHQ----LSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 140 RRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQA 218
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRA 241
|
...
gi 495290120 219 EAL 221
Cdd:PRK15134 242 ATL 244
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-219 |
1.64e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 59.47 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 22 VSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQrGDIRVGGCSLRTSVRPALKQL-GVVFQQSTLDLDLSVEQNLRYH 100
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHrAYLSQQQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 101 aaLHGLSRRQTGLRVDAELARQ-ALTERRRERVRELNGGHRRRVEIARA-------LLHEPSLLLLDEASVGLDPASRLA 172
Cdd:COG4138 94 --QPAGASSEAVEQLLAQLAEAlGLEDKLSRPLTQLSGGEWQRVRLAAVllqvwptINPEGQLLLLDEPMNSLDVAQQAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495290120 173 LNQHIRSLCREhNISVLWTTHLLDE-VQPRDDLLILHQGRLVASGQAE 219
Cdd:COG4138 172 LDRLLRELCQQ-GITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETA 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-233 |
1.85e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.52 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF 82
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMS 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 QQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEAS 162
Cdd:NF033858 346 QAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 163 VGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEALSLEHGGD-LGSAF 233
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARGAAtLEEAF 497
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-216 |
2.05e-10 |
|
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: 58.66 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPAL-KQLGV 80
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLrSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNL---------RYHAALHglsrrQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLH 151
Cdd:cd03244 83 IPQDPVL-FSGTIRSNLdpfgeysdeELWQALE-----RVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495290120 152 EPSLLLLDEASVGLDPASRLALNQHIRSLCREHniSVLWTTHLLDEVQPRDDLLILHQGRLVASG 216
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-193 |
2.62e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPalKQLGVVFQ 83
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS--RFMAYLGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHGLSRRQTGlrvDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK13543 90 LPGLKADLSTLENLHFLCGLHGRRAKQMP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190
....*....|....*....|....*....|
gi 495290120 164 GLDPASRLALNQHIRSLCREHNiSVLWTTH 193
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLRGGG-AALVTTH 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-219 |
2.98e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.87 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE----ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALK--- 76
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElse 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 ------------QLGVVFQQSTLDLD--LSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERVR----ELNGG 138
Cdd:PRK10261 93 qsaaqmrhvrgaDMAMIFQEPMTSLNpvFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSryphQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 139 HRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQ 217
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGS 252
|
..
gi 495290120 218 AE 219
Cdd:PRK10261 253 VE 254
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-63 |
3.26e-10 |
|
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: 56.69 E-value: 3.26e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVG 63
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG 60
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-239 |
4.14e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 4.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrTSVRPALK-QLG--V 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-NKLDHKLAaQLGigI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNLrYHAALhgLSRRQTG--------LRVDAE--LARQALTERRRERVRELNGGHRRRVEIARALL 150
Cdd:PRK09700 85 IYQELSVIDELTVLENL-YIGRH--LTKKVCGvniidwreMRVRAAmmLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 151 HEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALSLEH---- 225
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIrRICDRYTVMKDGSSVCSGMVSDVSNDDivrl 240
|
250
....*....|....*.
gi 495290120 226 --GGDLGSAFTRLTTS 239
Cdd:PRK09700 241 mvGRELQNRFNAMKEN 256
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-210 |
6.84e-10 |
|
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: 56.87 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 14 GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTrlydlQR-------GDIRVGGCSLRTSVRpalKQLGVVFQQST 86
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA-----GRktagvitGEILINGRPLDKNFQ---RSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 87 LDLDLSVEQNLRYHAALHGLSRRQtglrvdaelarqalterrrervrelngghRRRVEIARALLHEPSLLLLDEASVGLD 166
Cdd:cd03232 90 HSPNLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 495290120 167 PASRLALNQHIRSLCrEHNISVLWTTHlldevQPR-------DDLLILHQG 210
Cdd:cd03232 141 SQAAYNIVRFLKKLA-DSGQAILCTIH-----QPSasifekfDRLLLLKRG 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-214 |
1.15e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSvRPALKQ---LGV 80
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFN-GPKSSQeagIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLDLDLSVEQNL----RYHAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLL 156
Cdd:PRK10762 84 IHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 157 LLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVA 214
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIfEICDDVTVFRDGQFIA 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-213 |
1.20e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 56.27 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR--EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQ-LGV 80
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSsLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VFQQSTLdLDLSVEQNL-RYHaalhglsrRQTglrvDAELaRQALteRRRERVRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:cd03369 87 IPQDPTL-FSGTIRSNLdPFD--------EYS----DEEI-YGAL--RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 495290120 160 EASVGLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLV 213
Cdd:cd03369 151 EATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-193 |
1.25e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT----SVRPALKQLGVVFQQSTLDLD--- 90
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQDPYASLDprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 91 ---LSVEQNLRYHAALHGLSRRQtglRVDAELARQALTERRR-ERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLD 166
Cdd:PRK10261 419 tvgDSIMEPLRVHGLLPGKAAAA---RVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180
....*....|....*....|....*..
