|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-222 |
4.85e-106 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 308.92 E-value: 4.85e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 162 GLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKI 222
Cdd:COG1131 161 GLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
2-308 |
1.68e-94 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 282.05 E-value: 1.68e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:TIGR03522 3 IRVSSLTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYLPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:TIGR03522 83 HNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 162 GLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKgKERLQLEIGGPGEEvkN 241
Cdd:TIGR03522 163 GLDPNQLVEIRNVIKNIGKDKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAANK-KQVIEVEFEEQIDL--Q 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 242 ALRNVPGVANVQieiHELDGCFKYIVETEvkADIKKNLARIIADNKWDLYEMRTLGMTLEEIFMRYT 308
Cdd:TIGR03522 240 LFETLEEISSVK---NTGGNTWKLTFETP--NDTRPEIFKLAQQKGLKLISLQQNEKNLEQVFREIT 301
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-226 |
6.15e-83 |
|
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: 250.54 E-value: 6.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMP 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 161 SGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKE 226
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-304 |
3.06e-75 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 232.69 E-value: 3.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIleqSIDVRRNIGYMP 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 161 SGLDP------KQIIevRELIKglAGeHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIkGKERLQLEIGG 234
Cdd:COG4152 158 SGLDPvnvellKDVI--RELAA--KG-TTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQF-GRNTLRLEADG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 235 PGEEvknaLRNVPGVANVqieihELDGcFKYIVETEVKADIKKNLARIIADNKWDLYEMRTlgMTLEEIF 304
Cdd:COG4152 232 DAGW----LRALPGVTVV-----EEDG-DGAELKLEDGADAQELLRALLARGPVREFEEVR--PSLNEIF 289
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-207 |
3.28e-75 |
|
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: 228.44 E-value: 3.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLefvawikgikmkdipkridavmektsithvrdricgRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931518567 162 GLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:cd03230 125 GLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-213 |
7.24e-75 |
|
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: 229.00 E-value: 7.24e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGeILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518567 162 GLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-309 |
4.60e-71 |
|
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: 222.27 E-value: 4.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 9 KKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPESPPIYPE 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 89 MSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQI 168
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 169 IEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIkGKERLQLEIGGPGE-EVKNALRnv 246
Cdd:TIGR01188 161 RAIWDYIRALKEEgVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRL-GKDTLESRPRDIQSlKVEVSML-- 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 247 pgvanvqieIHELDGCFKYIVETEVKADIKKNLAR-----------IIADNKWDLYEMRTLGMTLEEIFMRYTT 309
Cdd:TIGR01188 238 ---------IAELGETGLGLLAVTVDSDRIKILVPdgdetvpeiveAAIRNGIRIRSISTERPSLDDVFLKLTG 302
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-218 |
7.98e-65 |
|
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: 203.76 E-value: 7.98e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 162 GLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-213 |
2.45e-64 |
|
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: 201.68 E-value: 2.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEqSIDVRRNIGYMPE 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKmkdiPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518567 162 GLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-213 |
2.95e-63 |
|
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: 199.52 E-value: 2.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNI 76
Cdd:cd03266 1 MITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGL-AGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-213 |
6.91e-62 |
|
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: 195.58 E-value: 6.91e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIleqSIDVRRNIGYMPE 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL---DIAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518567 162 GLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
2.42e-60 |
|
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: 193.34 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYM 79
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVqsyLEFVA--------WIKGIKMKDIpKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:COG1120 81 PQEPPAPFGLTV---RELVAlgryphlgLFGRPSAEDR-EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
5.42e-58 |
|
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: 186.17 E-value: 5.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQ--VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYM 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLT 219
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-218 |
5.05e-54 |
|
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: 175.98 E-value: 5.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYM 79
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLrELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PEsppiYPE-----MSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:COG1122 81 FQ----NPDdqlfaPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-194 |
1.33e-51 |
|
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: 169.20 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMP 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAWIKGIKMKDIpkRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*
gi 931518567 161 SGLDPKQIIEVRELIKG-LAGEHTVIVSTHILPEV 194
Cdd:COG4133 160 TALDAAGVALLAELIAAhLARGGAVLLTTHQPLEL 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-216 |
8.73e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 168.34 E-value: 8.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQsidvRRNIGYMP 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ---ESPPIYPeMSVqsyLEFVA--------WIKGIKMKDIpKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIH 149
Cdd:COG1121 82 qraEVDWDFP-ITV---RDVVLmgrygrrgLFRRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 150 NPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGwIVAQGTPE 216
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPE 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-213 |
4.05e-50 |
|
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: 164.53 E-value: 4.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS-IDVRRNIGYMPe 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSpKELARKIAYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 sppiypemsvQsylefvawikgikmkdipkridaVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03214 80 ----------Q-----------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931518567 162 GLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-213 |
8.12e-49 |
|
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: 162.32 E-value: 8.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILeqsiDVRRNIGYMPES 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 83 PPIYPEMSVqSYLEFVA--------WIKGIKMKDIpKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:cd03235 77 RSIDRDFPI-SVRDVVLmglyghkgLFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGwIVAQG 213
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-218 |
3.08e-48 |
|
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: 161.17 E-value: 3.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGYM 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHkrARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGEHTVIVST-HILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-218 |
4.80e-48 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 160.90 E-value: 4.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGYM 79
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHerARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWIKGIKMKD-IPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDLDRAeREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 159 PTSGLDPKQIIEVRELIKGLAGEHT-VIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIgVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-229 |
4.94e-48 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 160.64 E-value: 4.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATvagFDILEQSIDVRRNIGYMPESPP 84
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEII---FDGHPWTRKDLHKIGSLIESPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 85 IYPEMSVQSYLEFVAWIKGIKmkdiPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:TIGR03740 81 LYENLTARENLKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 165 PKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQGtpenltqKIKGKERLQ 229
Cdd:TIGR03740 157 PIGIQELRELIRSFPEQGiTVILSSHILSEVQQLADHIGIISEGVLGYQG-------KINKSENLE 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-207 |
1.59e-47 |
|
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: 158.78 E-value: 1.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISKKFGG--KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYM 79
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 ---PESPPIYPemSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:cd03225 81 fqnPDDQFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-207 |
3.51e-46 |
|
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: 155.34 E-value: 3.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGG----KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-----V 72
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPP 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 153 VLILDEPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHIlPEVKLTCERVIIINNG 207
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEagTTIVVVTHD-PELAEYADRIIELRDG 216
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-213 |
8.42e-46 |
|
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: 154.21 E-value: 8.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMPE 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931518567 162 GLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03259 160 ALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
1.15e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.34 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMP 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVqsyLEFVAwiKGIKMKDIPK-----RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:COG3842 84 QDYALFPHLTV---AENVA--FGLRMRGVPKaeiraRVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVkLT-CERVIIINNGWIVAQGTPENL 218
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEEA-LAlADRIAVMNDGRIEQVGTPEEI 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-220 |
1.58e-45 |
|
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: 154.37 E-value: 1.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID----VRRNI 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVqsyLEFVAW----IKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPP 152
Cdd:COG1127 85 GMLFQGGALFDSLTV---FENVAFplreHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 153 VLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-207 |
2.92e-45 |
|
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: 151.96 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDV---RRNIGYMPE 81
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVqsylefvawikgikmkdipkridavmektsithvRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03229 84 DFALFPHLTV----------------------------------LENIALGLSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931518567 162 GLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNG 207
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLgiTVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-220 |
3.08e-45 |
|
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: 153.81 E-value: 3.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS----IDVRRNIG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYPEMSVqsyLEFVAWikGIKMK-DIPKRI--DAVMEK---TSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:cd03261 81 MLFQSGALFDSLTV---FENVAF--PLREHtRLSEEEirEIVLEKleaVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-218 |
8.58e-45 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 152.49 E-value: 8.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR--RNIGY 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRarLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 159 PTSGLDPKQIIEVRELIKGLA----GehtVIVSTHilpEVKLT---CERVIIINNGWIVAQGTPENL 218
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLKergiG---VLITDH---NVRETlgiCDRAYIISEGKVLAEGTPEEI 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-220 |
4.10e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 150.98 E-value: 4.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI----DVRRN 75
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGralrRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVqsyLEFV------------AWIKGIKMKDIPKRIDAvMEKTSITHVRDRICGRLSKGYRQRVGL 143
Cdd:COG3638 82 IGMIFQQFNLVPRLSV---LTNVlagrlgrtstwrSLLGLFPPEDRERALEA-LERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTD 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-221 |
4.12e-44 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 161.06 E-value: 4.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGkqvlFS----ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIG 77
Cdd:NF033858 267 IEARGLTMRFGD----FTavdhVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:NF033858 343 YMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 158 EPTSGLDPkqiieV------RELIKgLAGEH--TVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:NF033858 423 EPTSGVDP-----VardmfwRLLIE-LSREDgvTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-212 |
1.02e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.42 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFG-GK---QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDV---- 72
Cdd:COG1136 4 LLELRNLTKSYGtGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 -RRNIGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:COG1136 84 rRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHIlPEVKLTCERVIIINNGWIVAQ 212
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-210 |
2.34e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.58 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-GGKQVLFSISFDVNKGEILgFL-GPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID----VRR 74
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipyLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGL--AGEhTVIVSTHILPEVKLTCERVIIINNGWIV 210
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEInrRGT-TVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-213 |
2.86e-42 |
|
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: 145.94 E-value: 2.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISK-KFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGY-MP 80
Cdd:cd03267 22 SLKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVvFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 161 SGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-216 |
3.58e-42 |
|
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: 145.66 E-value: 3.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGYM 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHeiARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSV----------QSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIH 149
Cdd:cd03219 81 FQIPRLFPELTVlenvmvaaqaRTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 150 NPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-226 |
4.43e-42 |
|
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: 145.56 E-value: 4.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKfGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMPESPPI 85
Cdd:cd03299 5 NLSKD-WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRDISYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 86 YPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP 165
Cdd:cd03299 83 FPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 166 KQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKE 226
Cdd:cd03299 163 RTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
6.13e-42 |
|
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: 151.59 E-value: 6.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF--GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCfLLPN----EGTATVAGFDILEQSIDVR- 73
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHggriSGEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 RNIGYMPESPP--IYPeMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:COG1123 83 RRIGMVFQDPMtqLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-218 |
8.97e-42 |
|
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: 144.75 E-value: 8.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFS-ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS-IDVRRNIGYM 79
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNnLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSI--THVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 158 EPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-218 |
1.71e-41 |
|
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: 144.18 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFG----GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI-LEQSIDVRRN 75
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPP--IYPEMSVQSYLEFVAWIKGIKmkDIPKRIDAVMEKTSIT-HVRDRICGRLSKGYRQRVGLAQALIHNPP 152
Cdd:COG1124 81 VQMVFQDPYasLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 153 VLILDEPTSGLDP---KQIIevrELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:COG1124 159 LLLLDEPTSALDVsvqAEIL---NLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
2.10e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.44 E-value: 2.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-----GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI----D 71
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslrE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 72 VRRNIGYMPESPpiY----PEMSVQSYLEFVAWIKGIKMK-DIPKRIDAVMEKTSI-THVRDRICGRLSKGYRQRVGLAQ 145
Cdd:COG1123 340 LRRRVQMVFQDP--YsslnPRMTVGDIIAEPLRLHGLLSRaERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 146 ALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-207 |
3.17e-41 |
|
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: 140.84 E-value: 3.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE-QSIDVRRNIGYMPE 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 sppiypemsvqsylefvawikgikmkdipkridavmektsithvrdricgrLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931518567 162 GLDPKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNG 207
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGrTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-240 |
1.13e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 144.46 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF----------GGKQVLFS-----------ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTAT 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGALKGLFRreyreveavddISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 60 VAGFDILEQSIDVRRNIGY-MPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSI-----THVRdricgRL 133
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVvFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLgelldTPVR-----QL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 134 SKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVA 211
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
|
250 260
....*....|....*....|....*....
gi 931518567 212 QGTPENLTQKIKGKERLQLEIGGPGEEVK 240
Cdd:COG4586 236 DGSLEELKERFGPYKTIVLELAEPVPPLE 264
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-218 |
1.80e-40 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 141.57 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI--LEQSIDVRRNIGYM 79
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIslLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWI-KGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 159 PTSGLDPKQIIEVRELIKGLAGEHT-VIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
2.04e-40 |
|
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: 141.71 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGY 78
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSV-------------QSYLEFVAWIKGIK--MKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGL 143
Cdd:COG0411 84 TFQNPRLFPELTVlenvlvaaharlgRGLLAALLRLPRARreEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
8.60e-40 |
|
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: 139.24 E-value: 8.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILtCFLL------PNEGTATVAGFDILEQSIDV--- 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNdlipgaPDEGEVLLDGKDIYDLDVDVlel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESPPIYPeMSVQSYLEFVAWIKGIKMKDIPKRIDA-VMEKTSIT-HVRDRICGR-LSKGYRQRVGLAQALIH 149
Cdd:cd03260 80 RRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWdEVKDRLHALgLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 150 NPPVLILDEPTSGLDP--KQIIEvrELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:cd03260 159 EPEVLLLDEPTSALDPisTAKIE--ELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTE 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-222 |
1.19e-39 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 139.91 E-value: 1.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE-QSIDVRRNIGYM 79
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQsylEFVA-----WikGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALI------ 148
Cdd:PRK13548 82 PQHSSLSFPFTVE---EVVAmgrapH--GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 149 HNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVsthILPEVKLT---CERVIIINNGWIVAQGTPEN-LTQKI 222
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIV---VLHDLNLAaryADRIVLLHQGRLVADGTPAEvLTPET 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-222 |
1.25e-39 |
|
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: 139.24 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFG-GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI----DVRRNI 76
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSV-----QSYLEFVAWIKGI----KMKDIPKRIDAvMEKTSITHVRDRICGRLSKGYRQRVGLAQAL 147
Cdd:cd03256 81 GMIFQQFNLIERLSVlenvlSGRLGRRSTWRSLfglfPKEEKQRALAA-LERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 148 IHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKI 222
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-207 |
1.75e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.03 E-value: 1.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMP 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEmSVQSYLEFVAWIKGIKMKdiPKRIDAVMEKTSITH-VRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNG 207
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-218 |
4.50e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 139.56 E-value: 4.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 162 GLDPKQIIEVRELIKGL-AGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK13537 168 GLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-218 |
6.57e-39 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 136.90 E-value: 6.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 22 FDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdilEQSIDVRRNIGYMPESP------PIYPEMSVQS-Y 94
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG----ASPGKGWRHIGYVPQRHefawdfPISVAHTVMSgR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 95 LEFVAWIKGIKMKDIpKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVREL 174
Cdd:TIGR03771 77 TGHIGWLRRPCVADF-AAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931518567 175 IKGLAGE-HTVIVSTHILPEVKLTCERVIIInNGWIVAQGTPENL 218
Cdd:TIGR03771 156 FIELAGAgTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQL 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-218 |
7.01e-39 |
|
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: 136.94 E-value: 7.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS----IDV 72
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESppiYPEMSVQSYLEFVAW---IKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIH 149
Cdd:cd03258 81 RRRIGMIFQH---FNLLSSRTVFENVALpleIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 150 NPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
1.81e-38 |
|
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: 136.37 E-value: 1.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEG-TATVAGFDILEQSI-DVRRNIGY 78
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVwELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MpeSP----PIYPEMSVqsyLEFVA---------WiKGIKMKDIpKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQ 145
Cdd:COG1119 83 V--SPalqlRFPRDETV---LDVVLsgffdsiglY-REPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 146 ALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTH----ILPEVkltcERVIIINNGWIVAQG------ 213
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHhveeIPPGI----THVLLLKDGRVVAAGpkeevl 231
|
....*..