gi 495290120 167 PASRLALNQHIRSLCREHNISVLWTTH 193
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISH 522
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-219 |
1.28e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.86 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 22 VSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDlQRGDIRVGGCSLRTSVRPAL-KQLGVVFQQSTLDLDLSVEQNLryh 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 101 aALHGLSRRQTGLRVDA--ELARQ-ALTERRRERVRELNGGHRRRVEIA-------RALLHEPSLLLLDEASVGLDPASR 170
Cdd:PRK03695 91 -TLHQPDKTRTEAVASAlnEVAEAlGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 495290120 171 LALNQHIRSLCREhNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAE 219
Cdd:PRK03695 170 AALDRLLSELCQQ-GIAVVMSSHDLNHTlRHADRVWLLKQGKLLASGRRD 218
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-216 |
1.56e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.76 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRlyDLQ----------RGDIRVGGCSLRTSVRP 73
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTgggaprgarvTGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 74 ALKQLGVVF-QQSTLDLDLSVEQNL---RY-HAALHGLSRRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARA 148
Cdd:PRK13547 80 RLARLRAVLpQAAQPAFAFSAREIVllgRYpHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 149 ---------LLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLD-EVQPRDDLLILHQGRLVASG 216
Cdd:PRK13547 160 laqlwpphdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-216 |
1.59e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 57.17 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE-----ALRQVSFNLAAGRFAALLGPNGAGKSTLI----ALLTRLY-DLQRGDIRVG--GCSLRTSV 71
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVthfnGLIKSKYgTIQVGDIYIGdkKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 72 RPALKQL----------GVVFQQSTLDL-DLSVEQNLRYHAALHGLSRRQTGLRVDAELARQALTERRRERV-RELNGGH 139
Cdd:PRK13631 102 NPYSKKIknfkelrrrvSMVFQFPEYQLfKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSpFGLSGGQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 140 RRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSlCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASG 216
Cdd:PRK13631 182 KRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTG 258
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-221 |
1.74e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 56.99 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE----ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYD---LQRGDIRVGGCSLRTSVRPALK 76
Cdd:COG0444 2 LEVRNLKVYFPTRRgvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 77 QL-----GVVFQ--QSTLDLDLSVEQ----NLRYHaalHGLSRRQTGLRVDAELARQALTERRRERVR---ELNGGHRRR 142
Cdd:COG0444 82 KIrgreiQMIFQdpMTSLNPVMTVGDqiaePLRIH---GGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 143 VEIARALLHEPSLLLLDEASVGLDPASR---LALnqhIRSLCREHNISVLWTTHLLDEVqpR---DDLLILHQGRLVASG 216
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQaqiLNL---LKDLQRELGLAILFITHDLGVV--AeiaDRVAVMYAGRIVEEG 233
|
....*
gi 495290120 217 QAEAL 221
Cdd:COG0444 234 PVEEL 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-221 |
4.26e-09 |
|
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: 56.23 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQ----REALRQVSFNLAAGRFAALLGPNGAGKS----TLIALLTRLYDLQRGDIRVGGCSLRTSVR 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 73 PALKQL-----GVVFQQ--STLDLDLSVEQNLRYHAALH-GLSRRQTGLRVDAELARQALTERRRERVR---ELNGGHRR 141
Cdd:COG4172 84 RELRRIrgnriAMIFQEpmTSLNPLHTIGKQIAEVLRLHrGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 142 RVEIARALLHEPSLLLLDEASVGLDP---ASRLALnqhIRSLCREHNISVLWTTHLLDEVQpR--DDLLILHQGRLVASG 216
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVtvqAQILDL---LKDLQRELGMALLLITHDLGVVR-RfaDRVAVMRQGEIVEQG 239
|
....*
gi 495290120 217 QAEAL 221
Cdd:COG4172 240 PTAEL 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-217 |
6.29e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 6.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 6 VSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLI-ALLTRLY-DLQRGDIRVGGcslRTSVRPALKQLGVVFQ 83
Cdd:PLN03211 71 ISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLnALAGRIQgNNFTGTILANN---RKPTKQILKRTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAAL---HGLSRRQTGLRVDAELARQALTERRRERV-----RELNGGHRRRVEIARALLHEPSL 155
Cdd:PLN03211 148 DDILYPHLTVRETLVFCSLLrlpKSLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 156 LLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQ 217
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFGK 290
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-222 |
8.90e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.41 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR---------EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR---TSV 71
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 72 RPalKQLGVVFQQSTLDLDLS------VEQNLRYHAALHGLSR--------RQTGLRVDaelarqalteRRRERVRELNG 137
Cdd:PRK15112 85 RS--QRIRMIFQDPSTSLNPRqrisqiLDFPLRLNTDLEPEQRekqiietlRQVGLLPD----------HASYYPHMLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 138 GHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTT-HLLDEVQPRDDLLILHQGRLVASG 216
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEVVERG 232
|
....*..
gi 495290120 217 Q-AEALS 222
Cdd:PRK15112 233 StADVLA 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-225 |
2.65e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.15 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAY---------GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL---- 67
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLakln 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 68 RTSVRPALKQLGVVFQQST------LDLDLSVEQNLRYhaaLHGLSRRQTGLRVDAELARQALTERRRERV-RELNGGHR 140
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSIsavnprKTVREIIREPLRH---LLSLDKAERLARASEMLRAVDLDDSVLDKRpPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 141 RRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQ-A 218
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFcQRVMVMDNGQIVETQPvG 237
|
....*..
gi 495290120 219 EALSLEH 225
Cdd:PRK10419 238 DKLTFSS 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-224 |
2.65e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSfaygqREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQlGVVF 82
Cdd:PRK15439 269 LTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlSTAQRLAR-GLVY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 -----QQSTLDLDLSVEQN---LRYH-----------AALHGLSRRQTGLRVdaELARQALterrrervRELNGGHRRRV 143
Cdd:PRK15439 343 lpedrQSSGLYLDAPLAWNvcaLTHNrrgfwikpareNAVLERYRRALNIKF--NHAEQAA--------RTLSGGNQQKV 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 144 EIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCrEHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALS 222
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIeQMADRVLVMHQGEISGALTGAAIN 491
|
..
gi 495290120 223 LE 224
Cdd:PRK15439 492 VD 493
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-114 |
3.78e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 52.78 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLS--FAYG---QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL--RTSVRPAlK 76
Cdd:COG1101 2 LELKNLSktFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYKRA-K 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 495290120 77 QLGVVFQQSTLDL--DLSVEQNLRYhAALHGLSRrqtGLR 114
Cdd:COG1101 81 YIGRVFQDPMMGTapSMTIEENLAL-AYRRGKRR---GLR 116
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-62 |
3.87e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 52.44 E-value: 3.87e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNA-LEVSDLS--FAYGQR-----EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRV 62
Cdd:COG4778 1 MTTlLEVENLSktFTLHLQggkrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV 70
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-212 |
4.05e-08 |
|
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: 51.66 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAYgqreALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVF 82
Cdd:cd03215 4 VLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 -----QQSTLDLDLSVEQNLryhaalhGLSRRqtglrvdaelarqalterrrervreLNGGHRRRVEIARALLHEPSLLL 157
Cdd:cd03215 80 vpedrKREGLVLDLSVAENI-------ALSSL-------------------------LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 158 LDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRL 212
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-206 |
5.24e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 15 QREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLY----DLQRGDIRVGGCSLRTSVRPALKQLGvvfqqstlDLD 90
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgtpVAGCVDVPDNQFGREASLIDAIGRKG--------DFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 91 LSVEqnlryhaALH--GLSRRQTGLRVDAELARqalterrrervrelngGHRRRVEIARALLHEPSLLLLDEASVGLDP- 167
Cdd:COG2401 114 DAVE-------LLNavGLSDAVLWLRRFKELST----------------GQKFRFRLALLLAERPKLLVIDEFCSHLDRq 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 495290120 168 -ASRLALNqhIRSLCREHNISVLWTTH---LLDEVQPrdDLLI 206
Cdd:COG2401 171 tAKRVARN--LQKLARRAGITLVVATHhydVIDDLQP--DLLI 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-193 |
7.04e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 7.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGcSLRTSVRPALKQLG 79
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-RVVNELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 80 VVFQQSTLDLDLSVEQNLRYHAALHGLSRRQTGLRVDA-----ELA-------RQalterrrervreLNGGHRRRVEIAR 147
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarilELEplldrkpRE------------LSGGQRQRVAMGR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 495290120 148 ALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTH 193
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTH 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-169 |
7.61e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQrGDIRVGGCSLRT-SVRPALKQLGV 80
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSvTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VfQQSTLDLDLSVEQNLRYHAALHGLS----RRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLL 156
Cdd:TIGR01271 1297 I-PQKVFIFSGTFRKNLDPYEQWSDEEiwkvAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170
....*....|...