gi 931518567 214 TPENLTQ 220
Cdd:COG1119 232 TSENLSE 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-237 |
2.01e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 138.81 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 162 GLDP--KQIIEVReLIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKERLQLEIGGPGE 237
Cdd:PRK13536 202 GLDPhaRHLIWER-LRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIYGGDPHE 278
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-220 |
2.02e-38 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 135.64 E-value: 2.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGYM 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWIKGIkmKDIPKRIDAVMEKTSITH-VRDRICGRLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR--AKRKARLERVYELFPRLKeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 159 PTSGLDPKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
2.81e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 138.67 E-value: 2.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMP 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-DRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFvawikGIKMKDIPK-----RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:COG3839 82 QSYALYPHMTVYENIAF-----PLKLRKVPKaeidrRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGLageH-----TVIVSTHILPEVkLT-CERVIIINNGWIVAQGTPENL 218
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRL---HrrlgtTTIYVTHDQVEA-MTlADRIAVMNDGRIQQVGTPEEL 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-220 |
4.70e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.14 E-value: 4.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG--FDI-----LEQSIDVRR 74
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFsqkpsEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIGYMPESPPIYPEMSV-QSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPV 153
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVmENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAG-EHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-161 |
7.10e-38 |
|
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: 131.62 E-value: 7.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMPESPPIYPEMSVQSYL 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERkSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 96 EFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGR----LSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-245 |
1.05e-37 |
|
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 upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 134.87 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF--GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS--IDVRRNIG 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YM---PESppiypemsvqsylEFVAWI-----------KGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGL 143
Cdd:TIGR04520 81 MVfqnPDN-------------QFVGATveddvafglenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ 226
|
250 260
....*....|....*....|....*
gi 931518567 222 IKGKERLQLEIggP-GEEVKNALRN 245
Cdd:TIGR04520 227 VELLKEIGLDV--PfITELAKALKK 249
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
1.71e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.58 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID---VRRNIG 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinkLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYPEMSVqsyLEFVA----WIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPV 153
Cdd:COG1126 81 MVFQQFNLFPHLTV---LENVTlapiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAGEH-TVIVSTHilpEVKLTCE---RVIIINNGWIVAQGTPE 216
Cdd:COG1126 158 MLFDEPTSALDPELVGEVLDVMRDLAKEGmTMVVVTH---EMGFAREvadRVVFMDGGRIVEEGPPE 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-207 |
2.76e-37 |
|
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: 130.97 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGG--KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGY 78
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeSLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYpemsvqsylefvawikgikmkdipkridavmeKTSIthvRDRIcgrLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:cd03228 81 VPQDPFLF--------------------------------SGTI---RENI---LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931518567 159 PTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLtCERVIIINNG 207
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-220 |
4.53e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 132.45 E-value: 4.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG--FDiLEQSID------VR 73
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFD-FSKTPSdkaireLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 RNIGYMPESPPIYPEMSV-QSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPP 152
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVqQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 153 VLILDEPTSGLDPKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-221 |
1.19e-36 |
|
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: 137.97 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIGYM 79
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAsWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPeMSVQSYLEFVAwikgikmKDIPK-RIDAVMEKTSI------------THVRDRicGR-LSKGYRQRVGLAQ 145
Cdd:COG4988 417 PQNPYLFA-GTIRENLRLGR-------PDASDeELEAALEAAGLdefvaalpdgldTPLGEG--GRgLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 146 ALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLtCERVIIINNGWIVAQGTPENLTQK 221
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-209 |
1.57e-36 |
|
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: 130.34 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID---VRRNIGY 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNineLRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVqsyLEFVA----WIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:cd03262 81 VFQQFNLFPHLTV---LENITlapiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWI 209
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLAEEGmTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-258 |
2.08e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 133.73 E-value: 2.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDiLEQSIDVR-RNIGYMP 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLPPReRRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVqsyLEFVAwiKGIKMKDIPK-----RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:COG1118 82 QHYALFPHMTV---AENIA--FGLRVRPPSKaeiraRVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 156 LDEPTSGLDP---KQI-IEVRELIKGLagEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL------------- 218
Cdd:COG1118 157 LDEPFGALDAkvrKELrRWLRRLHDEL--GGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVydrpatpfvarfl 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 931518567 219 -------TQKIKGkerlQLEIGGPGEEVKNALRNVPGVANV---QIEIHE 258
Cdd:COG1118 235 gcvnvlrGRVIGG----QLEADGLTLPVAEPLPDGPAVAGVrphDIEVSR 280
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-206 |
1.54e-35 |
|
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: 127.97 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQ----VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdilEQSIDVRRNIG 77
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 931518567 158 EPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINN 206
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-213 |
1.62e-35 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 128.01 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIL----EQSIDV 72
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLklsrRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESPP--IYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRIcGR----LSKGYRQRVGLAQA 146
Cdd:cd03257 81 RKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVL-NRypheLSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 147 LIHNPPVLILDEPTSGLDPK---QIIevrELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSvqaQIL---DLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-218 |
2.09e-35 |
|
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: 128.12 E-value: 2.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMPE 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-KRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 162 GLDPK----QIIEVRELIKGLagEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03300 160 ALDLKlrkdMQLELKRLQKEL--GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-244 |
3.51e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGG--KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGY 78
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPP-IYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:PRK13635 86 VFQNPDnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 158 EPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLTQKIKGKERLQLEIGGP 235
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKSGHMLQEIGLDVPFS 244
|
....*....
gi 931518567 236 gEEVKNALR 244
Cdd:PRK13635 245 -VKLKELLK 252
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
7.57e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.15 E-value: 7.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR-RNIGYM 79
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELaRRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PEsppiypemsvQSYLEF---VAWIkgIKM---------KDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQAL 147
Cdd:COG4559 81 PQ----------HSSLAFpftVEEV--VALgraphgssaAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 148 --IHNPP-----VLILDEPTSGLDPKQIIEVRELIKGLAGEH-TVIVsthILPEVKLT---CERVIIINNGWIVAQGTPE 216
Cdd:COG4559 149 aqLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRGgGVVA---VLHDLNLAaqyADRILLLHQGRLVAQGTPE 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-210 |
9.06e-35 |
|
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: 125.83 E-value: 9.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIleqsIDVR---RNIGYMPE 81
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV----TDLPpkdRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 931518567 162 GLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIV 210
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLgtTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-218 |
1.09e-34 |
|
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: 126.25 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGY 78
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVQSYLEFVAWIKGIKmKDIPKRIDAVM-------EKtsithvRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYARRDR-AEVRADLERVYelfprlkER------RRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIV----STHILPEVkltCERVIIINNGWIVAQGTPENL 218
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILlveqNARFALEI---ADRAYVLERGRIVLEGTAAEL 223
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-213 |
1.27e-34 |
|
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: 125.39 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQ--VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS-IDVRRNIGYMPE 81
Cdd:cd03245 6 RNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpADLRRNIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPI------------YPEMSVQSYLEfVAWIKGIK--MKDIPKRIDavmektsiTHVRDRICGrLSKGYRQRVGLAQAL 147
Cdd:cd03245 86 DVTLfygtlrdnitlgAPLADDERILR-AAELAGVTdfVNKHPNGLD--------LQIGERGRG-LSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 148 IHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLtCERVIIINNGWIVAQG 213
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDL-VDRIIVMDSGRIVADG 220
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-220 |
1.58e-34 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 125.87 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFG-GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI-------LEQsidV 72
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrgkkLRK---L 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESPPIYPEMSVqsyLE-----FVAWIKGIKM-------KDIPKRIDAvMEKTSITHVRDRICGRLSKGYRQR 140
Cdd:TIGR02315 78 RRRIGMIFQHYNLIERLTV---LEnvlhgRLGYKPTWRSllgrfseEDKERALSA-LERVGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 141 VGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
..
gi 931518567 219 TQ 220
Cdd:TIGR02315 234 DD 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-221 |
4.23e-34 |
|
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: 131.88 E-value: 4.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGG--KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGY 78
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPaSLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIY------------PEMSVQSYLEfVAWIKGIkMKDI---PKRIDavmektsiTHVRDRicGR-LSKGYRQRVG 142
Cdd:COG2274 554 VLQDVFLFsgtirenitlgdPDATDEEIIE-AARLAGL-HDFIealPMGYD--------TVVGEG--GSnLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDP---KQIIEVrelIKGLAGEHTVIVSTHILPEVKLtCERVIIINNGWIVAQGTPENLT 219
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAeteAIILEN---LRRLLKGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELL 697
|
..
gi 931518567 220 QK 221
Cdd:COG2274 698 AR 699
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-216 |
3.62e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 126.11 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYM 79
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSArAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEfvawikgikMKDIPKR-------------IDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQA 146
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVE---------MGRTPHRsrfdtwtetdraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 147 LIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-221 |
9.58e-33 |
|
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: 127.19 E-value: 9.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF--GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIGY 78
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIY------------PEMS---VQSYLEFV---AWIKGIkmkdiPKRIDAVMEKTsithvrdricGR-LSKGYRQ 139
Cdd:COG4987 414 VPQRPHLFdttlrenlrlarPDATdeeLWAALERVglgDWLAAL-----PDGLDTWLGEG----------GRrLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 140 RVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLtCERVIIINNGWIVAQGTPENLT 219
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL 557
|
..
gi 931518567 220 QK 221
Cdd:COG4987 558 AQ 559
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-207 |
1.19e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 120.05 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIL----EQSIDVRRN 75
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNrlrgRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGL--AGEhTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLnkRGT-TVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-203 |
1.20e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 121.35 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF----GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSidvrRNI 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLM 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPE-VKLtCERVII 203
Cdd:COG1116 163 DEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEaVFL-ADRVVV 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-210 |
1.28e-32 |
|
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: 119.67 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISKKFGGKQ-VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQsiDVRRNIGYMPE 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 sppiypEMSVQSYLEFVAWIKGIKMKDIPK---RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:cd03226 79 ------DVDYQLFTDSVREELLLGLKELDAgneQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518567 159 PTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIV 210
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-218 |
1.70e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 121.01 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI-------LEQSI--D 71
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsQQKGLirQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 72 VRRNIGYMPESPPIYPEMSV-QSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHN 150
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVlENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 151 PPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-218 |
2.60e-32 |
|
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: 120.14 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMPE 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVqsyLEFVAWikGIKMK---------DIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPP 152
Cdd:cd03296 82 HYALFRHMTV---FDNVAF--GLRVKprserppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 153 VLILDEPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElhVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-215 |
4.58e-32 |
|
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: 126.28 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF--GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIlEQSID-VRRNIGY 78
Cdd:TIGR01257 929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDaVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:TIGR01257 1008 CPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 159 PTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTP 215
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-258 |
6.66e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 123.98 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFdilEQSID-----VRRN 75
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIRsprdaIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVqsyLEFVA------WIKGIKMKDIPKRIDAVMEKTSItHVR-DRICGRLSKGYRQRVGLAQALI 148
Cdd:COG3845 82 IGMVHQHFMLVPNLTV---AENIVlgleptKGGRLDRKAARARIRELSERYGL-DVDpDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 149 HNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQK------ 221
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEelaelm 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 931518567 222 -----IKGKERLQLEIGGPGEEVKN----ALRNVPGVANVQIEIHE 258
Cdd:COG3845 238 vgrevLLRVEKAPAEPGEVVLEVENlsvrDDRGVPALKDVSLEVRA 283
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-189 |
8.16e-32 |
|
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: 117.14 E-value: 8.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 12 GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI---LEQSIDVRRNIGYM---PESPPI 85
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVfqdPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 86 YPemSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP 165
Cdd:TIGR01166 83 AA--DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*
gi 931518567 166 KQIIEVRELIKGL-AGEHTVIVSTH 189
Cdd:TIGR01166 161 AGREQMLAILRRLrAEGMTVVISTH 185
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
8.20e-32 |
|
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: 119.86 E-value: 8.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGG-----KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIL----EQSIDV 72
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPEsppiYPEMsvQSYLEFVAwiK---------GIKMKDIPKRIDAVMEKTSITH-VRDRICGRLSKGYRQRVG 142
Cdd:TIGR04521 81 RKKVGLVFQ----FPEH--QLFEETVY--KdiafgpknlGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkgLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
250
....*....|.
gi 931518567 221 KIKGKERLQLE 231
Cdd:TIGR04521 233 DVDELEKIGLD 243
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-212 |
1.44e-31 |
|
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: 115.60 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdileqsIDVRRNigympe 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------KEVSFA------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPpiypemsvqsyleFVAWIKGIKMkdipkridaVMEktsithvrdricgrLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03216 68 SP-------------RDARRAGIAM---------VYQ--------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 931518567 162 GLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQ 212
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-214 |
1.49e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.57 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTcfLL--PNEGTATVAGFDILEQS----I 70
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCIN--LLerPTSGSVLVDGVDLTALSerelR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 71 DVRRNIGympesppiypeMSVQSY--------LEFVAW---IKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQ 139
Cdd:COG1135 79 AARRKIG-----------MIFQHFnllssrtvAENVALpleIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 140 RVGLAQALIHNPPVLILDEPTSGLDP---KQIIEV-----RELikGLagehTVIVSTHilpE---VKLTCERVIIINNGW 208
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPettRSILDLlkdinREL--GL----TIVLITH---EmdvVRRICDRVAVLENGR 218
|
....*.
gi 931518567 209 IVAQGT 214
Cdd:COG1135 219 IVEQGP 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
1.70e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.55 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKqvLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRrnigymp 80
Cdd:COG3840 1 MLRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 espPI---------YPEMSVQSYLEFvawikGI--KMK---DIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQA 146
Cdd:COG3840 72 ---PVsmlfqennlFPHLTVAQNIGL-----GLrpGLKltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 147 LIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
7-213 |
4.64e-31 |
|
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: 115.86 E-value: 4.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 7 ISKKFGGkqvlFS--ISFDVNkGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG---FDIlEQSIDV---RRNIGY 78
Cdd:cd03297 6 IEKRLPD----FTlkIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDS-RKKINLppqQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVQSYLEFVAwiKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 159 PTSGLDP--KQII--EVRELIKGLAGehTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03297 158 PFSALDRalRLQLlpELKQIKKNLNI--PVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-190 |
1.12e-30 |
|
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: 114.38 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPE 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVQSYLEFVAWIKGIKMKDipkrIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQRT----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|....
gi 931518567 162 GLDPKQIievrELIKGLAGEHT-----VIVSTHI 190
Cdd:TIGR01189 157 ALDKAGV----ALLAGLLRAHLarggiVLLTTHQ 186
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-245 |
1.22e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 116.75 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQ---VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNI 76
Cdd:PRK13650 4 IIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPP-IYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK13650 84 GMVFQNPDnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTcERVIIINNGWIVAQGTPENLTQkiKGKERLQLEIG 233
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALS-DRVLVMKNGQVESTSTPRELFS--RGNDLLQLGLD 240
|
250
....*....|...
gi 931518567 234 GP-GEEVKNALRN 245
Cdd:PRK13650 241 IPfTTSLVQSLRQ 253
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-215 |
1.34e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.87 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG--FDILEQSI-DVRRNIGYMPESP--PIYp 87
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLmKLRESVGMVFQDPdnQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 88 EMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQ 167
Cdd:PRK13636 97 SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518567 168 IIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTP 215
Cdd:PRK13636 177 VSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-216 |
1.47e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 115.88 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYM 79
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIyPE-MSVQsylEFVA-----WIK--GIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:PRK11231 82 PQHHLT-PEgITVR---ELVAygrspWLSlwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-207 |
2.26e-30 |
|
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: 114.04 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQV-LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE----QSIDVRRNI 76
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518567 157 DEPTSGLDPKQIIEVRELIKG--LAGEhTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKinKAGT-TVVVATHAKELVDTTRHRVIALERG 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-218 |
2.62e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.80 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDV---RRNIG 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErliRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYPEMSVqsyLEFVAW----IKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPV 153
Cdd:PRK09493 81 MVFQQFYLFPHLTA---LENVMFgplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-314 |
7.21e-30 |
|
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: 120.12 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 24 VNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPESPPIYPEMSVQSYLEFVAWIKG 103
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRG 2041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 104 IKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-H 182
Cdd:TIGR01257 2042 VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgR 2121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 183 TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKERLQLEIGGPGEEVKNALR--------NVPGvaNVQI 254
Cdd:TIGR01257 2122 AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLLPDLNpveqffqgNFPG--SVQR 2199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 255 EIHEldgcfkYIVETEVKADIKKNLARIIADNKWDLY--EMRTLGMTLEEIFMRYTTGETFT 314
Cdd:TIGR01257 2200 ERHY------NMLQFQVSSSSLARIFQLLISHKDSLLieEYSVTQTTLDQVFVNFAKQQTET 2255
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-213 |
9.62e-30 |
|
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: 111.87 E-value: 9.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKK------FGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFL--LPNEGTATVAGFDILEQSIdvR 73
Cdd:cd03213 4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDKRSF--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 RNIGYMPESPPIYPEMSVQSYLEFVAWIKGIkmkdipkridavmektsithvrdricgrlSKGYRQRVGLAQALIHNPPV 153
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLA-GEHTVIVSTHILP-EVKLTCERVIIINNGWIVAQG 213
Cdd:cd03213 133 LFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-215 |
1.80e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.43 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMPE 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-NRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 SPPIYPEMSVqsyLEFVAWikGIKMKDIPKR-IDA-VMEKTSITHVR---DRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:PRK09452 94 SYALFPHMTV---FENVAF--GLRMQKTPAAeITPrVMEALRMVQLEefaQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTP 215
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-218 |
3.33e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.43 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMPESPP 84
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 85 IYPEMSVQSYLEFvawikGIKMKDIPK-----RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:PRK11432 89 LFPHMSLGENVGY-----GLKMLGVPKeerkqRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFniTSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-221 |
4.36e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 12 GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIGYMPESPPIYpEMS 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEsLRRQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 91 VqsyLEFVAWikGikmkdipkRIDA----VMEKTSITHVRDRICgRLSKGY---------------RQRVGLAQALIHNP 151
Cdd:COG1132 430 I---RENIRY--G--------RPDAtdeeVEEAAKAAQAHEFIE-ALPDGYdtvvgergvnlsggqRQRIAIARALLKDP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIR-NADRILVLDDGRIVEQGTHEELLAR 564
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-189 |
1.00e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 110.90 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRiltCF-----LLPN---EGTATVAGFDILEQSIDV- 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLR---CLnrmndLIPGarvEGEILLDGEDIYDPDVDVv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 --RRNIGYMPESPPIYPeMSVqsYlEFVAW---IKGIKMKdipKRIDAVMEKtSITH------VRDRI---CGRLSKGYR 138
Cdd:COG1117 89 elRRRVGMVFQKPNPFP-KSI--Y-DNVAYglrLHGIKSK---SELDEIVEE-SLRKaalwdeVKDRLkksALGLSGGQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518567 139 QRVGLAQALIHNPPVLILDEPTSGLDPK--QIIEvrELIKGLAGEHTVIVSTH 189
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPIstAKIE--ELILELKKDYTIVIVTH 211
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
1.14e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.24 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGG--KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIG 77
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPP-IYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:PRK13632 87 IIFQNPDnQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLA--GEHTVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLtqkIKGKERLQL 230
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRktRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI---LNNKEILEK 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-216 |
2.52e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 112.10 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIleQSIDVR-RNIGYMP 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV--SRLHARdRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFvawikGIKM---------KDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:PRK10851 81 QHYALFRHMTVFDNIAF-----GLTVlprrerpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElkFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-213 |
2.72e-28 |
|
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: 107.78 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGG--KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYM 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPemsvqsylefvawikgikmkdipkridavmektsiTHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:cd03247 81 NQRPYLFD-----------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQG 213
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-202 |
3.24e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 108.42 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQsiDVRRNIGYMP 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP--DVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAWIKGikmkDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:PRK13539 80 HRNAMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 931518567 161 SGLDPKQIIEVRELIKG-LAGEHTVIVSTHIlpEVKLTCERVI 202
Cdd:PRK13539 156 AALDAAAVALFAELIRAhLAQGGIVIAATHI--PLGLPGAREL 196
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-214 |
3.70e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 109.44 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIL---EQSIdVRRNIGYMPES 82
Cdd:COG4674 15 DLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTgldEHEI-ARLGIGRKFQK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 83 PPIYPEMSVQSYLEFVA-----WIKGIKMK---DIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:COG4674 94 PTVFEELTVFENLELALkgdrgVFASLFARltaEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGT 214
Cdd:COG4674 174 LLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-218 |
3.94e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.85 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDiLEQSIDVRRNIGYMP 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFvawikGIKMKDIPKR--IDAVMEKTSITHVRD---RICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK11607 98 QSYALFPHMTVEQNIAF-----GLKQDKLPKAeiASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 156 LDEPTSGLDPK----QIIEVRELIKGLAGehTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDILERVGV--TCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-232 |
2.65e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 2.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGG------KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI--LEQSIDV 72
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESP--PIYPEMsVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHN 150
Cdd:PRK13633 84 RNKAGMVFQNPdnQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 151 PPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLTQKIKGKERL 228
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKEVEMMKKI 241
|
....