gi 495290120 157 LLDEASVGLDPAS 169
Cdd:TIGR01271 1376 LLDEPSAHLDPVT 1388
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-221 |
7.99e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.89 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQL----GVVFQQ--STLDLDL 91
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkiQIVFQNpyGSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 92 SVEQNLRYHAALH-GLSRRQTGLRVDAELARQAL-TERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEasvgldPAS 169
Cdd:PRK11308 110 KVGQILEEPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE------PVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495290120 170 rlALNQHIRS--------LCREHNISVLWTTHLLDEVQP-RDDLLILHQGRLVASGQAEAL 221
Cdd:PRK11308 184 --ALDVSVQAqvlnlmmdLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-227 |
1.04e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLT--RLYDLQRGDIRVGGCSLrTSVRPALK-QLGV 80
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESI-LDLEPEERaHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 --VFQQSTLDLDLSVEQNLR--YHAalhglSRRQTGL-RVDA----ELARQALTERRRERV-------RELNGGHRRRVE 144
Cdd:CHL00131 87 flAFQYPIEIPGVSNADFLRlaYNS-----KRKFQGLpELDPleflEIINEKLKLVGMDPSflsrnvnEGFSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 145 IARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNiSVLWTTH---LLDEVQPrDDLLILHQGRLVASGQAE-A 220
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHyqrLLDYIKP-DYVHVMQNGKIIKTGDAElA 239
|
....*..
gi 495290120 221 LSLEHGG 227
Cdd:CHL00131 240 KELEKKG 246
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-239 |
1.17e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.29 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR----TSVRPALK---QLGVVFQQST-LDLD 90
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfglTDLRRVLSiipQSPVLFSGTVrFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 91 LSVEQN-LRYHAALH------GLSRRQTGLrvDAELARQAlterrrervRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PLN03232 1332 PFSEHNdADLWEALErahikdVIDRNPFGL--DAEVSEGG---------ENFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 164 GLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLVA-SGQAEALSLEhggdlGSAFTRLTTS 239
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSGQVLEyDSPQELLSRD-----TSAFFRMVHS 1470
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-61 |
1.44e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.44e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIR 61
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-148 |
1.53e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 51.27 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQRE-----------ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL----R 68
Cdd:COG4608 8 LEVRDLKKHFPVRGglfgrtvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglsG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 69 TSVRPALKQLGVVFQ--QSTLDLDLSVEQNLRYHAALHGL-SRRQTGLRVDAELARQALterrreRVRELN-------GG 138
Cdd:COG4608 88 RELRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL------RPEHADryphefsGG 161
|
170
....*....|
gi 495290120 139 HRRRVEIARA 148
Cdd:COG4608 162 QRQRIGIARA 171
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-216 |
2.26e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.31 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG-----CSLRTSVRPALKQL 78
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 -----GVVFQQSTLDLDLSVE-----------------QNLRYhAALHGLSRRQTGL-RVDaELARQalterrrervreL 135
Cdd:PRK11701 87 lrtewGFVHQHPRDGLRMQVSaggnigerlmavgarhyGDIRA-TAGDWLERVEIDAaRID-DLPTT------------F 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 136 NGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTH------LLDevqprDDLLILHQ 209
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHdlavarLLA-----HRLLVMKQ 227
|
....*..
gi 495290120 210 GRLVASG 216
Cdd:PRK11701 228 GRVVESG 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-216 |
3.59e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 14 GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTrlyDLQRGDIRVGGCSLRTSVRPALKQL----GVVFQQSTLDL 89
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA---FRSPKGVKGSGSVLLNGMPIDAKEMraisAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 90 DLSVEQNLRYHAAL---HGLSRRQTGLRVDAELARQALTE------RRRERVRELNGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:TIGR00955 113 TLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 161 ASVGLDPASRLALNQHIRSLCREHNISVLwTTHlldevQPR-------DDLLILHQGRLVASG 216
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIIC-TIH-----QPSselfelfDKIILMAEGRVAYLG 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-63 |
4.34e-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: 50.32 E-value: 4.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVG 63
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG 382
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-99 |
4.37e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR---EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRpaLK---- 76
Cdd:PTZ00265 383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDIN--LKwwrs 460
|
90 100
....*....|....*....|...
gi 495290120 77 QLGVVFQQSTLdLDLSVEQNLRY 99
Cdd:PTZ00265 461 KIGVVSQDPLL-FSNSIKNNIKY 482
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-216 |
6.45e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.02 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLT--RLYDLQRGDIRVGGCSLrTSVRPALKQLGVV 81
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDL-LELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDL-SVEQNLRYHAALHGLS--RRQTGL-RVD--------AELARQALTERRRERVRELNGGHRRRVEIARAL 149
Cdd:PRK09580 81 FMAFQYPVEIpGVSNQFFLQTALNAVRsyRGQEPLdRFDfqdlmeekIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 150 LHEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTH---LLDEVQPrDDLLILHQGRLVASG 216
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHyqrILDYIKP-DYVHVLYQGRIVKSG 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-167 |
2.04e-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: 47.54 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY--GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQrGDIRVGGCSLRT-SVRPALKQLGV 80
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VfQQSTLDLDLSVEQNLRYHAALHGLS----RRQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLL 156
Cdd:cd03289 82 I-PQKVFIFSGTFRKNLDPYGKWSDEEiwkvAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170
....*....|.
gi 495290120 157 LLDEASVGLDP 167
Cdd:cd03289 161 LLDEPSAHLDP 171
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-64 |
2.06e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 2.06e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495290120 4 LEVSDLSFAYGQRE-ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG 64
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDG 384
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-167 |
2.72e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR--TSVRPALKQLGVV 81
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 82 FQQSTLDLDLSVEQNLRYHAALHGLSRRQTGL-RVDAELARqaLTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDE 160
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFFAERDQFQERIkWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
....*..
gi 495290120 161 ASVGLDP 167
Cdd:PRK11614 164 PSLGLAP 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-63 |
3.42e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 3.42e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVG 63
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG 384
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-224 |
3.43e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 17 EALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQ-LGVVFQQSTLDLDLSVE 94
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENgISMVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 95 QNL---RYhaALHGLSRRQTGLRVDAELARQALTERR--RERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPAS 169
Cdd:PRK10982 92 DNMwlgRY--PTKGMFVDQDKMYRDTKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 170 RLALNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALSLE 224
Cdd:PRK10982 170 VNHLFTIIRKL-KERGCGIVYISHKMEEIfQLCDEITILRDGQWIATQPLAGLTMD 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-216 |
6.43e-06 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 45.33 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTL---IALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGVVFQQSTLDLDLSVEQ 95
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLlkaLANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 96 NLRYHAALHGlsrrqtglrvdAELARqalterrrervrELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQ 175
Cdd:cd03233 103 TLDFALRCKG-----------NEFVR------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495290120 176 HIRSLCREHNISVLWTTHlldevQPR-------DDLLILHQGRLVASG 216
Cdd:cd03233 160 CIRTMADVLKTTTFVSLY-----QASdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-217 |
7.11e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 46.23 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQR-----EALRQVSFNLAAGRFAALLGPNGAGKSTLI----ALL-------------------TRLYDL 55
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnALLlpdtgtiewifkdeknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 56 QRGDIRVGGCSLR--TSVRPALKQLGVVFQQSTLDL-DLSVEQNLRYHAALHGLSRRQTglrvdAELARQALTERRRERV 132
Cdd:PRK13651 83 VLEKLVIQKTRFKkiKKIKEIRRRVGVVFQFAEYQLfEQTIEKDIIFGPVSMGVSKEEA-----KKRAAKYIELVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 133 R------ELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDD-LL 205
Cdd:PRK13651 158 YlqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVLEWTKrTI 236
|
250
....*....|..
gi 495290120 206 ILHQGRLVASGQ 217
Cdd:PRK13651 237 FFKDGKIIKDGD 248
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-242 |
7.45e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQLGVVFQQSTL---------- 87
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLfsgtvrfnld 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 88 ------DLDL--SVEQnlryhAALHGLSRRQTgLRVDAELARQAlterrrervRELNGGHRRRVEIARALLHEPSLLLLD 159
Cdd:PLN03130 1335 pfnehnDADLweSLER-----AHLKDVIRRNS-LGLDAEVSEAG---------ENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 160 EASVGLDPASRLALNQHIRSLCRehNISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEAL-SLEhggdlGSAFTRLTT 238
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIREEFK--SCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNE-----GSAFSKMVQ 1472
|
....*
gi 495290120 239 S-GAA 242
Cdd:PLN03130 1473 StGAA 1477
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-97 |
7.49e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 5 EVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLtrLYDLQ--RGDIRVGgcslrTSVRPALkqlgvvF 82
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQadSGRIHCG-----TKLEVAY------F 387
|
90
....*....|....*..