gi 931518567 229 QLEI 232
Cdd:PRK13633 242 GLDV 245
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-207 |
3.02e-27 |
|
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: 104.61 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQ--VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIGY 78
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNeLGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPEsppiypemsvqsylefvawikgikmkdipkriDAVMEKTSIthvRDRIcgrLSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:cd03246 81 LPQ--------------------------------DDELFSGSI---AENI---LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518567 159 PTSGLDPKQIIEVRELIKGL-AGEHTVIVSTHiLPEVKLTCERVIIINNG 207
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAH-RPETLASADRILVLEDG 171
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-258 |
3.65e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.88 E-value: 3.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRN-IGY 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAgIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVqsyLE--FVA-------WIKGIKMKdipKRIDAVMEKTSItHVR-DRICGRLSKGYRQRVGLAQALI 148
Cdd:COG1129 84 IHQELNLVPNLSV---AEniFLGreprrggLIDWRAMR---RRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 149 HNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQG-----TPENLTQKI 222
Cdd:COG1129 157 RDARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVRLM 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 931518567 223 KGKERLQL------EIGGPGEEVKNaLRNVPGVANVQIEIHE 258
Cdd:COG1129 237 VGRELEDLfpkraaAPGEVVLEVEG-LSVGGVVRDVSFSVRA 277
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-218 |
3.90e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 108.66 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFGGKQVlfSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG---FDIlEQSIDV---RRNIGYM 79
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDS-RKGIFLppeKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFvawikGIKMKDIPKRI---DAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRY-----GMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGEHT--VIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGipILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-218 |
6.61e-27 |
|
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: 106.57 E-value: 6.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS----IDVRRN-IG 77
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelRELRRKkIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:cd03294 106 MVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 158 EPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPE-VKLTcERVIIINNGWIVAQGTPENL 218
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEaLRLG-DRIAIMKDGRLVQVGTPEEI 248
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS---IDVRRNI 76
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESP--PIYPEmSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:PRK13639 81 GIVFQNPddQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-221 |
1.24e-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: 105.00 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIGYMPESPPIYPEmSV 91
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDsLRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 92 QSYLEFVAW-------IKGIKMKDIPKRIDAVMEKTSiTHVRDRicG-RLSKGYRQRVGLAQALIHNPPVLILDEPTSGL 163
Cdd:cd03253 92 GYNIRYGRPdatdeevIEAAKAAQIHDKIMRFPDGYD-TIVGER--GlKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 164 DPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:cd03253 169 DTHTEREIQAALRDVSKGRTTIVIAHRLSTIV-NADKIIVLKDGRIVERGTHEELLAK 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-214 |
1.56e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 106.81 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF--GGKQV--LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS----IDV 72
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGympesppiypeMSVQ------SYLEF--VAW---IKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRV 141
Cdd:PRK11153 81 RRQIG-----------MIFQhfnllsSRTVFdnVALpleLAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 142 GLAQALIHNPPVLILDEPTSGLDP---KQIIEV-----RELikGLagehTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPattRSILELlkdinREL--GL----TIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
.
gi 931518567 214 T 214
Cdd:PRK11153 224 T 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
1.72e-26 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 104.81 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTatvagfdiLEQSIDVRrnIGYMP 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV--------IKRNGKLR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVqSYLEFVAWIKGIKMKDI-P--KRIDAvmektsiTHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:PRK09544 74 QKLYLDTTLPL-TVNRFLRLRPGTKKEDIlPalKRVQA-------GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 158 EPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHILPEVKLTCERVIIInNGWIVAQGTPE 216
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRREldCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPE 205
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
1.88e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.27 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGY 78
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESP--PIYPEmSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:PRK13652 83 VFQNPddQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-221 |
1.89e-26 |
|
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: 104.23 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYM 79
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRkSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEmsvqSYLEfvawikGIKMKDIPKRIDAVMEKTSITHVRDRI--------------CGRLSKGYRQRVGLAQ 145
Cdd:cd03254 83 LQDTFLFSG----TIME------NIRLGRPNATDEEVIEAAKEAGAHDFImklpngydtvlgenGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 146 ALIHNPPVLILDEPTSGLDPK--QIIE--VRELIKGlageHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTEteKLIQeaLEKLMKG----RTSIIIAHRLSTIK-NADKILVLDDGKIIEEGTHDELLAK 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-189 |
2.09e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 108.61 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 4 AKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdileqsiDVRrnIGYMPESP 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------GLR--IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 84 PIYPEMSVqsyLEFVawIKGIK-MKDIPKRIDAVMEKTSITHVR------------------------------------ 126
Cdd:COG0488 71 PLDDDLTV---LDTV--LDGDAeLRALEAELEELEAKLAEPDEDlerlaelqeefealggweaearaeeilsglgfpeed 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 127 -DRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGehTVIVSTH 189
Cdd:COG0488 146 lDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSH 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-204 |
1.07e-25 |
|
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: 106.99 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGK-QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDV-RRNIGYM 79
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPemsvQSYLEFVAwikgIKMKDI-PKRIDAVMEKTSI-THVRDRICG----------RLSKGYRQRVGLAQAL 147
Cdd:TIGR02857 402 PQHPFLFA----GTIAENIR----LARPDAsDAEIREALERAGLdEFVAALPQGldtpigeggaGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 148 IHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHiLPEVKLTCERVIII 204
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH-RLALAALADRIVVL 529
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
18-213 |
1.12e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 101.86 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 18 FSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILeQSIDVRRNIGYMPESPPIYPEMSVQSYLEf 97
Cdd:TIGR01277 15 MEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT-GLAPYQRPVSMLFQENNLFAHLTVRQNIG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 98 VAWIKGIKMKDIPK-RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIK 176
Cdd:TIGR01277 93 LGLHPGLKLNAEQQeKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 931518567 177 GLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:TIGR01277 173 QLCSERqrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-221 |
1.15e-25 |
|
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: 102.23 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 15 QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMPESPPIYpEMSVQS 93
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLrWLRSQIGLVSQEPVLF-DGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 94 YLEF-------VAWIKGIKMKDIPKRIDAVMEKTSiTHVRDRICgRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPK 166
Cdd:cd03249 96 NIRYgkpdatdEEVEEAAKKANIHDFIMSLPDGYD-TLVGERGS-QLSGGQKQRIAIARALLRNPKILLLDEATSALDAE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 167 QIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:cd03249 174 SEKLVQEALDRAMKGRTTIVIAHRLSTIR-NADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-232 |
1.19e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI---DVRRNIGYMPEsppiYPEM- 89
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsDIRKKVGLVFQ----YPEYq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 ----SVQSYLEFVAWIKGIKMKDIPKRIDAVME--KTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGL 163
Cdd:PRK13637 96 lfeeTIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 164 DPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKERLQLEI 232
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESIGLAV 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-213 |
4.32e-25 |
|
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: 100.30 E-value: 4.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF----------------------GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTat 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 60 vagfdileqsIDVRRNIgympeSPPI------YPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRL 133
Cdd:cd03220 79 ----------VTVRGRV-----SSLLglgggfNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 134 SKGYRQRVGLAQALIHNPPVLILDEPTSGLDP----KQIIEVRELIKGLAgehTVIVSTHILPEVKLTCERVIIINNGWI 209
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAafqeKCQRRLRELLKQGK---TVILVSHDPSSIKRLCDRALVLEKGKI 220
|
....
gi 931518567 210 VAQG 213
Cdd:cd03220 221 RFDG 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-218 |
4.55e-25 |
|
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: 100.77 E-value: 4.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQ--VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGY 78
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEmsvqSYLEFVAWIK-GIKMKDIPKRIDAV--------MEKTSITHVRDRiCGRLSKGYRQRVGLAQALIH 149
Cdd:cd03251 81 VSQDVFLFND----TVAENIAYGRpGATREEVEEAARAAnahefimeLPEGYDTVIGER-GVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 150 NPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIE-NADRIVVLEDGKIVERGTHEEL 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-213 |
4.70e-25 |
|
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: 100.42 E-value: 4.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLlpnEGTATVAG---FDILEQSID-VRRNIGYMPESPPIYPEM 89
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGqilFNGQPRKPDqFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 SVQSYLEFVAWIKG--IKMKDIPKRIDAV--MEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP 165
Cdd:cd03234 97 TVRETLTYTAILRLprKSSDAIRKKRVEDvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518567 166 KQIIEVRELIKGLA-GEHTVIVSTHI-LPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03234 177 FTALNLVSTLSQLArRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-216 |
5.05e-25 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 100.59 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR--- 73
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 --RNIGYMPESPPIYPEMSVqsyLEFVA---WIKGikMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALI 148
Cdd:COG4181 88 raRHVGFVFQSFQLLPTLTA---LENVMlplELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 149 HNPPVLILDEPTSGLDPK---QIIevrELIKGLAGEH--TVIVSTHilpEVKLT--CERVIIINNGWIVAQGTPE 216
Cdd:COG4181 163 TEPAILFADEPTGNLDAAtgeQII---DLLFELNRERgtTLVLVTH---DPALAarCDRVLRLRAGRLVEDTAAT 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-213 |
6.01e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 104.48 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG--FDILEQSIDVRRNIGY 78
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVQSYL-------EFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:PRK09700 85 IYQELSVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVS-THILPEVKLTCERVIIINNGWIVAQG 213
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYiSHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-218 |
6.95e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 100.65 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI--------------- 65
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 66 --LEQsidVRRNIGYMPESPPIYPEMSV-QSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVG 142
Cdd:COG4598 88 rqLQR---IRTRLGMVFQSFNLWSHMTVlENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH-TVIVSTHilpEVKLTCE---RVIIINNGWIVAQGTPENL 218
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGrTMLVVTH---EMGFARDvssHVVFLHQGRIEEQGPPAEV 241
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-213 |
1.42e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 98.72 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 18 FSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI--LEQSidvRRNIGYMPESPPIYPEMSVQSYL 95
Cdd:cd03298 15 MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaAPPA---DRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 96 EfVAWIKGIKMKDIP-KRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVREL 174
Cdd:cd03298 92 G-LGLSPGLKLTAEDrQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 931518567 175 IKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-190 |
1.68e-24 |
|
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: 98.33 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 4 AKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMPESP 83
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 84 PIYPEMSVQSYLEFVAWIKGikmkdiPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGL 163
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*...
gi 931518567 164 DPKQIIEVRELIKG-LAGEHTVIVSTHI 190
Cdd:cd03231 157 DKAGVARFAEAMAGhCARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-221 |
2.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMPESP--PIYpEM 89
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKVGLVFQDPddQVF-SS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 SVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQII 169
Cdd:PRK13647 96 TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 931518567 170 EVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:PRK13647 176 TLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-244 |
2.91e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.40 E-value: 2.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILtcfllpNEGTATVAGF----DIL---------EQ 68
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL------NRMNDKVSGYrysgDVLlggrsifnyRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 69 SIDVRRNIGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSI-THVRDRICG---RLSKGYRQRVGLA 144
Cdd:PRK14271 96 VLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 145 QALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKG 224
Cdd:PRK14271 176 RTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKH 255
|
250 260
....*....|....*....|
gi 931518567 225 KERLQLeIGGPGEEVKNALR 244
Cdd:PRK14271 256 AETARY-VAGLSGDVKDAKR 274
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-218 |
3.38e-24 |
|
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: 100.95 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAkNISKKFGGkqvlFS--ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG---FDIlEQSIDV--- 72
Cdd:COG4148 2 MLEV-DFRLRRGG----FTldVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDS-ARGIFLpph 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESPPIYPEMSVQSYLEFVawikgikMKDIPK-----RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQAL 147
Cdd:COG4148 76 RRRIGYVFQEARLFPHLSVRGNLLYG-------RKRAPRaerriSFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 148 IHNPPVLILDEPTSGLDP--KQiiEVRELIKGLAGEHTV-IV-STHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:COG4148 149 LSSPRLLLMDEPLAALDLarKA--EILPYLERLRDELDIpILyVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-218 |
4.64e-24 |
|
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: 99.74 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPN---EGTATVAGFDILEQS---- 69
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 70 IDVR-RNIGYMPESPpiY----PEMSVQSYLEFVAWI-KGIKMKDIPKRIDAVMEKTSITHVRDRIcGR----LSKGYRQ 139
Cdd:COG0444 81 RKIRgREIQMIFQDP--MtslnPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRL-DRypheLSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 140 RVGLAQALIHNPPVLILDEPTSGLDP---KQIIevrELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGT 214
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVtiqAQIL---NLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
....
gi 931518567 215 PENL 218
Cdd:COG0444 235 VEEL 238
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-218 |
5.61e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 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. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 99.49 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 33 LGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvRRNIGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKR 112
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 113 IDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPK---QI-IEVRELIKGLAgeHTVIVST 188
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdQMqLELKTIQEQLG--ITFVFVT 158
|
170 180 190
....*....|....*....|....*....|
gi 931518567 189 HILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:TIGR01187 159 HDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-213 |
5.97e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.06 E-value: 5.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCF--LLPN---EGTATVAGFDILEQS-IDVRRN 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDvIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVqsyLEFVAWikGIKM-------KDIPKRIDAVMEKTSI-THVRDRI---CGRLSKGYRQRVGLA 144
Cdd:PRK14247 84 VQMVFQIPNPIPNLSI---FENVAL--GLKLnrlvkskKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 145 QALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-218 |
9.03e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 101.74 E-value: 9.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAM------RILtcfllpNEGTATVAGFDILEQSI--DVR 73
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEVLGGDMADARHrrAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 RNIGYMPES--PPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:NF033858 76 PRIAYMPQGlgKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 152 PVLILDEPTSGLDP---KQIIevrELIKGLAGEH---TVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENL 218
Cdd:NF033858 156 DLLILDEPTTGVDPlsrRQFW---ELIDRIRAERpgmSVLVATAYMEEAE-RFDWLVAMDAGRVLATGTPAEL 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-218 |
9.65e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.14 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI--DVRRNIG 77
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPI-YPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENV 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-221 |
2.24e-23 |
|
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: 96.02 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFG--GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI-LEQSIDVRRNIGY 78
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MpesppiypemsVQSYLEFVAWIK-GIKMKDIPKRIDAVMEKTSITHVRDRIC--------------GRLSKGYRQRVGL 143
Cdd:cd03252 81 V-----------LQENVLFNRSIRdNIALADPGMSMERVIEAAKLAGAHDFISelpegydtivgeqgAGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVK-NADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-220 |
3.10e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.12 E-value: 3.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPN---EGTATVAGFDILEQSIdvRRNIGYMPESPPIYPEMS 90
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 91 VQSYLEFVAWIKgikMK-DIPK-----RIDAVMEKTSITHVRDRICGR------LSKGYRQRVGLAQALIHNPPVLILDE 158
Cdd:TIGR00955 116 VREHLMFQAHLR---MPrRVTKkekreRVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 159 PTSGLDPKQIIEVRELIKGLA-GEHTVIVSTHiLPEVKLTC--ERVIIINNGWIVAQGTPENLTQ 220
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAqKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-207 |
7.07e-23 |
|
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: 92.13 E-value: 7.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdileqsidvRRNIGYMPe 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYFE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 sppiypemsvqsylefvawikgikmkdipkridavmektsithvrdricgRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:cd03221 70 --------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518567 162 GLDPKQIIEVRELIKGLAGehTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:cd03221 100 HLDLESIEALEEALKEYPG--TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-226 |
7.93e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.23 E-value: 7.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCF--LLPN---EGTATVAGFDILE---QSIDV 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSprtDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESPPIYPeMSVQSYLEFVAWIKGIKMKDIpkrIDAVMEKT----SI-THVRDRICGR---LSKGYRQRVGLA 144
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSlkgaSIwDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 145 QALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKG 224
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
..