gi 495290120 83 QQ--STLDLDLSVEQNL 97
Cdd:PRK11147 388 DQhrAELDPEKTVMDNL 404
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-193 |
8.30e-06 |
|
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: 46.33 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALL--TRLYDLQRGDI--RVGGCSLRTSV-RPAL--- 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyHVALCEKCGYVeRPSKvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 --KQLGVVFQQSTLD---LDLSVEQNLRYHAA--------LHGLSR---------RQTGLRVDAELARQA-------LTE 126
Cdd:TIGR03269 81 pcPVCGGTLEPEEVDfwnLSDKLRRRIRKRIAimlqrtfaLYGDDTvldnvlealEEIGYEGKEAVGRAVdliemvqLSH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 127 RRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTH 193
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-175 |
1.55e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 7 SDLSFAY-GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTrlydlqrGDIR-VGGCSLRTS-VRPAlkqlgvVFQ 83
Cdd:PLN03073 512 SDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------GELQpSSGTVFRSAkVRMA------VFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLD-LDLSV--------------EQNLRYHAALHGLSrrqtglrvdAELARQALterrrervRELNGGHRRRVEIARA 148
Cdd:PLN03073 579 QHHVDgLDLSSnpllymmrcfpgvpEQKLRAHLGSFGVT---------GNLALQPM--------YTLSGGQKSRVAFAKI 641
|
170 180
....*....|....*....|....*..
gi 495290120 149 LLHEPSLLLLDEASVGLDPASRLALNQ 175
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQ 668
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-60 |
1.63e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 4 LEVSDLSFAYGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDI 60
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-219 |
1.75e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.38 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAygqreALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQlGVVF 82
Cdd:PRK10762 258 LKVDNLSGP-----GVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrSPQDGLAN-GIVY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 83 -----QQSTLDLDLSVEQNLRYhAALHGLSRRQTGLRVDAElaRQAL----------TERRRERVRELNGGHRRRVEIAR 147
Cdd:PRK10762 332 isedrKRDGLVLGMSVKENMSL-TALRYFSRAGGSLKHADE--QQAVsdfirlfnikTPSMEQAIGLLSGGNQQKVAIAR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495290120 148 ALLHEPSLLLLDEASVGLDPASRLALNQHIRSLcREHNISVLWTTHLLDEVQPRDD-LLILHQGRLVASGQAE 219
Cdd:PRK10762 409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDrILVMHEGRISGEFTRE 480
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-221 |
2.64e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 44.94 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 2 NALEVSDLSFAYGQRE--ALRQVSFNLAAGRFAALLGPNGAGKSTLI-ALLTRLYDLQrgdirvGGCSLRTSVrpalkql 78
Cdd:TIGR00957 635 NSITVHNATFTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLsALLAEMDKVE------GHVHMKGSV------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLDLDlSVEQNLRYHAALHGLSRRQT----GLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPS 154
Cdd:TIGR00957 702 AYVPQQAWIQND-SLRENILFGKALNEKYYQQVleacALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 155 LLLLDeasvglDPASrlALNQHIRSLCREH---------NISVLWTTHLLDEVQPRDDLLILHQGRLVASGQAEAL 221
Cdd:TIGR00957 781 IYLFD------DPLS--AVDAHVGKHIFEHvigpegvlkNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-219 |
2.66e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTLI-ALLTRLYDLQRGD---IRVGGCSLRtSVRPALKqlGVVFQQSTLDL---DL 91
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGFHIGVegvITYDGITPE-EIKKHYR--GDVVYNAETDVhfpHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 92 SVEQNLRYHAALHGLSRRQTGL--------RVDAELARQAL-----TERRRERVRELNGGHRRRVEIARALLHEPSLLLL 158
Cdd:TIGR00956 154 TVGETLDFAARCKTPQNRPDGVsreeyakhIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCW 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495290120 159 DEASVGLDPASRLalnQHIRSLCREHNIsvLWTTHLLDEVQPR-------DDLLILHQGRLVASGQAE 219
Cdd:TIGR00956 234 DNATRGLDSATAL---EFIRALKTSANI--LDTTPLVAIYQCSqdayelfDKVIVLYEGYQIYFGPAD 296
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-194 |
4.13e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREaLRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRTSVRPALKQLGvvfQ 83
Cdd:PRK13541 2 LSLHQLQFNIEQKN-LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG---H 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 84 QSTLDLDLSVEQNLRYHAALHglsrrQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASV 163
Cdd:PRK13541 78 NLGLKLEMTVFENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180 190
....*....|....*....|....*....|.
gi 495290120 164 GLDPASRLALNQHIRSLCREHNIsVLWTTHL 194
Cdd:PRK13541 153 NLSKENRDLLNNLIVMKANSGGI-VLLSSHL 182
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-226 |
5.45e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAYGQREAL---RQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQR----------------------- 57
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 58 -------------------------------GDIRVGGCSLRTSVRPALKQLGVVFQQSTLDLDLSVEQNLRY---HAAL 103
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFgkeDATR 1325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 104 HGLSRRQTGLRVDA--ELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLC 181
Cdd:PTZ00265 1326 EDVKRACKFAAIDEfiESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 495290120 182 REHNISVLWTTHLLDEVQPRDDLLILHQ----GRLVAS--GQAEALSLEHG 226
Cdd:PTZ00265 1406 DKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhgTHEELLSVQDG 1456
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-193 |
7.92e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.08 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 13 YGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLT-----------RLYDLQRG------DIRvggcslrtsvrpal 75
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFGRRRGsgetiwDIK-------------- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 KQLGVVfqQSTLDLDLSVEQNLR-------------YHAalhgLSRRQTglrvdaELARQALTERRRERVR------ELN 136
Cdd:PRK10938 336 KHIGYV--SSSLHLDYRVSTSVRnvilsgffdsigiYQA----VSDRQQ------KLAQQWLDILGIDKRTadapfhSLS 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 495290120 137 GGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTH 193
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-64 |
1.07e-04 |
|
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: 42.07 E-value: 1.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 4 LEVSDLSFAYGQRE-----ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG 64
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG 66
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-193 |
1.91e-04 |
|
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: 41.62 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 34 LLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLrtSVRPalkqlgvvfQQSTLDLDLSVEQNLRYHAALHG-LSRRQTG 112
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV--SYKP---------QYIKADYEGTVRDLLSSITKDFYtHPYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 113 ----LRVDAELARQALTerrrervreLNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISV 188
Cdd:cd03237 99 iakpLQIEQILDREVPE---------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTA 169
|
....*
gi 495290120 189 LWTTH 193
Cdd:cd03237 170 FVVEH 174
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-224 |
2.10e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.93 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSfaygQREALRQVSFNLAAGR---FAALLGpngAGKSTLIALLTRLYDLQRGDIRVGGCSLR-TSVRPALKQl 78
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRA- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVF-----QQSTLDLDLSVEQN-----LRYHAALHGLSRRQtgLRVDAELARQAL---TERRRERVRELNGGHRRRVEI 145
Cdd:COG1129 328 GIAYvpedrKGEGLVLDLSIRENitlasLDRLSRGGLLDRRR--ERALAEEYIKRLrikTPSPEQPVGNLSGGNQQKVVL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 146 ARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREhNISVLWTTHLLDEV-QPRDDLLILHQGRLVASGQAEALSLE 224
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELlGLSDRILVMREGRIVGELDREEATEE 484
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-219 |
2.87e-04 |
|
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: 41.71 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 4 LEVSDLSFAY-----GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGD--IRVG---------GCSL 67
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGdewvdmtkpGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 68 RTSVRPalkQLGVVFQQSTLDLDLSVEQNLRYHAALH---GLSRRQT--GLRV---DAELARQALTERRRErvreLNGGH 139
Cdd:TIGR03269 360 RGRAKR---YIGILHQEYDLYPHRTVLDNLTEAIGLElpdELARMKAviTLKMvgfDEEKAEEILDKYPDE----LSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 140 RRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGRLVASGQA 218
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVcDRAALMRDGKIVKIGDP 512
|
.
gi 495290120 219 E 219
Cdd:TIGR03269 513 E 513
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-219 |
4.14e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.86 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 1 MNALEVSDLSFAYGQRE----ALRQVSFNLAAGRFAALLGPNGAGKS-TLIALLtrlyDLQRGDIRVGGcSLRTSVRPAL 75
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM----GLLAANGRIGG-SATFNGREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 76 ------------KQLGVVFQQSTLDLD--LSVEQNLRYHAALH-GLSRRQT---GLR-VDA----ElARQALTERRRErv 132
Cdd:PRK09473 85 nlpekelnklraEQISMIFQDPMTSLNpyMRVGEQLMEVLMLHkGMSKAEAfeeSVRmLDAvkmpE-ARKRMKMYPHE-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 133 reLNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALNQHIRSLCREHNISVLWTTHLLDEVQPR-DDLLILHQGR 211
Cdd:PRK09473 162 --FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGIcDKVLVMYAGR 239
|
....*...