gi 931518567 225 KE 226
Cdd:PRK14239 241 KE 242
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-207 |
1.17e-22 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 93.96 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF--GGK--QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR--- 73
Cdd:TIGR02211 1 LLKCENLGKRYqeGKLdtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERakl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 --RNIGYMPESPPIYPEMSVqsyLEFVAW---IKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALI 148
Cdd:TIGR02211 81 rnKKLGFIYQFHHLLPDFTA---LENVAMpllIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 149 HNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTcERVIIINNG 207
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELntSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
1.38e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.29 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI--LEQSIDVRRNIGY 78
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVQSYLeFVAWIKGIKM----------------KDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVG 142
Cdd:PRK11300 85 TFQHVRLFREMTVIENL-LVAQHQQLKTglfsgllktpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
15-226 |
1.57e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 15 QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDV-----RRNIGYMPESPPIYPEM 89
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrREHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 SVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQII 169
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 170 EVRELIKGLAGE-HTVIVSTHIlPEVKLTCERVIIINNGWIVAQGTPENlTQKIKGKE 226
Cdd:PRK10535 182 EVMAILHQLRDRgHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQE-KVNVAGGT 237
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-234 |
1.99e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.27 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIL--------------E 67
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 68 QSIDVRRNIGYMPESPPIYPEMSV-QSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITH-VRDRICGRLSKGYRQRVGLAQ 145
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVlENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 146 ALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKg 224
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ- 244
|
250
....*....|
gi 931518567 225 KERLQLEIGG 234
Cdd:PRK10619 245 SPRLQQFLKG 254
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-215 |
3.20e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.48 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTcfllpneGTATVAGFDIL--EQSI-DV---RRN 75
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIA-------GLEDITSGDLFigEKRMnDVppaERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 156 LDEPTSGLDPK---QI-IEVRELIKGLagEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTP 215
Cdd:PRK11000 157 LDEPLSNLDAAlrvQMrIEISRLHKRL--GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-222 |
3.55e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.41 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-----GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATV----AGFDILEQSID 71
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 72 VR----RNIGYMPESPPIYPEMSVqsyLEFVAWIKGIKMKDIPKRIDAVM-------EKTSITHVRDRICGRLSKGYRQR 140
Cdd:TIGR03269 359 GRgrakRYIGILHQEYDLYPHRTV---LDNLTEAIGLELPDELARMKAVItlkmvgfDEEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 141 VGLAQALIHNPPVLILDEPTSGLDP-------KQIIEVRELIkglagEHTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPitkvdvtHSILKAREEM-----EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
....*....
gi 931518567 214 TPENLTQKI 222
Cdd:TIGR03269 511 DPEEIVEEL 519
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-262 |
4.28e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.84 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR-RNIGYM 79
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELaKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQsylEFVA-----WIKGiKMKDIPKR-IDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPV 153
Cdd:COG4604 81 RQENHINSRLTVR---ELVAfgrfpYSKG-RLTAEDREiIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIV--------STHilpevkltCERVIIINNGWIVAQGTPENLTQkik 223
Cdd:COG4604 157 VLLDEPLNNLDMKHSVQMMKLLRRLADELgkTVVIvlhdinfaSCY--------ADHIVAMKDGRVVAQGTPEEIIT--- 225
|
250 260 270
....*....|....*....|....*....|....*....
gi 931518567 224 gkerlqleiggpgEEVKNALRNVPgvanvqIEIHELDGC 262
Cdd:COG4604 226 -------------PEVLSDIYDTD------IEVEEIDGK 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-216 |
4.87e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF----------------------GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTA 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 59 TV-----------AGFDileqsidvrrnigympesppiyPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRD 127
Cdd:COG1134 84 EVngrvsallelgAGFH----------------------PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 128 RICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP----KQIIEVRELIKGLAgehTVIVSTHILPEVKLTCERVII 203
Cdd:COG1134 142 QPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIRELRESGR---TVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|...
gi 931518567 204 INNGWIVAQGTPE 216
Cdd:COG1134 219 LEKGRLVMDGDPE 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-216 |
1.22e-21 |
|
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: 95.20 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 12 GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR-RNIGYMPESPpiypems 90
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELgRHIGYLPQDV------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 91 vqsylEFVAwikG-IK-----MKDIPKriDAVMEKTSITHVRDRIC--------------GRLSKGYRQRVGLAQALIHN 150
Cdd:COG4618 416 -----ELFD---GtIAeniarFGDADP--EKVVAAAKLAGVHEMILrlpdgydtrigeggARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 151 PPVLILDEPTSGLDPKQIIEVRELIKGL-AGEHTVIVSTH---ILPEvkltCERVIIINNGWIVAQGTPE 216
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHrpsLLAA----VDKLLVLRDGRVQAFGPRD 551
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-189 |
1.60e-21 |
|
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: 94.73 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 12 GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIGYMPESPPIY---- 86
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSVCAQDAHLFdttv 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 87 --------PEMSVQSYLEFVAWIK-GIKMKDIPKRIDAVMEKTSIthvrdricgRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:TIGR02868 426 renlrlarPDATDEELWAALERVGlADWLRALPDGLDTVLGEGGA---------RLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|...
gi 931518567 158 EPTSGLDPKQIIE-VRELIKGLAGEhTVIVSTH 189
Cdd:TIGR02868 497 EPTEHLDAETADElLEDLLAALSGR-TVVLITH 528
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-234 |
1.63e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIG-YM 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 -PESPPIYPEMSVQSYLEFvawikGI-KMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:PRK15439 91 vPQEPLLFPNLSVKENILF-----GLpKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 158 EPTSGLDPkqiIEVREL---IKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQG--------------TPENLT 219
Cdd:PRK15439 166 EPTASLTP---AETERLfsrIRELLAQgVGIVFISHKLPEIRQLADRISVMRDGTIALSGktadlstddiiqaiTPAARE 242
|
250
....*....|....*
gi 931518567 220 QKIKGKERLQLEIGG 234
Cdd:PRK15439 243 KSLSASQKLWLELPG 257
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-218 |
2.12e-21 |
|
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: 94.40 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGG--KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGY 78
Cdd:TIGR02203 331 VEFRNVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLaSLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEmsvqSYLEFVAWIKgikMKDIPK-RIDAVMEKTSITHVRDRI-----------CGRLSKGYRQRVGLAQA 146
Cdd:TIGR02203 411 VSQDVVLFND----TIANNIAYGR---TEQADRaEIERALAAAYAQDFVDKLplgldtpigenGVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 147 LIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENL 218
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGTHNEL 554
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-207 |
3.08e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTatvagfdileqsidVRR----NI 76
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT--------------VKLgetvKI 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMP-ESPPIYPEMSVqsyLEFVAwikgikmkdipkridAVMEKTSITHVR-------------DRICGRLSKGYRQRVG 142
Cdd:COG0488 381 GYFDqHQEELDPDKTV---LDELR---------------DGAPGGTEQEVRgylgrflfsgddaFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDpkqiIEVRE-LIKGLAG-EHTVIVSTH----IlpevKLTCERVIIINNG 207
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLD----IETLEaLEEALDDfPGTVLLVSHdryfL----DRVATRILEFEDG 505
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-194 |
3.37e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 11 FGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdileqsidvRRNIGYMP---ESPPIYP 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPqrsEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 88 eMSVQSYLEFVAWIK----GIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGL 163
Cdd:NF040873 72 -LTVRDLVAMGRWARrglwRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190
....*....|....*....|....*....|..
gi 931518567 164 DPKQIIEVRELIKGLAGEH-TVIVSTHILPEV 194
Cdd:NF040873 151 DAESRERIIALLAEEHARGaTVVVVTHDLELV 182
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-204 |
3.78e-21 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 89.21 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE----QSIDVRRN-IGYM 79
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlnskKASKFRREkLGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:TIGR03608 82 FQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGE-HTVIVSTHIlPEVKLTCERVIII 204
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEgKTIIIVTHD-PEVAKQADRVIEL 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-207 |
3.90e-21 |
|
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: 88.64 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGYMPESPP---IYPEMSVqsy 94
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYVPEDRKregLVLDLSV--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 95 lefvawikgikmkdipkridavMEKTSITHvrdricgRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVREL 174
Cdd:cd03215 96 ----------------------AENIALSS-------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRL 146
|
170 180 190
....*....|....*....|....*....|....
gi 931518567 175 IKGLAGE-HTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:cd03215 147 IRELADAgKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-224 |
4.49e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE-QSIDVRRNIGYMP 80
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLE---------FVAWikgikMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:PRK10253 88 QNATTPGDITVQELVArgryphqplFTRW-----RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE-----NLTQKIKG 224
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKeivtaELIERIYG 242
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
17-230 |
6.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-----VRRNIGYM---PESppiypE 88
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikqIRKKVGLVfqfPES-----Q 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 89 MSVQSYLEFVAWIK---GIKMKDIPKRidaVMEKTSITHVRDRICGR----LSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:PRK13649 98 LFEETVLKDVAFGPqnfGVSQEEAEAL---AREKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 162 GLDPKQIIEVRELIKGL-AGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKERLQL 230
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQL 244
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-225 |
7.84e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 91.34 E-value: 7.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMrILTCFLLPNEGTATVAGFDILEQSIDVRRNIG-YMP 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:NF000106 93 VR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 161 SGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGK 225
Cdd:NF000106 173 TGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGR 238
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-218 |
1.38e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.25 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS----IDVRRN-I 76
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKkI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-218 |
1.88e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMPESPP-IYPEMSVQSY 94
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDnQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 95 LEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVREL 174
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 931518567 175 IKGLAGEH--TVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK13642 183 IHEIKEKYqlTVLSITHDLDEAA-SSDRILVMKAGEIIKEAAPSEL 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-222 |
1.93e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 91.64 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 12 GGKQ-VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIleQSIDVR---RNIGYMPESPPIYP 87
Cdd:TIGR01842 328 GGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADL--KQWDREtfgKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 88 emsvQSYLEFVAwikgiKMKDIPKRiDAVMEKTSITHVRDRICG--------------RLSKGYRQRVGLAQALIHNPPV 153
Cdd:TIGR01842 406 ----GTVAENIA-----RFGENADP-EKIIEAAKLAGVHELILRlpdgydtvigpggaTLSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGL-AGEHTVIVSTHiLPEVkLTC-ERVIIINNGWIVAQGTPENLTQKI 222
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALkARGITVVVITH-RPSL-LGCvDKILVLQDGRIARFGERDEVLAKL 544
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-222 |
2.95e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.64 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 15 QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-----VRRNIGYM---PESPPIy 86
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVfqfPESQLF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 87 pEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSIT-HVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP 165
Cdd:PRK13643 99 -EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 166 KQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKI 222
Cdd:PRK13643 178 KARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEV 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-246 |
3.30e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.32 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLP---NEGTATVAGFDILEQSI-DVRRNIGYMPESPP-IYPE 88
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVwDIREKVGIVFQNPDnQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 89 MSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQI 168
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 169 IEVRELIKGLAGEH--TVIVSTHILPEVKLTcERVIIINNGWIVAQGTPENLTQKIKGKERLQLEIggP-GEEVKNALRN 245
Cdd:PRK13640 180 EQILKLIRKLKKKNnlTVISITHDIDEANMA-DQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDI--PfVYKLKNKLKE 256
|
.
gi 931518567 246 V 246
Cdd:PRK13640 257 K 257
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-258 |
3.50e-20 |
|
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: 90.63 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRIL--TCFLLPNEG----------------------- 56
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGriiyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 57 TATVAGFDILEQSID-----------VRRNIGYMPESP-PIYPEMSV-QSYLEFVAWIkGIKMKDIPKRIDAVMEKTSIT 123
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDfwnlsdklrrrIRKRIAIMLQRTfALYGDDTVlDNVLEALEEI-GYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 124 HVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHiLPEV--KLTcE 199
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH-WPEVieDLS-D 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 200 RVIIINNGWIVAQGTPENLTQK----IKGKERL-QLEIGGPGEEVKNALRN--------VPGVANVQIEIHE 258
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVfmegVSEVEKEcEVEVGEPIIKVRNVSKRyisvdrgvVKAVDNVSLEVKE 309
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-207 |
7.43e-20 |
|
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: 86.33 E-value: 7.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-----GGKQ--VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATV----AGFDILE-- 67
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 68 --QSIDVRRN-IGY-------MPEsppiypemsvQSYLEFVAWikgikmkdiPKRIDAVMEKTSITHVRD-----RICGR 132
Cdd:COG4778 84 prEILALRRRtIGYvsqflrvIPR----------VSALDVVAE---------PLLERGVDREEARARAREllarlNLPER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 L--------SKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVS-THILPEVKLTCERVII 203
Cdd:COG4778 145 LwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRVVD 224
|
....
gi 931518567 204 INNG 207
Cdd:COG4778 225 VTPF 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-189 |
8.40e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTamrILTCF-----LLPN---EGTATVAGFDILEQSID-- 71
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKST---ILRCFnrlndLIPGfrvEGKVTFHGKNLYAPDVDpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 72 -VRRNIGYMPESPPIYPEmSVQSYLEFVAWIKGIK--MKDIPKRidAVMEKTSITHVRDRICGR---LSKGYRQRVGLAQ 145
Cdd:PRK14243 88 eVRRRIGMVFQKPNPFPK-SIYDNIAYGARINGYKgdMDELVER--SLRQAALWDEVKDKLKQSglsLSGGQQQRLCIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 931518567 146 ALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTH 189
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-213 |
8.50e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 8.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 12 GGKQVLFSISFDVNKGEILGFLGPNAAGK-TTAMRILTcfLLPNEGTATVAGFDI----LEQSIDVRRNIGYMPESP--P 84
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKsTTGLALLR--LINSQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQDPnsS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 85 IYPEMSVQSYLEfvawiKGIKM-------KDIPKRIDAVMEKTSI-THVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:PRK15134 375 LNPRLNVLQIIE-----EGLRVhqptlsaAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 157 DEPTSGLD---PKQIIevrELIKGLAGEHTV--IVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:PRK15134 450 DEPTSSLDktvQAQIL---ALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-220 |
1.00e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 89.50 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILtCFLLPN---EGTATVAGFDILEQSI--DVRRN 75
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYPHgtwDGEIYWSGSPLKASNIrdTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVQS--YLEFVAWIKGIKMKD--IPKRIDAVMEKTSITHVRD-RICGRLSKGYRQRVGLAQALIHN 150
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAEniFLGNEITLPGGRMAYnaMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 151 PPVLILDEPTSGLDPKQIIEVRELIKGLAgEHTV--IVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVacVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-209 |
1.11e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.66 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGtATVAGFDILEQsidVRRNIGYMPESPP 84
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAGTAPLAE---AREDTRLMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 85 IYPEMSVqsyLEFVAWikGIKMKDIPKRIDAvMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK11247 92 LLPWKKV---IDNVGL--GLKGQWRDAALQA-LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931518567 165 PKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWI 209
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
1.30e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 86.73 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQ--VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIG 77
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFeKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPiypEMSVQSYLEF-VAWikGIKMKDIP-----KRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:PRK13648 87 IVFQNPD---NQFVGSIVKYdVAF--GLENHAVPydemhRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLTQKIKG 224
Cdd:PRK13648 162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-220 |
1.70e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.99 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE-QSIDVRRNIGYMPESP 83
Cdd:PRK10575 15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 84 PIYPEMSVQsylEFVA-----WIKGIKMKDIPKR--IDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:PRK10575 95 PAAEGMTVR---ELVAigrypWHGALGRFGAADRekVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-189 |
2.30e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.66 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPN-----EGTATVAGFDILEQSID---VR 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpieVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 RNIGYMPESPPIYPEMSVqsyLEFVAWikGIKM-------KDIPKRIDAVMEKTSI-THVRDRI---CGRLSKGYRQRVG 142
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTI---YDNVAI--GVKLnglvkskKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQRLV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTH 189
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-189 |
3.07e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 84.09 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKqVLFS-ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYM 79
Cdd:PRK13538 1 MLEARNLACERDER-ILFSgLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVQSYLEFVAWIKGIKMKDipkRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:PRK13538 80 GHQPGIKTELTALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|....*
gi 931518567 160 TSGLDpKQIIEVrelIKGLAGEHT-----VIVSTH 189
Cdd:PRK13538 157 FTAID-KQGVAR---LEALLAQHAeqggmVILTTH 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-215 |
3.39e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.44 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfDILEQS----IDVRRNI 76
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSkrglLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYM---PESPPIYPEmsVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPV 153
Cdd:PRK13638 80 ATVfqdPEQQIFYTD--IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTP 215
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
4.95e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.16 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGY 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESPPIYPEMSVQSYLEFVAWIkgIKMKDIPKRIDAVMEK-TSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFF--AERDQFQERIKWVYELfPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 158 EPTSGLDPKQIIEVRELIKGLAGEHTVI--VSTHILPEVKLTcERVIIINNGWIVAQGTPENL 218
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIflVEQNANQALKLA-DRGYVLENGHVVLEDTGDAL 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-220 |
5.18e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISkkfgGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID--VRRNIGYMP 80
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaIRAGIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 E---SPPIYPEMSVQ-----SYLEFVAWIKGIKMKDIPKRIDAVMEKTSI-THVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:COG1129 334 EdrkGEGLVLDLSIRenitlASLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDP 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 152 PVLILDEPTSGLDP--KQiiEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:COG1129 414 KVLILDEPTRGIDVgaKA--EIYRLIRELAAEgKAVIVISSELPELLGLSDRILVMREGRIVGELDREEATE 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-211 |
5.31e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG----F----DILEQSIDVrrnig 77
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFasttAALAAGVAI----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 ympesppIY------PEMSVQsylefvawiKGIKMKDIPKRIDAVMEKTSITHVRDRI------------CGRLSKGYRQ 139
Cdd:PRK11288 84 -------IYqelhlvPEMTVA---------ENLYLGQLPHKGGIVNRRLLNYEAREQLehlgvdidpdtpLKYLSIGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931518567 140 RVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVS-THILPEVKLTCERVIIINNGWIVA 211
Cdd:PRK11288 148 MVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYvSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-209 |
5.34e-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: 5.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 15 QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI-LEQSIDVRRNIGYMPESPPIYPEmSVQS 93
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 94 YLEFvawikgiKMKDIPkrIDAVMEKTSITHVRDRIC--------------GRLSKGYRQRVGLAQALIHNPPVLILDEP 159
Cdd:cd03248 107 NIAY-------GLQSCS--FECVKEAAQKAHAHSFISelasgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWI 209
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-221 |
5.76e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 5.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFGGK-QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-VRRNIGYMPESP 83
Cdd:PRK13657 339 DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAsLRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 84 PIY-----------------PEM----SVQSYLEFVAwikgikmkDIPKRIDavmektsiTHVRDRicGR-LSKGYRQRV 141
Cdd:PRK13657 419 GLFnrsiednirvgrpdatdEEMraaaERAQAHDFIE--------RKPDGYD--------TVVGER--GRqLSGGERQRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 142 GLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVR-NADRILVFDNGRVVESGSFDELVAR 559
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-164 |
8.63e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 8.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvrRNIGYMP 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--RGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESppIYPEMSVQSYLEFvawikGIKMKDIPK-----RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK11248 79 EG--LLPWRNVQDNVAF-----GLQLAGVEKmqrleIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
....*....
gi 931518567 156 LDEPTSGLD 164
Cdd:PRK11248 152 LDEPFGALD 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-218 |
1.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKF---GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFL------LPNEGTATVAGFDILE-QSIDVRRN 75
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQiDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVQSYLEFVAWIKGIKMK-DIPKRIDAVMEKTSI-THVRDRI---CGRLSKGYRQRVGLAQALIHN 150
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 151 PPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-207 |
1.09e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 83.00 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE-QSIDV---RRN 75
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVpflRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 156 LDEPTSGLDPkqiiEVRELIKGLAGEH-----TVIVSTHILPEVKLTCERVIIINNG 207
Cdd:PRK10908 161 ADEPTGNLDD----ALSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-218 |
1.35e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.11 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS-----IDVRRNIGYM---PESPPI 85
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknlKKLRKKVSLVfqfPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 86 ypEMSVQSYLEF----------------VAWIKGIKMKDipkridAVMEKTSIthvrdricgRLSKGYRQRVGLAQALIH 149
Cdd:PRK13641 100 --ENTVLKDVEFgpknfgfsedeakekaLKWLKKVGLSE------DLISKSPF---------ELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 150 NPPVLILDEPTSGLDPKQIIEVRELIKGL--AGeHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYqkAG-HTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-218 |
1.40e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.31 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQ-------------------SIDVRR 74
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYdhhylhrqvalvgqepvlfSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIGYMPESPPIYPEMSVQSYLEFVAWIKGikmkdIPKRIDA-VMEKTSithvrdricgRLSKGYRQRVGLAQALIHNPPV 153
Cdd:TIGR00958 574 NIAYGLTDTPDEEIMAAAKAANAHDFIME-----FPNGYDTeVGEKGS----------QLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKglAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENL 218
Cdd:TIGR00958 639 LILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-194 |
1.74e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.16 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCF-----LLPNEGTATVAGFDILEQSIDV---R 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLnrlR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 RNIGYMPESPPIYPeMSVQSYLEF----VAWIKGIKMKDIPKR-IDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALI 148
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYgvkiVGWRPKLEIDDIVESaLKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931518567 149 HNPPVLILDEPTSGLDPKQIIEVRELIKG--LAGEHTVIVSTHILPEV 194
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQV 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-218 |
1.74e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 82.71 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 21 SFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFD------------ILEQS------IDVRRNIGYmpes 82
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtttppsrrpvsMLFQEnnlfshLTVAQNIGL---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 83 pPIYPEMSVQSYlefvawiKGIKMKDIPKRIdavmektSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSG 162
Cdd:PRK10771 95 -GLNPGLKLNAA-------QREKLHAIARQM-------GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 163 LDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-220 |
2.36e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTamrILTCF--LLPNEGTATVAGFDILEQSI-DVRRNIGYMPESPPIYPEMSVQS 93
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 94 YLE-FVAwiKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQAL--IH---NP--PVLILDEPTSGLDP 165
Cdd:PRK03695 89 YLTlHQP--DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWpdiNPagQLLLLDEPMNSLDV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 166 KQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQG------TPENLTQ 220
Cdd:PRK03695 167 AQQAALDRLLSELCQQGiAVVMSSHDLNHTLRHADRVWLLKQGKLLASGrrdevlTPENLAQ 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-233 |
3.01e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.42 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRIL------TcfllPNEGTATVAGFDILEQSID--VRRNI 76
Cdd:COG0396 4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghpkyE----VTSGSILLDGEDILELSPDerARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGR-----LSKGYRQRVGLAQALIHNP 151
Cdd:COG0396 80 FLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRyvnegFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 152 PVLILDEPTSGLDpkqiIE----VRELIKGLAGEHT-VIVSTH---ILPEVKltCERVIIINNGWIVAQGTPEnLTQKI- 222
Cdd:COG0396 160 KLAILDETDSGLD----IDalriVAEGVNKLRSPDRgILIITHyqrILDYIK--PDFVHVLVDGRIVKSGGKE-LALELe 232
|
250
....*....|..
gi 931518567 223 -KGKERLQLEIG 233
Cdd:COG0396 233 eEGYDWLKEEAA 244
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-216 |
3.14e-18 |
|
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: 81.03 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCF--LLPNEGTATVAGFDILEQSID--VRRNIGYMP 80
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerARLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAwiKGikmkdipkridavmektsithvrdricgrLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:cd03217 84 QYPPEIPGVKNADFLRYVN--EG-----------------------------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 161 SGLDPKQIIEVRELIKGLAGEHT-VIVSTH---ILPEVKLTceRVIIINNGWIVAQGTPE 216
Cdd:cd03217 133 SGLDIDALRLVAEVINKLREEGKsVLIITHyqrLLDYIKPD--RVHVLYDGRIVKSGDKE 190
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-227 |
7.16e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 7.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATvagfdILEQSID--VRRN-IGYMPES------- 82
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIS-----ILGQPTRqaLQKNlVAYVPQSeevdwsf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 83 PPIYPEMSVQSYLEFVAWIKGIKMKDiPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSG 162
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 163 LDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIInNGWIVAQG------TPENLTQKIKGKER 227
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGptettfTAENLELAFSGVLR 243
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
5-202 |
7.85e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 80.91 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDV-RRNIGYMPESP 83
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 84 PIYPEmSVQSYLEFVAWIKGIKMKdiPKRIDAVMEKTSI-THVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSG 162
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931518567 163 LDPKQIIEVRELIKGLAGEHTVIV--STHILPEVKlTCERVI 202
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEIN-HADKVI 208
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-215 |
1.57e-17 |
|
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: 79.85 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF--GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAM----RILTCFllpnEGTATVAGFDIleQSI---DV 72
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVELS----SGSILIDGVDI--SKIglhDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNIGYMPESP------------P--IYPEMSVQSYLEFVawikgiKMKDI----PKRIDAVMEKtsithvrdriCGR-L 133
Cdd:cd03244 77 RSRISIIPQDPvlfsgtirsnldPfgEYSDEELWQALERV------GLKEFveslPGGLDTVVEE----------GGEnL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 134 SKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVkLTCERVIIINNGWIVAQG 213
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFD 219
|
..
gi 931518567 214 TP 215
Cdd:cd03244 220 SP 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-220 |
1.98e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMR-ILTCFLLPNEGTATVAG--FDILEQSIDVRRNIGYMPESPP---IYPEMSVQ- 92
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGkpVKIRNPQQAIAQGIAMVPEDRKrdgIVPVMGVGk 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 93 -----SYLEFVAWI---KGIKMKDIPKRIDAVMEKTSitHVRDRIcGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK13549 361 nitlaALDRFTGGSridDAAELKTILESIQRLKVKTA--SPELAI-ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 165 PKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGvAIIVISSELPEVLGLSDRVLVMHEGKLKGDLINHNLTQ 494
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-164 |
2.18e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.29 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGG----KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIleQSIDVRRNI 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV--TGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESppIYPEMSVQSYLEFvawikGIKMKDIPK-----RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:COG4525 81 VFQKDA--LLPWLNVLDNVAF-----GLRLRGVPKaerraRAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170
....*....|...
gi 931518567 152 PVLILDEPTSGLD 164
Cdd:COG4525 154 RFLLMDEPFGALD 166
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-232 |
2.76e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.21 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSID-----VRRNIGYM---PESPPI 85
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirpVRKRIGMVfqfPESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 86 ypEMSVQSYLEFVAWIKGIKMKDIPKR-IDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK13646 100 --EDTVEREIIFGPKNFKMNLDEVKNYaHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 165 PKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKERLQLEI 232
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKLADWHIGL 247
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-220 |
2.89e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTamrILTCF--LLPNEGTATVAGFDILEQSID---VRRniGYMPE--SPPiyPEM 89
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAelaRHR--AYLSQqqSPP--FAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 SVQSYLEFVAwIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQAL--IH---NPP--VLILDEPTSG 162
Cdd:COG4138 85 PVFQYLALHQ-PAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWptiNPEgqLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 163 LDPKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQG------TPENLTQ 220
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQGiTVVMSSHDLNHTLRHADRVWLLKQGKLVASGetaevmTPENLSE 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-191 |
3.19e-17 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 79.72 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 27 GEILGFLGPNAAGKTTAMRILTCFLLPN-----------------EGTATVAGF-DILEQSIDVRRNIGYMPESPpiype 88
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNlgkfddppdwdeildefRGSELQNYFtKLLEGDVKVIVKPQYVDLIP----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 89 msvqsylefvAWIKG-----IKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGL 163
Cdd:cd03236 101 ----------KAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180
....*....|....*....|....*....
gi 931518567 164 DPKQIIEVRELIKGLAGE-HTVIVSTHIL 191
Cdd:cd03236 171 DIKQRLNAARLIRELAEDdNYVLVVEHDL 199
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
3.23e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.52 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGK-----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNI 76
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 gympesppIYPEMSVQsyLEFVAWIKgiKMKDIPKRIDAVME-------KTSIThvRDRICG------------------ 131
Cdd:PRK13651 83 --------VLEKLVIQ--KTRFKKIK--KIKEIRRRVGVVFQfaeyqlfEQTIE--KDIIFGpvsmgvskeeakkraaky 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 132 ----------------RLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEV 194
Cdd:PRK13651 149 ielvgldesylqrspfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNV 228
|
250 260
....*....|....*....|.
gi 931518567 195 KLTCERVIIINNGWIVAQGTP 215
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGDT 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-203 |
5.44e-17 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 81.37 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFGGkqvlFSISFD---VNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGtatvagfdileqSIDVRRNIGYMPES 82
Cdd:COG1245 346 DLTKSYGG----FSLEVEggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG------------EVDEDLKISYKPQY 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 83 PPIYPEMSVQSYLEfvawikgikmKDIPKRIDA------VMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLIL 156
Cdd:COG1245 410 ISPDYDGTVEEFLR----------SANTDDFGSsyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931518567 157 DEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVII 203
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-221 |
5.69e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISkkFG----GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS-IDVRRNI 76
Cdd:PRK11160 339 LTLNNVS--FTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSeAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYP--------------------EMSVQSYLEfvawikgiKMKDIPKRIDAVMEKTsithvrdricGR-LSK 135
Cdd:PRK11160 417 SVVSQRVHLFSatlrdnlllaapnasdealiEVLQQVGLE--------KLLEDDKGLNAWLGEG----------GRqLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 136 GYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHilpevKLTC----ERVIIINNGWIVA 211
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH-----RLTGleqfDRICVMDNGQIIE 553
|
250
....*....|
gi 931518567 212 QGTPENLTQK 221
Cdd:PRK11160 554 QGTHQELLAQ 563
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-218 |
1.22e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.11 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGG----KQVLFSISFDVNKGEILGFLGPNAAGKT-TAMRILTcfLLPN-----EGTATVAGFDILEQSI 70
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILR--LLPDpaahpSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 71 D----VR-RNIGyMpesppIYPE--------MSVQSYL-EFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRIcGR---- 132
Cdd:COG4172 84 RelrrIRgNRIA-M-----IFQEpmtslnplHTIGKQIaEVLRLHRGLSGAAARARALELLERVGIPDPERRL-DAyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP---KQIIevrELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNG 207
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQIL---DLLKDLQRELgmALLLITHDLGVVRRFADRVAVMRQG 233
|
250
....*....|.
gi 931518567 208 WIVAQGTPENL 218
Cdd:COG4172 234 EIVEQGPTAEL 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-218 |
1.38e-16 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.11 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLF-----------SISFDVNKGEILGFLGPNAAGKTT-AMRILTcfLLPNEGTATVAGFDIL--- 66
Cdd:COG4172 276 LEARDLKVWFPIKRGLFrrtvghvkavdGVSLTLRRGETLGLVGESGSGKSTlGLALLR--LIPSEGEIRFDGQDLDgls 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 67 -EQSIDVRRNIGYMPESPpiY----PEMSVQsylEFVA---WIKGIKM--KDIPKRIDAVMEKTSITH-VRDRICGRLSK 135
Cdd:COG4172 354 rRALRPLRRRMQVVFQDP--FgslsPRMTVG---QIIAeglRVHGPGLsaAERRARVAEALEEVGLDPaARHRYPHEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 136 GYRQRVGLAQALIHNPPVLILDEPTSGLD---PKQIIevrELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIV 210
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDvsvQAQIL---DLLRDLQREHglAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
....*...
gi 931518567 211 AQGTPENL 218
Cdd:COG4172 506 EQGPTEQV 513
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-189 |
1.54e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.81 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 16 VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIleQSIDVRRNIGYMPESPPIYPEMSVQSYL 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA--TRGDRSRFMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 96 EFVAWIKGIKMKDIPKRIDAVMektSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELI 175
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170
....*....|....*
gi 931518567 176 KG-LAGEHTVIVSTH 189
Cdd:PRK13543 181 SAhLRGGGAALVTTH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-189 |
1.75e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGkqvlFSISFD---VNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGtatvagfdileqSIDVRRNIG 77
Cdd:PRK13409 340 LVEYPDLTKKLGD----FSLEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG------------EVDPELKIS 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYPEMSVQSYLEFVA------WIKGIKMKdiPKRIDAVMEKtsitHVRDricgrLSKGYRQRVGLAQALIHNP 151
Cdd:PRK13409 404 YKPQYIKPDYDGTVEDLLRSITddlgssYYKSEIIK--PLQLERLLDK----NVKD-----LSGGELQRVAIAACLSRDA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTH 189
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-191 |
2.06e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 79.44 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 26 KGEILGFLGPNAAGKTTAMRILTCFLLPNEGtatvagfdileqsidvrrnigyMPESPPIYPE-------MSVQSYLEFV 98
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLG----------------------DYDEEPSWDEvlkrfrgTELQDYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 99 A------------------WIKGiKMKDIPKRID------AVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:COG1245 156 AngeikvahkpqyvdlipkVFKG-TVRELLEKVDergkldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*...
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGEH-TVIVSTHIL 191
Cdd:COG1245 235 FFDEPSSYLDIYQRLNVARLIRELAEEGkYVLVVEHDL 272
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-215 |
2.25e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.73 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK-QVLFSISFDVNKGEILGFLGPNAAGKTTAMRIltcfllpnegtatVAGfdiLEQ------SIDVR 73
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRM-------------VAG---LERitsgeiWIGGR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 ---------RNIGYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLA 144
Cdd:PRK11650 67 vvnelepadRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 145 QALIHNPPVLILDEPTSGLDPK---QI-IEVRELIKGLAGehTVIVSTHILPEVKLTCERVIIINNGWIVAQGTP 215
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAKlrvQMrLEIQRLHRRLKT--TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTP 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-210 |
3.11e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 77.03 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGG---------KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIL----E 67
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnrA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 68 QSIDVRRNIGYMPESPP--IYPEMSVQSYL-EFVAWIKGIKMKDIPKRIDAVMEKTSIT-HVRDRICGRLSKGYRQRVGL 143
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSIsaVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGL---AGEHTVIVsTHILPEVKLTCERVIIINNGWIV 210
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqqqFGTACLFI-THDLRLVERFCQRVMVMDNGQIV 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-191 |
3.90e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 3.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 26 KGEILGFLGPNAAGKTTAMRILTCFLLPNEGTatvagfdileqsidvrrnigymPESPPIYPEM-------SVQSYLEFV 98
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD----------------------YEEEPSWDEVlkrfrgtELQNYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 99 A------------------WIKGiKMKDIPKRID------AVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:PRK13409 156 YngeikvvhkpqyvdlipkVFKG-KVRELLKKVDergkldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*..