gi 495290120 212 LVASGQAE 219
Cdd:PRK09473 240 TMEYGNAR 247
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
18-118 |
4.23e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 18 ALRQVSFNLaaGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRvGGCSLRTSVRPALKQLGVVFQQS---TLDLDLSVE 94
Cdd:COG4637 12 SLRDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDAARGGLQ-DALARRGGLEELLWRGPRTITEPirlELEFAEEDE 88
|
90 100
....*....|....*....|....
gi 495290120 95 QNLRYHAALhGLSRRQTGLRVDAE 118
Cdd:COG4637 89 RDLRYELEL-GLPEPGGRPEVKEE 111
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-222 |
5.94e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.88 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFAY---GQREALRQVSFNLAAGRFAALLGPNGAGKSTLI-ALLTRLYDLQRGdirvgGCSLRTSVrPALKQL 78
Cdd:PLN03130 614 AISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDA-----SVVIRGTV-AYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 79 GVVFQQSTLDLDL--SVEQNLRYHAALHglsrrQTGLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLL 156
Cdd:PLN03130 688 SWIFNATVRDNILfgSPFDPERYERAID-----VTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495290120 157 LLDeasvglDPASrlALNQHI------RSLCRE--HNISVLWTT--HLLDEVqprDDLLILHQGRLVASGQAEALS 222
Cdd:PLN03130 763 IFD------DPLS--ALDAHVgrqvfdKCIKDElrGKTRVLVTNqlHFLSQV---DRIILVHEGMIKEEGTYEELS 827
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-97 |
7.60e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSLRT-SVRPALKQLGVVFQQSTLdLDLSVEQNL 97
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyGLRELRRQFSMIPQDPVL-FDGTVRQNV 1404
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-53 |
8.72e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 8.72e-04
10 20 30
....*....|....*....|....*....|....*.
gi 495290120 18 ALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLY 53
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY 51
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-224 |
1.77e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.24 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 3 ALEVSDLSFA-YGQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGGCSL-RTSVRpALKQLGV 80
Cdd:COG3845 257 VLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLSPR-ERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 81 VF-----QQSTLDLDLSVEQNL---RYHAAlhGLSRRQTgLRVDA--ELARQAL------TERRRERVRELNGGHRRRVE 144
Cdd:COG3845 336 AYipedrLGRGLVPDMSVAENLilgRYRRP--PFSRGGF-LDRKAirAFAEELIeefdvrTPGPDTPARSLSGGNQQKVI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 145 IARALLHepslllldEASV--------GLDPASRLALNQHIRSLcREHNISVLWTTHLLDEV-QPRDDLLILHQGRLVAS 215
Cdd:COG3845 413 LARELSR--------DPKLliaaqptrGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEIlALSDRIAVMYEGRIVGE 483
|
....*....
gi 495290120 216 GQAEALSLE 224
Cdd:COG3845 484 VPAAEATRE 492
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-210 |
6.12e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 37.78 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 14 GQREALRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYD---LQRGDIRVGGCSLRTSVRpalKQLGVVFQQstlDLD 90
Cdd:TIGR00956 774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSFQ---RSIGYVQQQ---DLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 91 L---SVEQNLRYHAALH---GLSRRQTGLRVDA-------ELARQALTERRRERvreLNGGHRRRVEIA-RALLHEPSLL 156
Cdd:TIGR00956 848 LptsTVRESLRFSAYLRqpkSVSKSEKMEYVEEvikllemESYADAVVGVPGEG---LNVEQRKRLTIGvELVAKPKLLL 924
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 495290120 157 LLDEASVGLDPASRLALNQHIRSLCrEHNISVLWTTH-----LLDEVqprDDLLILHQG 210
Cdd:TIGR00956 925 FLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIHqpsaiLFEEF---DRLLLLQKG 979
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-210 |
8.75e-03 |
|
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: 37.20 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 19 LRQVSFNLAAGRFAALLGPNGAGKSTLIALLTRLYDLQRGDIRVGG----CSLRTSVRPALKQLGVVFqqstldlDLSVE 94
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGrisfSPQTSWIMPGTIKDNIIF-------GLSYD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495290120 95 QnLRYHAALHGLSrrqtgLRVDAELARQALTERRRERVRELNGGHRRRVEIARALLHEPSLLLLDEASVGLDPASRLALN 174
Cdd:TIGR01271 515 E-YRYTSVIKACQ-----LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
170 180 190
....*....|....*....|....*....|....*..
gi 495290120 175 QhiRSLCR-EHNISVLWTTHLLDEVQPRDDLLILHQG 210
Cdd:TIGR01271 589 E--SCLCKlMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| |