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHIL 191
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
20-221 |
4.56e-16 |
|
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: 78.33 E-value: 4.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMR-ILTCFLLPNEGTATVAG--FDILEQSIDVRRNIGYMPESPP---IYPEMSVQS 93
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGkpVDIRNPAQAIRAGIAMVPEDRKrhgIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 94 YLEFVAWIK--GIKMKDIPKRIDAVMEKTSITHVR----DRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQ 167
Cdd:TIGR02633 359 NITLSVLKSfcFKMRIDAAAELQIIGSAIQRLKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 168 IIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:TIGR02633 439 KYEIYKLINQLAQEGvAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQE 493
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-220 |
6.67e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILtCFLLPN---EGTATVAGFDILEQSI-DVRRN-IGYM 79
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPHgtyEGEIIFEGEELQASNIrDTERAgIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 80 PESPPIYPEMSVqsyLE--FVA--WIKGIKMkDIPK---RIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPP 152
Cdd:PRK13549 88 HQELALVKELSV---LEniFLGneITPGGIM-DYDAmylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 153 VLILDEPTSGLDPKQIIEVRELIKGLAgEHTV--IVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQ 220
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLK-AHGIacIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTE 232
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-189 |
7.95e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.00 E-value: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFGGKQ-------------VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFD--ILEQsi 70
Cdd:PLN03211 60 NIKRILGHKPkisdetrqiqertILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNrkPTKQ-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 71 dVRRNIGYMPESPPIYPEMSVQSYLEFVAWI---KGIKMKDIPKRIDAVMEKTSITHVRDRICGR-----LSKGYRQRVG 142
Cdd:PLN03211 138 -ILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVS 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTH 189
Cdd:PLN03211 217 IAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKgKTIVTSMH 264
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-164 |
9.49e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.31 E-value: 9.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFS-----------ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS- 69
Cdd:COG4608 8 LEVRDLKKHFPVRGGLFGrtvgvvkavdgVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 70 ---IDVRRNIGYMPESPpiY----PEMSVQSYLEFVAWIKGIKMK-DIPKRIDAVMEKtsithVR------DRICGRLSK 135
Cdd:COG4608 88 relRPLRRRMQMVFQDP--YaslnPRMTVGDIIAEPLRIHGLASKaERRERVAELLEL-----VGlrpehaDRYPHEFSG 160
|
170 180
....*....|....*....|....*....
gi 931518567 136 GYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-207 |
1.66e-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: 74.42 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDvrRNIGYMPESppIYPEMSVQsylEFVA 99
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYS--LLPWLTVR---ENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 100 WIKGIKMKDIPKR-----IDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVREL 174
Cdd:TIGR01184 77 LAVDRVLPDLSKSerraiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 931518567 175 IKGLAGEH--TVIVSTHILPEVKLTCERVIIINNG 207
Cdd:TIGR01184 157 LMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-220 |
1.76e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNIS-KKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLlPNEGTATVAGfdileqsIDVRrnigymp 80
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKING-------IELR------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 esppiypEMSVQSYLEFVAWI-------KG-----IKMKDI---PKRIDAVMEKTSI------------THVRDRiCGRL 133
Cdd:PRK11174 415 -------ELDPESWRKHLSWVgqnpqlpHGtlrdnVLLGNPdasDEQLQQALENAWVseflpllpqgldTPIGDQ-AAGL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 134 SKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQG 213
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLA-QWDQIWVMQDGQIVQQG 565
|
....*..
gi 931518567 214 TPENLTQ 220
Cdd:PRK11174 566 DYAELSQ 572
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-203 |
2.11e-15 |
|
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: 74.37 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 23 DVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDileqsidvrrnIGYMPESPPIYPEMSVQSYLEFVAWIK 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-----------VSYKPQYIKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 103 GIKmkdiPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH 182
Cdd:cd03237 90 YTH----PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180
....*....|....*....|...
gi 931518567 183 --TVIVSTHILPEVKLTCERVII 203
Cdd:cd03237 166 ekTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-222 |
2.86e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRN-IGYMPESP---------PIYPE 88
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLANgIVYISEDRkrdglvlgmSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 89 MSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSI-THVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQ 167
Cdd:PRK10762 351 MSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 168 IIEVRELIKGLAGE--HTVIVSTHiLPEVKLTCERVIIINNGWIVAQGTPENLTQKI 222
Cdd:PRK10762 431 KKEIYQLINQFKAEglSIILVSSE-MPEVLGMSDRILVMHEGRISGEFTREQATQEK 486
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-258 |
3.92e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGT---------------ATVAGFDILEQS 69
Cdd:PRK10762 8 KGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSilylgkevtfngpksSQEAGIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 70 IDvrrnigympesppIYPEMSVQS--YL--EFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQ 145
Cdd:PRK10762 88 LN-------------LIPQLTIAEniFLgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 146 ALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVS-THILPEVKLTCERVIIINNG-WI----VAQGTPENLT 219
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYiSHRLKEIFEICDDVTVFRDGqFIaereVADLTEDSLI 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 931518567 220 QKIKGKE------RLQLEIGGPGEEVKNAlrNVPGVANVQIEIHE 258
Cdd:PRK10762 235 EMMVGRKledqypRLDKAPGEVRLKVDNL--SGPGVNDVSFTLRK 277
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-221 |
4.67e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVaGFDILEQSID------VRRNIGYM---PESPPIyp 87
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkklkpLRKKVGIVfqfPEHQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 88 EMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITH-VRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPK 166
Cdd:PRK13634 100 EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 167 QIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKglTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-211 |
4.94e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 4 AKNISKKFGGKqvLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS--IDVRRNIGYMPE 81
Cdd:PRK09700 268 VRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSplDAVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 S---PPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRI---C-------GRLSKGYRQRVGLAQALI 148
Cdd:PRK09700 346 SrrdNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLalkChsvnqniTELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 149 HNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVI--VSTHiLPEVKLTCERVIIINNGWIVA 211
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIlmVSSE-LPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-215 |
5.39e-15 |
|
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: 72.44 E-value: 5.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGK--QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI----LEqsiDVRRN 75
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstipLE---DLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYMPESPPIYpEMSVQSYLefvawikgikmkDIPKRID--AVMEKTSITHVRDRicgrLSKGYRQRVGLAQALIHNPPV 153
Cdd:cd03369 84 LTIIPQDPTLF-SGTIRSNL------------DPFDEYSdeEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVkLTCERVIIINNGWIVAQGTP 215
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
6.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.12 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQ-----VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIlEQSIDVRRN 75
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYI-GDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 IGYmPESPPI---------------YPEM-----SVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITH-VRDRICGRLS 134
Cdd:PRK13631 100 ITN-PYSKKIknfkelrrrvsmvfqFPEYqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 135 KGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIK-GLAGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILdAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
..
gi 931518567 214 TP 215
Cdd:PRK13631 259 TP 260
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-191 |
6.74e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.97 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATV------AGFDILEQSIDVRRN 75
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklAYVDQSRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 76 igympesppIYPEMSvqsylefvawiKGIKMKDIPKRidavmEKTSITHV---------RDRICGRLSKGYRQRVGLAQA 146
Cdd:TIGR03719 403 ---------VWEEIS-----------GGLDIIKLGKR-----EIPSRAYVgrfnfkgsdQQKKVGQLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 931518567 147 LIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVI---------VSTHIL 191
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVIshdrwfldrIATHIL 511
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-218 |
1.05e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS----IDVRRNI 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrlYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVqsyLEFVAWIKGiKMKDIPKRI--DAVMEKTSITHVR---DRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:PRK11831 87 SMLFQSGALFTDMNV---FDNVAYPLR-EHTQLPAPLlhSTVMMKLEAVGLRgaaKLMPSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGL--AGEHTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
14-217 |
1.16e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 73.76 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVN-----KGeILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG---FDIlEQSIDV---RRNIGYMPES 82
Cdd:PRK11144 7 KQQLGDLCLTVNltlpaQG-ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDA-EKGICLppeKRRIGYVFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 83 PPIYPEMSVQSYLEFvawikGIKMKDiPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSG 162
Cdd:PRK11144 85 ARLFPHYKVRGNLRY-----GMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931518567 163 LD-PKQiievRELI---KGLAGE-HTVIV-STHILPEVKLTCERVIIINNGWIVAQGTPEN 217
Cdd:PRK11144 159 LDlPRK----RELLpylERLAREiNIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-207 |
1.52e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.96 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 8 SKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdileqsidvrrNIGYMPESPPIYP 87
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 88 eMSVQSYLEFvawikGIKMKdiPKRIDAVMEKTSI------------THVRDRicGR-LSKGYRQRVGLAQALIHNPPVL 154
Cdd:cd03250 80 -GTIRENILF-----GKPFD--EERYEKVIKACALepdleilpdgdlTEIGEK--GInLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 155 ILDEPTSGLDP---KQIIEvrELIKG-LAGEHTVIVSTH---ILPEvkltCERVIIINNG 207
Cdd:cd03250 150 LLDDPLSAVDAhvgRHIFE--NCILGlLLNNKTRILVTHqlqLLPH----ADQIVVLDNG 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-214 |
2.10e-14 |
|
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: 73.70 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 15 QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI--LEQSiDVRRNIGYMPESP-----PIY- 86
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdVTQA-SLRAAIGIVPQDTvlfndTIAy 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 87 ------PEMSVQsylEFVAWIKGIKMKD----IPKRIDavmektsiTHVRDRicG-RLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:COG5265 451 niaygrPDASEE---EVEAAARAAQIHDfiesLPDGYD--------TRVGER--GlKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVkLTCERVIIINNGWIVAQGT 214
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI-VDADEILVLEAGRIVERGT 575
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-189 |
5.10e-14 |
|
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: 69.19 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNIS----KKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTcfllpNEGTATVAGFDIL----EQSIDVR 73
Cdd:cd03232 4 LTWKNLNytvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA-----GRKTAGVITGEILingrPLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 74 RNIGYMPESPPIYPEMSVQSYLEFVAWIKGIkmkdipkridavmektSITHvrdricgrlskgyRQRVGLAQALIHNPPV 153
Cdd:cd03232 79 RSTGYVEQQDVHSPNLTVREALRFSALLRGL----------------SVEQ-------------RKRLTIGVELAAKPSI 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTH 189
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADSgQAILCTIH 166
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-221 |
7.22e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.97 E-value: 7.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQV--LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILE------------ 67
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDytlaslrnqval 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 68 --QSI-----DVRRNIGYMPESppIYPEMSVQ-----SY-LEFVawikgIKMKDipkRIDAVMEKTSIThvrdricgrLS 134
Cdd:PRK11176 422 vsQNVhlfndTIANNIAYARTE--QYSREQIEeaarmAYaMDFI-----NKMDN---GLDTVIGENGVL---------LS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 135 KGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKLTCErVIIINNGWIVAQGT 214
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADE-ILVVEDGEIVERGT 561
|
....*..
gi 931518567 215 PENLTQK 221
Cdd:PRK11176 562 HAELLAQ 568
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-216 |
8.33e-14 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 71.29 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGK----------------------QVL--FSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEG 56
Cdd:COG4175 3 KIEVRNLYKIFGKRperalklldqgkskdeilektgQTVgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 57 TATVAGFDIL----EQSIDVRR--------NIGYMPEsppiypeMSVqsyLEFVAW---IKGIKMKDIPKRIDAVMEKTS 121
Cdd:COG4175 83 EVLIDGEDITklskKELRELRRkkmsmvfqHFALLPH-------RTV---LENVAFgleIQGVPKAERRERAREALELVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 122 ITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPkqIIevR-----ELIKgLAGEH--TVIVSTHILPE- 193
Cdd:COG4175 153 LAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP--LI--RremqdELLE-LQAKLkkTIVFITHDLDEa 227
|
250 260
....*....|....*....|...
gi 931518567 194 VKLTcERVIIINNGWIVAQGTPE 216
Cdd:COG4175 228 LRLG-DRIAIMKDGRIVQIGTPE 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-209 |
9.29e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 9.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIG--YMPE---------SPPIYPE 88
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPEdrqssglylDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 89 MSVQSYLEFVAWIKgikmkdiPKRIDAVMEK------TSITHVrDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSG 162
Cdd:PRK15439 362 VCALTHNRRGFWIK-------PARENAVLERyrralnIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 931518567 163 LDPKQIIEVRELIKGLAGEHT-VIVSTHILPEVKLTCERVIIINNGWI 209
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-213 |
3.15e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 3.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDileqsiDVRRNIGYMP 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD------GQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPpiypemsvQSYLEFVAW-------IKGIKMK-----DIPKRIDAV---------------MEKTSITHVR-DRICGR 132
Cdd:PRK11701 80 EAE--------RRRLLRTEWgfvhqhpRDGLRMQvsaggNIGERLMAVgarhygdiratagdwLERVEIDAARiDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQALIHNPPVLILDEPTSGLDpkqiIEVR----ELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINN 206
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD----VSVQarllDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQ 227
|
....*..
gi 931518567 207 GWIVAQG 213
Cdd:PRK11701 228 GRVVESG 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
5.01e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFG-G----KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR-R 74
Cdd:COG1101 1 MLELKNLSKTFNpGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIGYMPESPPI--YPEMSVQSYLEfVAWIKG----IKMKDIPKRIDAVMEKTSIT------HVRDRIcGRLSKGYRQRVG 142
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLA-LAYRRGkrrgLRRGLTKKRRELFRELLATLglglenRLDTKV-GLLSGGQRQALS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILpEVKLTC-ERVIIINNGWIVAQgtpenlt 219
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM-EQALDYgNRLIMMHEGRIILD------- 230
|
250
....*....|...
gi 931518567 220 qkIKGKERLQLEI 232
Cdd:COG1101 231 --VSGEEKKKLTV 241
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-204 |
6.02e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 69.55 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKF--GGKQVLFSISFDVNKGEILGFLGPNAAGKTTamrILTCFL--LPNEGTATVAGfdILEQSIDV---RRNIG 77
Cdd:TIGR01271 1221 QGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLrlLSTEGEIQIDG--VSWNSVTLqtwRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 YMPESPPIYP---EMSVQSYLEF-------VAWIKGIK--MKDIPKRIDAVMEKTSIThvrdricgrLSKGYRQRVGLAQ 145
Cdd:TIGR01271 1296 VIPQKVFIFSgtfRKNLDPYEQWsdeeiwkVAEEVGLKsvIEQFPDKLDFVLVDGGYV---------LSNGHKQLMCLAR 1366
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 146 ALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILpEVKLTCERVIII 204
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVI 1424
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-218 |
1.16e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.96 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEgtATVAGFDILEQSI--------DV 72
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDK--SAGSHIELLGRTVqregrlarDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRN---IGYMPESPPIYPEMSVQSYLEFVA------WIKGIK--MKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRV 141
Cdd:PRK09984 82 RKSranTGYIFQQFNLVNRLSVLENVLIGAlgstpfWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 142 GLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-191 |
1.34e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.99 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFG-GK---QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVR-----RNI 76
Cdd:PRK11629 10 NLCKRYQeGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVqsyLEFVAW---IKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPV 153
Cdd:PRK11629 90 GFIYQFHHLLPDFTA---LENVAMpllIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931518567 154 LILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHIL 191
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDL 206
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-213 |
3.03e-12 |
|
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: 64.59 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNIS----KKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPN---EGTATVAGFDILEQSIDVRR 74
Cdd:cd03233 4 LSWRNISfttgKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIGYMPESPPIYPEMSVQSYLEFVAWIKGIKMkdipkridavmektsithVRDricgrLSKGYRQRVGLAQALIHNPPVL 154
Cdd:cd03233 84 EIIYVSEEDVHFPTLTVRETLDFALRCKGNEF------------------VRG-----ISGGERKRVSIAEALVSRASVL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVS-THILPEVKLTCERVIIINNGWIVAQG 213
Cdd:cd03233 141 CWDNSTRGLDSSTALEILKCIRTMADVLktTTFVSlYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-231 |
3.29e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 6 NISKKFGGK-----QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATV------AGFDILEQSIDVRR 74
Cdd:PRK13645 11 NVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIGYMPESPP--IYPEmSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITH-VRDRICGRLSKGYRQRVGLAQALIHNP 151
Cdd:PRK13645 91 EIGLVFQFPEyqLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGEHT--VIVSTHILPEVKLTCERVIIINNGWIVAQGTPENLTQKIKGKERLQ 229
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIE 249
|
..
gi 931518567 230 LE 231
Cdd:PRK13645 250 ID 251
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-218 |
4.24e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKF--GG--KQVLFSISFDVNKGEILGFLGPNAAGKT-TAMRILTcfLLPN------EGTATVAGFDIL--- 66
Cdd:PRK15134 5 LLAIENLSVAFrqQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESLLhas 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 67 EQSI-DVRRNIGYMPESPPIY---PEMSVQSYL-EFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICG---RLSKGYR 138
Cdd:PRK15134 83 EQTLrGVRGNKIAMIFQEPMVslnPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDyphQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 139 QRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE--HTVIVSTHILPEVKLTCERVIIINNGWIVAQGTPE 216
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElnMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
..
gi 931518567 217 NL 218
Cdd:PRK15134 243 TL 244
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-230 |
4.84e-12 |
|
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: 65.26 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKF--GGKQVLFSISFDVNKGEILGFLGPNAAGKTTamrILTCFL--LPNEGTATVAGfdILEQSIDV---RR 74
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKST---LLSAFLrlLNTEGDIQIDG--VSWNSVPLqkwRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIGYMPESPPIYPEMSVQSYLEFVAWikgiKMKDIPKRIDAVMEKTSITHVRDRI--------CgRLSKGYRQRVGLAQA 146
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDPYGKW----SDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggC-VLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 147 LIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILpEVKLTCERVIIINNGWIVAQGTPENL-------T 219
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLlnekshfK 231
|
250
....*....|.
gi 931518567 220 QKIKGKERLQL 230
Cdd:cd03289 232 QAISPSDRLKL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-307 |
5.34e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTatvagfdileqSIDVRRNIGYMPESPPIYpEMSVQS 93
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS-----------SVVIRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 94 YLEFvawikGIKMKdiPKRIDAVMEKTSITHVRDRICGR-----------LSKGYRQRVGLAQALIHNPPVLILDEPTSG 162
Cdd:PLN03232 698 NILF-----GSDFE--SERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 163 LDPKQIIEVRE--LIKGLAGEHTVIVST--HILPEVkltcERVIIINNGWIVAQGTPENLTQKikgkerlqleiggpGEE 238
Cdd:PLN03232 771 LDAHVAHQVFDscMKDELKGKTRVLVTNqlHFLPLM----DRIILVSEGMIKEEGTFAELSKS--------------GSL 832
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 239 VKNALRNVpGVANVQIEIHELDGCFKYIVETeVKADIKKNLARIIADNKWDL-----YEMRTLGMTLEEIFMRY 307
Cdd:PLN03232 833 FKKLMENA-GKMDATQEVNTNDENILKLGPT-VTIDVSERNLGSTKQGKRGRsvlvkQEERETGIISWNVLMRY 904
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-218 |
1.37e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 64.34 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQ---------------------SIDVRRNIGY 78
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddewravrsdiqmifqdplaSLNPRMTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 79 MPESP--PIYPEMSVQsylefvawikgikmkDIPKRIDAVMEKTSI-THVRDRICGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK15079 120 IIAEPlrTYHPKLSRQ---------------EVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-218 |
2.69e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQS-ID-VRRNIGYMPE---SPPIYPEMSVQ-- 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDaIRAGIMLCPEdrkAEGIIPVHSVAdn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 93 -------SYLEFVAWIKGIKMKDIPKR-IDAVMEKTSithVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK11288 352 inisarrHHLRAGCLINNRWEAENADRfIRSLNIKTP---SREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 165 PKQIIEVRELIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIV-----AQGTPENL 218
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGvAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQA 488
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-218 |
3.12e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 16 VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMPESPPIYP---EMSV 91
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLtDLRRVLSIIPQSPVLFSgtvRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 92 QSYLEFV---AW--IKGIKMKDIPKR----IDA-VMEKTSithvrdricgRLSKGYRQRVGLAQALIHNPPVLILDEPTS 161
Cdd:PLN03232 1331 DPFSEHNdadLWeaLERAHIKDVIDRnpfgLDAeVSEGGE----------NFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 162 GLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENL 218
Cdd:PLN03232 1401 SVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQEL 1456
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-221 |
3.37e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 16 VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMPESPPIYpEMSVQSY 94
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLmDLRKVLGIIPQAPVLF-SGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 95 LEFVA-------W--IKGIKMKDIPKR----IDA-VMEKTSithvrdricgRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:PLN03130 1333 LDPFNehndadlWesLERAHLKDVIRRnslgLDAeVSEAGE----------NFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 161 SGLDPKQ--IIE--VRELIKGLagehTVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:PLN03130 1403 AAVDVRTdaLIQktIREEFKSC----TMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-189 |
3.78e-11 |
|
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: 63.80 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKF-GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILtcfllpnegtatvAGFD-------ILEQSIdvrrNI 76
Cdd:TIGR03719 8 NRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGVDkdfngeaRPQPGI----KV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSV-QSYLEFVAWIKGI---------KMKDIPKRIDAVMEKTsiTHVRDRI----------------- 129
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVrENVEEGVAEIKDAldrfneisaKYAEPDADFDKLAAEQ--AELQEIIdaadawdldsqleiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 130 ---C-------GRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGehTVIVSTH 189
Cdd:TIGR03719 149 alrCppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-218 |
4.28e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPN---EGTATVAGFDIL---EQSIDVRR--NIGYMPESP--PIYPEM 89
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILnlpEKELNKLRaeQISMIFQDPmtSLNPYM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 SVQSYLEFV-----------AWIKGIKMkdipkrIDAVmektSITHVRDRIC---GRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK09473 115 RVGEQLMEVlmlhkgmskaeAFEESVRM------LDAV----KMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIVAQGTPENL 218
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-171 |
8.29e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYMP 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYLEFVAWIKGIKMKdipkrIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170
....*....|.
gi 931518567 161 SGLDPKQIIEV 171
Cdd:PRK13540 156 VALDELSLLTI 166
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-191 |
1.05e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAgfdileQSIDvrrnIGYMPE 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG------ETVK----LAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 82 S-PPIYPEMSVqsylefvaW--IKG----IKM--KDIPKR--IDAVMEKTSithvrD--RICGRLSKGYRQRVGLAQALI 148
Cdd:PRK11819 395 SrDALDPNKTV--------WeeISGgldiIKVgnREIPSRayVGRFNFKGG-----DqqKKVGVLSGGERNRLHLAKTLK 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 149 HNPPVLILDEPTSGLDpkqiIE-VRELIKGL---AGEHTVI---------VSTHIL 191
Cdd:PRK11819 462 QGGNVLLLDEPTNDLD----VEtLRALEEALlefPGCAVVIshdrwfldrIATHIL 513
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-213 |
1.37e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTC----FLLPNEGTATVAGFDILEQSIDVRRNIGYMPESPPIYPEM 89
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 SVQSYLEFVAwikgiKMKDIPKRIDAVMEKTSITHVRD---RICG--------------R-LSKGYRQRVGLAQALIHNP 151
Cdd:TIGR00956 154 TVGETLDFAA-----RCKTPQNRPDGVSREEYAKHIADvymATYGlshtrntkvgndfvRgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 152 PVLILDEPTSGLDPKQIIEVRELIKGLAGE--HTVIVSthIL---PEVKLTCERVIIINNGWIVAQG 213
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTSANIldTTPLVA--IYqcsQDAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-207 |
2.22e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.79 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 16 VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDIL----EQSIDVR-RNIGYMPESPPIYPEMS 90
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeEARAKLRaKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 91 VQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIE 170
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 931518567 171 VRELIKGLAGEH--TVIVSTHIlPEVKLTCERVIIINNG 207
Cdd:PRK10584 185 IADLLFSLNREHgtTLILVTHD-LQLAARCDRRLRLVNG 222
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-220 |
2.83e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.96 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKT-TAMRIL----------TCFL------LPNEGTATVAGF-----D------ 64
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFgrsygrnisgTVFKdgkevdVSTVSDAIDAGLayvteDrkgygl 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 65 ILEQSIdvRRNIGympesppiypemsvqsylefVAWIKGIKMKDIpkrIDAVMEKTSITHVRDRI----------CGRLS 134
Cdd:NF040905 352 NLIDDI--KRNIT--------------------LANLGKVSRRGV---IDENEEIKVAEEYRKKMniktpsvfqkVGNLS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 135 KGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVISSELPELLGMCDRIYVMNEGRITGEL 486
|
....*..
gi 931518567 214 TPENLTQ 220
Cdd:NF040905 487 PREEASQ 493
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-207 |
3.26e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.90 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRNIGYM-----PESPPIYPEMSV--- 91
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAlvteeRRSTGIYAYLDIgfn 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 92 ------QSYLEFVAWIKGIKMK-DIPKRIDAVMEKTSITHVRdriCGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK10982 347 slisniRNYKNKVGLLDNSRMKsDTQWVIDSMRVKTPGHRTQ---IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 931518567 165 PKQIIEVRELIKGLA--GEHTVIVSTHiLPEVKLTCERVIIINNG 207
Cdd:PRK10982 424 VGAKFEIYQLIAELAkkDKGIIIISSE-MPELLGITDRILVMSNG 467
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-219 |
3.95e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 12 GGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRN--IGYMPESPPIY--- 86
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRlgVAYIPEDRLGRglv 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 87 PEMSV------QSY--LEFVAWIKgIKMKDIPKRIDAVMEKTSI-THVRDRICGRLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:COG3845 349 PDMSVaenlilGRYrrPPFSRGGF-LDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 158 EPTSGLDP-------KQIIEVREliKGLAgehTVIVSTHiLPEVKLTCERVIIINNGWIVAQGTPENLT 219
Cdd:COG3845 428 QPTRGLDVgaiefihQRLLELRD--AGAA---VLLISED-LDEILALSDRIAVMYEGRIVGEVPAAEAT 490
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-164 |
5.47e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTAtvagfdileqSIDVRRNIGYMP 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV----------SLDPNERLGKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVqsylefvawikgikmkdipkrIDAVM----EKTSITHVRDRI--------------------------- 129
Cdd:PRK15064 71 QDQFAFEEFTV---------------------LDTVImghtELWEVKQERDRIyalpemseedgmkvadlevkfaemdgy 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 130 -----CGRL------------------SKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK15064 130 taearAGELllgvgipeeqhyglmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-164 |
5.84e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFS----------ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQ--- 68
Cdd:PRK11308 6 LQAIDLKKHYPVKRGLFKperlvkaldgVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 69 ------------------SIDVRRNIGYMPESP-PIYPEMSVQSYLEfvawikgikmkdipkRIDAVMEKTSI-THVRDR 128
Cdd:PRK11308 86 aqkllrqkiqivfqnpygSLNPRKKVGQILEEPlLINTSLSAAERRE---------------KALAMMAKVGLrPEHYDR 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 931518567 129 ICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK11308 151 YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
51-218 |
6.54e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 51 LLPNEGTATVAGFDILEQSIDVRRNIGYMPESPPIYPEMSVQSYLEF---VAWIKGIKMKDIPKRIDAVMEktSITHVRD 127
Cdd:PTZ00265 1272 VFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFgkeDATREDVKRACKFAAIDEFIE--SLPNKYD 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 128 RICG----RLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP-------KQIIEVRElikglAGEHTVIVSTHILPEVKL 196
Cdd:PTZ00265 1350 TNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseklieKTIVDIKD-----KADKTIITIAHRIASIKR 1424
|
170 180
....*....|....*....|....*..
gi 931518567 197 TcERVIIINN-----GWIVAQGTPENL 218
Cdd:PTZ00265 1425 S-DKIVVFNNpdrtgSFVQAHGTHEEL 1450
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-164 |
6.98e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 3 SAKNISKKFGG-KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVA-GFdileqsidvrrNIGYMP 80
Cdd:PRK11819 8 TMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGI-----------KVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSV-QSYLEFVAWIKGI---------KMKDIPKRIDAVMEK-----TSITHV-------------------- 125
Cdd:PRK11819 77 QEPQLDPEKTVrENVEEGVAEVKAAldrfneiyaAYAEPDADFDALAAEqgelqEIIDAAdawdldsqleiamdalrcpp 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 931518567 126 RDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK11819 157 WDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
15-166 |
7.70e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 7.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 15 QVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPN--EGTATVAGFDILEQSIdvRRNIGYMPESPPIYPEMSVQ 92
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETF--ARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 93 SYLEFVAWI---KGIKMKDIPKRIDAVMEKTSITHVRDRICGR-----LSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PLN03140 972 ESLIYSAFLrlpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
..
gi 931518567 165 PK 166
Cdd:PLN03140 1052 AR 1053
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-221 |
9.89e-10 |
|
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: 59.57 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 16 VLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSI-DVRRNIGYMPESPPIYP---EMSV 91
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLhDLRFKITIIPQDPVLFSgslRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 92 Q---SYLEFVAWIkGIKMKDIPKRIDAVMEKTsithvrDRICGR----LSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:TIGR00957 1381 DpfsQYSDEEVWW-ALELAHLKTFVSALPDKL------DHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 165 PKQIIEVRELIKGLAGEHTVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENLTQK 221
Cdd:TIGR00957 1454 LETDNLIQSTIRTQFEDCTVLTIAHRLNTI-MDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
7-204 |
2.09e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.04 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 7 ISKKFGGKQVLFSISfDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATvagfdileqsidvrrnigyMPESPPIY 86
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE-------------------WDGITPVY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 87 PemsvqsylefvawikgikmkdiPKRIDavmektsithvrdricgrLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPK 166
Cdd:cd03222 66 K----------------------PQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 931518567 167 QIIEVRELIKGLA--GEHTVIVSTHILPEVKLTCERVIII 204
Cdd:cd03222 106 QRLNAARAIRRLSeeGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-178 |
4.03e-09 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 54.85 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILtCFLLPNeGTATVagfdileqSIDVRRNIGYMPESP--P------ 84
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPW-GSGRI--------GMPEGEDLLFLPQRPylPlgtlre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 85 --IYPemsvqsylefvaWikgikmkdipkridavmektsithvrDRIcgrLSKGYRQRVGLAQALIHNPPVLILDEPTSG 162
Cdd:cd03223 83 qlIYP------------W--------------------------DDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170
....*....|....*.
gi 931518567 163 LDPKQIIEVRELIKGL 178
Cdd:cd03223 122 LDEESEDRLYQLLKEL 137
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-207 |
5.34e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTatvagfdileqsIDVRRNIGYMPESPPIYPEMSVQSYLE 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT------------VDIKGSAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 97 FVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP-------KQII 169
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQtftkkclDKMN 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 931518567 170 EVRELIKglagehTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:PRK13545 188 EFKEQGK------TIFFISHSLSQVKSFCTKALWLHYG 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-207 |
5.91e-09 |
|
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: 57.23 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdileqsidvrrNIGYMPESPPIYPEMSVQ 92
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 93 ------SYLEF--VAWIKGIKMKD----IPKRIDAVMEKTSIThvrdricgrLSKGYRQRVGLAQALIHNPPVLILDEPT 160
Cdd:TIGR01271 506 niifglSYDEYryTSVIKACQLEEdialFPEKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 931518567 161 SGLD---PKQIIEvRELIKGLAGEhTVIVSTHILPEVKlTCERVIIINNG 207
Cdd:TIGR01271 577 THLDvvtEKEIFE-SCLCKLMSNK-TRILVTSKLEHLK-KADKILLLHEG 623
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
132-218 |
8.46e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.40 E-value: 8.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 132 RLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHT--VIVSTHILPEVKLTCERVIIINNGWI 209
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGEA 247
|
....*....
gi 931518567 210 VAQGTPENL 218
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-218 |
1.18e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 56.28 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVagfdileqsidVRRNIGYMPEsppiypemsvqs 93
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQ------------ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 94 ylefVAWIKGIKMKD--------IPKRIDAVMEKTSITHVRDRICGR-----------LSKGYRQRVGLAQALIHNPPVL 154
Cdd:PLN03130 687 ----VSWIFNATVRDnilfgspfDPERYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 155 ILDEPTSGLDP---KQIIEvrELIKG-LAGEHTVIVST--HILPEVkltcERVIIINNGWIVAQGTPENL 218
Cdd:PLN03130 763 IFDDPLSALDAhvgRQVFD--KCIKDeLRGKTRVLVTNqlHFLSQV----DRIILVHEGMIKEEGTYEEL 826
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
1.30e-08 |
|
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: 56.11 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTAMriltcfllpnegTATVAGFDILEQSIDVRRNIGYMPESppiypemsvqsyle 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLL------------SALLAEMDKVEGHVHMKGSVAYVPQQ-------------- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 97 fvAWIKGIKMKD--------IPKRIDAVMEKTSITHVRDRICG-----------RLSKGYRQRVGLAQALIHNPPVLILD 157
Cdd:TIGR00957 708 --AWIQNDSLREnilfgkalNEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 158 EPTSGLDP---KQIIEVRELIKGLAGEHTVIVSTH---ILPEVKLtcerVIIINNGWIVAQGTPENLTQK 221
Cdd:TIGR00957 786 DPLSAVDAhvgKHIFEHVIGPEGVLKNKTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQELLQR 851
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-213 |
1.80e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfdileQSID---------VRRNIGYMPESP--PIYPE 88
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNG-----QRIDtlspgklqaLRRDIQFIFQDPyaSLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 89 MSV-QSYLEFVAWIKGIKMKDIPKRIDAVMEKTSI--THVRdRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDP 165
Cdd:PRK10261 418 QTVgDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 166 K---QIIEV-----RELikGLAgehtVIVSTHILPEVKLTCERVIIINNGWIVAQG 213
Cdd:PRK10261 497 SirgQIINLlldlqRDF--GIA----YLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-258 |
7.55e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDI--------LEQSIDVRRNI 76
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskeaLENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 GYMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKridAVMEKTSI-THVRDRIcGRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTK---AIFDELDIdIDPRAKV-ATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 156 LDEPTSGLDPKQIIEVRELIKGLAGEHTVIVS-THILPEVKLTCERVIIINNG-WIVAQGTPENLTQKIKG-------KE 226
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYiSHKMEEIFQLCDEITILRDGqWIATQPLAGLTMDKIIAmmvgrslTQ 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 931518567 227 RLQLEIGGPGE---EVKN--ALRNvPGVANVQIEIHE 258
Cdd:PRK10982 238 RFPDKENKPGEvilEVRNltSLRQ-PSIRDVSFDLHK 273
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
132-195 |
9.51e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 9.51e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 132 RLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHT--VIVSTHILPEVK 195
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENriTIIIAHRLSTIR 644
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
132-189 |
9.89e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 9.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 931518567 132 RLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTH 189
Cdd:COG4178 485 VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-189 |
1.10e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 4 AKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTA------TVAGFDILEQSIDvrrnig 77
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklEVAYFDQHRAELD------ 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 78 ympesppiyPEMSVqsyLEFVA------WIKGIK------MKDI---PKRidavmektSITHVRdricgRLSKGYRQRVG 142
Cdd:PRK11147 396 ---------PEKTV---MDNLAegkqevMVNGRPrhvlgyLQDFlfhPKR--------AMTPVK-----ALSGGERNRLL 450
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 931518567 143 LAQALIHNPPVLILDEPTSGLDpkqiIEVRELIKGLAGEH--TVIVSTH 189
Cdd:PRK11147 451 LARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYqgTVLLVSH 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-195 |
1.21e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLpneGTATVAGFDILEQSIDVRRNIgymPESppIYPEMSVQS 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGCVDVPDNQFGREASL---IDA--IGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 94 YLEFVAwIKGIKmkdipkriDAVMEKTSITHvrdricgrLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRE 173
Cdd:COG2401 115 AVELLN-AVGLS--------DAVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177
|
170 180
....*....|....*....|....
gi 931518567 174 LIKGLAGEH--TVIVSTHIlPEVK 195
Cdd:COG2401 178 NLQKLARRAgiTLVVATHH-YDVI 200
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-214 |
1.35e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.71 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLF---------SISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAG-------FD 64
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFrrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 65 ILEQSIdvrRNIgYMPESPPIYPEMSVQSYLEFVAWIK-GIKMKDIPKRIDAVMEKTSIthVRDRIC---GRLSKGYRQR 140
Cdd:PRK15112 84 YRSQRI---RMI-FQDPSTSLNPRQRISQILDFPLRLNtDLEPEQREKQIIETLRQVGL--LPDHASyypHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931518567 141 VGLAQALIHNPPVLILDEPTSGLD---PKQIIEVRELIKGLAGEHTVIVSTHiLPEVKLTCERVIIINNGWIVAQGT 214
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDmsmRSQLINLMLELQEKQGISYIYVTQH-LGMMKHISDQVLVMHQGEVVERGS 233
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
13-165 |
1.44e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 13 GKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATvagfdileqsIDVRRNIGYMPESP--------- 83
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLT----------KPAKGKLFYVPQRPymtlgtlrd 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 84 -PIYPeMSVQSYLEfvawiKGIKMKDIPKRIDAVmektSITHVRDRICG---------RLSKGYRQRVGLAQALIHNPPV 153
Cdd:TIGR00954 534 qIIYP-DSSEDMKR-----RGLSDKDLEQILDNV----QLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQF 603
|
170
....*....|..
gi 931518567 154 LILDEPTSGLDP 165
Cdd:TIGR00954 604 AILDECTSAVSV 615
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-188 |
1.71e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLlpNEGTAT----VAGFDILEQSIdvRRNIGYMPESPPIYPEM 89
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITggdrLVNGRPLDSSF--QRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 90 SVQSYLEFVAWIKgiKMKDIPKR-----IDAVMEKTSITHVRDRICGRLSKGY----RQRVGLAQALIHNPPVLI-LDEP 159
Cdd:TIGR00956 852 TVRESLRFSAYLR--QPKSVSKSekmeyVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180
....*....|....*....|....*....
gi 931518567 160 TSGLDPKQIIEVRELIKGLAGEHTVIVST 188
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQAILCT 958
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-213 |
3.08e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.56 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTamriLTCFLLPNE------GTATVAGFDILEQSIDVRR 74
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKST----LSATLAGREdyevtgGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 75 NIG------YMPESPPIYPEMSVQSYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGR-----LSKGYRQRVGL 143
Cdd:PRK09580 77 GEGifmafqYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRsvnvgFSGGEKKRNDI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLA-GEHTVIVSTH---ILPEVKltCERVIIINNGWIVAQG 213
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqrILDYIK--PDYVHVLYQGRIVKSG 228
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-181 |
3.13e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRI------------LTCFllpneGTATVAGfdilEQS 69
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLF-----GRRRGSG----ETI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 70 IDVRRNIGYMPESppIYPEMSVQSYLEFV---AWIKGIKM-KDIPKRIDA-VMEKTSITHVRDRICG----RLSKGyRQR 140
Cdd:PRK10938 332 WDIKKHIGYVSSS--LHLDYRVSTSVRNVilsGFFDSIGIyQAVSDRQQKlAQQWLDILGIDKRTADapfhSLSWG-QQR 408
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 931518567 141 VGL-AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGE 181
Cdd:PRK10938 409 LALiVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISE 450
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
127-189 |
3.52e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 3.52e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 127 DRICGRLSKGYRQRVGLAQALIHNPP--VLILDEPTSGLDPKQIIEVRELIKGLAGE-HTVIVSTH 189
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLgNTVILIEH 147
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-218 |
4.77e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFS----ISFDVNKGEILGFLGPNAAGKT-TAMRILTCFLLPNEGTATVAGF---DILEQSIDV 72
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRavdrISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRVMAEKLEFngqDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 73 RRNI----------GYMPESPPIYpEMSVQsYLEFVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRI---CGRLSKGYRQ 139
Cdd:PRK11022 83 RRNLvgaevamifqDPMTSLNPCY-TVGFQ-IMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 140 RVGLAQALIHNPPVLILDEPTSGLD---PKQIIEVreLIKGLAGEH-TVIVSTHILPEVKLTCERVIIINNGWIVAQGTP 215
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDvtiQAQIIEL--LLELQQKENmALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
...
gi 931518567 216 ENL 218
Cdd:PRK11022 239 HDI 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-168 |
5.44e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 4 AKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAgfdilEQSidvrrNIGYMPESp 83
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-----ENA-----NIGYYAQD- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 84 piypemsvqSYLEF------VAWIKGIKmkdipkridavMEKTSITHVRDrICGRL--------------SKGYRQRVGL 143
Cdd:PRK15064 391 ---------HAYDFendltlFDWMSQWR-----------QEGDDEQAVRG-TLGRLlfsqddikksvkvlSGGEKGRMLF 449
|
170 180
....*....|....*....|....*
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQI 168
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESI 474
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-218 |
7.69e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.78 E-value: 7.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQAL---IHNPPVLILDEPTSGL---DPKQIIEVrelIKGLAGE-HTVIVSTHILPEVKlTCERVIII- 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDIKKLLEV---LQRLVDKgNTVVVIEHNLDVIK-TADYIIDLg 905
|
90
....*....|....*....
gi 931518567 205 -----NNGWIVAQGTPENL 218
Cdd:TIGR00630 906 peggdGGGTVVASGTPEEV 924
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-186 |
8.43e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 21 SFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEG-------TATVAGFDILEQSID---VRRNIGYMPESPPIYPEMS 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqfsHITRLSFEQLQKLVSdewQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 91 VQSYLEFVawikgikmKDiPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIE 170
Cdd:PRK10938 103 AEIIQDEV--------KD-PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|....*.
gi 931518567 171 VRELIKGLAGEHTVIV 186
Cdd:PRK10938 174 LAELLASLHQSGITLV 189
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-164 |
1.67e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTAtvagfdILEQSIDVRRnigyMP 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI------IYEQDLIVAR----LQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 81 ESPPIYPEMSVQSYL-EFVAWIKGI-----------------KMKDIPKRIDAVMEKTSITHVRDRI---CGR------- 132
Cdd:PRK11147 73 QDPPRNVEGTVYDFVaEGIEEQAEYlkryhdishlvetdpseKNLNELAKLQEQLDHHNLWQLENRInevLAQlgldpda 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 931518567 133 ----LSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:PRK11147 153 alssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-216 |
2.33e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 1 MISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFllP----NEGTATVAGFDILEQSIDVRRNI 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 77 G-YMPESPPI-YPEMSVQSYLEFVAWIKGIKMKDipKRIDA------VMEKTSITHVRDRICGR-----LSKGYRQRVGL 143
Cdd:CHL00131 85 GiFLAFQYPIeIPGVSNADFLRLAYNSKRKFQGL--PELDPlefleiINEKLKLVGMDPSFLSRnvnegFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 144 AQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAG-EHTVIVSTH-------ILPEVkltcerVIIINNGWIVAQGTP 215
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqrlldyIKPDY------VHVMQNGKIIKTGDA 236
|
.
gi 931518567 216 E 216
Cdd:CHL00131 237 E 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-220 |
3.58e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.17 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGtatvagfDILEQSI--------DVRRNIGYMPESPPI 85
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG-------DIRFHDIpltklqldSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 86 Y------------PEMSvQSYLEFVAWIKGIKmKDI---PKRIDavmektsiTHVRDRicG-RLSKGYRQRVGLAQALIH 149
Cdd:PRK10789 401 FsdtvannialgrPDAT-QQEIEHVARLASVH-DDIlrlPQGYD--------TEVGER--GvMLSGGQKQRISIARALLL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 150 NPPVLILDEPTSGLDPKQiieVRELIKGLA--GEH-TVIVSTHILPEVKLTCErVIIINNGWIVAQGTPENLTQ 220
Cdd:PRK10789 469 NAEILILDDALSAVDGRT---EHQILHNLRqwGEGrTVIISAHRLSALTEASE-ILVMQHGHIAQRGNHDQLAQ 538
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
93-204 |
4.80e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.81 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 93 SYLEFVAWIKGIKMKDIPKRIDAVM--EKTSITHVRDRICGRLSKGYRQRVGLAQALIH---NP-PVLILDEPTSGLDPK 166
Cdd:cd03227 36 TILDAIGLALGGAQSATRRRSGVKAgcIVAAVSAELIFTRLQLSGGEKELSALALILALaslKPrPLYILDEIDRGLDPR 115
|
90 100 110
....*....|....*....|....*....|....*....
gi 931518567 167 QIIEVRELIKGLAGEH-TVIVSTHiLPEVKLTCERVIII 204
Cdd:cd03227 116 DGQALAEAILEHLVKGaQVIVITH-LPELAELADKLIHI 153
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-221 |
4.95e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQALIH---NPPVLILDEPTSGL---DPKQIIEVRELIKGLAgeHTVIVSTHILPEVKlTCERVIIIN- 205
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQG--HTVVIIEHNMHVVK-VADYVLELGp 886
|
90 100
....*....|....*....|.
gi 931518567 206 -----NGWIVAQGTPENLTQK 221
Cdd:PRK00635 887 eggnlGGYLLASCSPEELIHL 907
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
133-215 |
7.79e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQALIH---NPPVLILDEPTSGL---DPKQIIEVreLIKGLAGEHTVIVSTHILPEVKlTCERVIII-- 204
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLhfhDVKKLLEV--LQRLVDKGNTVVVIEHNLDVIK-CADWIIDLgp 246
|
90
....*....|....*
gi 931518567 205 ----NNGWIVAQGTP 215
Cdd:cd03271 247 eggdGGGQVVASGTP 261
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
133-220 |
7.96e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.23 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHT--VIVSTHILPEVKLTCERVIIINNGWIV 210
Cdd:PRK10418 141 MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
90
....*....|
gi 931518567 211 AQGTPENLTQ 220
Cdd:PRK10418 221 EQGDVETLFN 230
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
133-220 |
1.03e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 46.94 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQAL--IHNPPVL-ILDEPTSGL---DPKQIIEV-RELI-KGlageHTVIVSTHILpEVKLTCERVIII 204
Cdd:COG0178 827 LSGGEAQRVKLASELskRSTGKTLyILDEPTTGLhfhDIRKLLEVlHRLVdKG----NTVVVIEHNL-DVIKTADWIIDL 901
|
90 100
....*....|....*....|..
gi 931518567 205 ------NNGWIVAQGTPENLTQ 220
Cdd:COG0178 902 gpeggdGGGEIVAEGTPEEVAK 923
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-237 |
1.13e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 16 VLFSISFDVNKGEILGFLGPNAAGKTTA----MRIL-TCfllpnEGTATVAGFDILEQSI-DVRRNIGYMPESPPIYP-- 87
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLlltfMRMVeVC-----GGEIRVNGREIGAYGLrELRRQFSMIPQDPVLFDgt 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 88 -EMSVQSYLEFVA---WiKGIKMKDIPKR-------IDA-VMEKTSithvrdricgRLSKGYRQRVGLAQALIHNPPVLI 155
Cdd:PTZ00243 1400 vRQNVDPFLEASSaevW-AALELVGLRERvasesegIDSrVLEGGS----------NYSVGQRQLMCMARALLKKGSGFI 1468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 156 L-DEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVKlTCERVIIINNGWIVAQGTPENLTQKIKGKERLQLEIGG 234
Cdd:PTZ00243 1469 LmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVA-QYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEALG 1547
|
...
gi 931518567 235 PGE 237
Cdd:PTZ00243 1548 RSE 1550
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
134-189 |
1.75e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 931518567 134 SKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGehTVIVSTH 189
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG--TLILISH 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
131-189 |
3.06e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 3.06e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931518567 131 GRLSKGYRQ------RVGLAQALIHNPPVLILDEPTSGLDP----KQIIEVRELIKGLAGEHtVIVSTH 189
Cdd:cd03240 114 GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenieESLAEIIEERKSQKNFQ-LIVITH 181
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
103-189 |
3.12e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.07 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 103 GIKMKDIPKRIDAVMEKTSITHVRDRICGR----LSKGYRQRVGLAQALI---HNPPVLILDEPTSGLDPKQIIEVRELI 175
Cdd:pfam13304 203 GEGIEKSLLVDDRLRERGLILLENGGGGELpafeLSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELL 282
|
90
....*....|....*
gi 931518567 176 KGLAGEHT-VIVSTH 189
Cdd:pfam13304 283 KELSRNGAqLILTTH 297
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-218 |
4.16e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 44.13 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 14 KQVLFSISFDVNKGEILGFLGPNAAGKTTA----MRILTCFllpnEGTATVAGFDILEQSID-VRRNIGYMPESPPIY-- 86
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLHtLRSRLSIILQDPILFsg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 87 -------PEM-----SVQSYLEfVAWIKGIkMKDIPKRIDAVMEKTSithvrdricGRLSKGYRQRVGLAQALIHNPPVL 154
Cdd:cd03288 110 sirfnldPECkctddRLWEALE-IAQLKNM-VKSLPGGLDAVVTEGG---------ENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931518567 155 ILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVkLTCERVIIINNGWIVAQGTPENL 218
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENL 241
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
142-189 |
4.61e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 44.54 E-value: 4.61e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 931518567 142 GLAQALIHN--PPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTH 189
Cdd:COG4637 268 ALLAALLSPrpPPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTH 317
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
132-250 |
7.23e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 44.32 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 132 RLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEHTVIVSTHILPEVkLTCERVIIINNGWIVA 211
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI-VEADTILVLHRGQAVE 554
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 931518567 212 QGTPENLTQKiKGK----ERLQLeiggPGEEVKNALRNVPGVA 250
Cdd:PRK10790 555 QGTHQQLLAA-QGRywqmYQLQL----AGEELAASVREEESLS 592
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-189 |
1.16e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 26 KGEILGFLGPNAAGKTTAMRILTCFLLPNEGTA-TVAGFDILEQSIDVRRNIGYMPESPPIYPEMsvqsylefvawikgi 104
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLIIVGGKKASGSGEL--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 105 kmkdipkridavmektsithvrdricgrlskgyRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH-- 182
Cdd:smart00382 66 ---------------------------------RLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLlk 112
|
170
....*....|..
gi 931518567 183 -----TVIVSTH 189
Cdd:smart00382 113 seknlTVILTTN 124
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-47 |
1.33e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 931518567 5 KNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRIL 47
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVL 47
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
133-216 |
2.10e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQALiHNPP----VLILDEPTSGL---DPKQIIEV-RELI-KGlageHTVIVSTHILPEVKlTCERVII 203
Cdd:PRK00349 831 LSGGEAQRVKLAKEL-SKRStgktLYILDEPTTGLhfeDIRKLLEVlHRLVdKG----NTVVVIEHNLDVIK-TADWIID 904
|
90
....*....|....*....
gi 931518567 204 I------NNGWIVAQGTPE 216
Cdd:PRK00349 905 LgpeggdGGGEIVATGTPE 923
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-165 |
2.95e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 20 ISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGFDILEQSIDVRRN---------------IGymPESPP 84
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKlfsavftdfhlfdqlLG--PEGKP 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 85 IYPEMsVQSYLEFvawikgIKMKDipkridavmektSITHVRDRICG-RLSKGYRQRVGLAQALIHNPPVLILDEPTSGL 163
Cdd:PRK10522 420 ANPAL-VEKWLER------LKMAH------------KLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
..
gi 931518567 164 DP 165
Cdd:PRK10522 481 DP 482
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
127-221 |
3.17e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 127 DRICGRLSKGYRQRVGLAQ----ALIHnppVL-ILDEPTSGLDPKqiiEVRELIKGLAG----EHTVIVSTHIlPEVKLT 197
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATqigsGLTG---VLyVLDEPSIGLHQR---DNRRLINTLKRlrdlGNTLIVVEHD-EDTIRA 555
|
90 100 110
....*....|....*....|....*....|
gi 931518567 198 CERVIII------NNGWIVAQGTPENLTQK 221
Cdd:TIGR00630 556 ADYVIDIgpgageHGGEVVASGTPEEILAN 585
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-189 |
4.65e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 2 ISAKNISKKFGGKQVLFSISFDVNKGEILGFLGPNAAGKTTAMRILT----------CFLLPNE----GTATVAGFDILE 67
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipknCQILHVEqevvGDDTTALQCVLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 68 QSIDVRRnigYMPESPPIYPEmsvQSYLEFVAWIKGIKMK---------------DIPKR---IDA---------VMEKT 120
Cdd:PLN03073 258 TDIERTQ---LLEEEAQLVAQ---QRELEFETETGKGKGAnkdgvdkdavsqrleEIYKRlelIDAytaearaasILAGL 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 121 SIT-HVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIkgLAGEHTVIVSTH 189
Cdd:PLN03073 332 SFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-207 |
7.70e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 17 LFSISFDVNKGEILGFLGPNAAGKTTAMRILTCFLLPNEGTATVAGfDILEQSIDVRRNigympesppiyPEMSVQSYLE 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISAGLS-----------GQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 97 FVAWIKGIKMKDIPKRIDAVMEKTSITHVRDRICGRLSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPK-------QII 169
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfaqkcldKIY 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 931518567 170 EVRELIKglagehTVIVSTHILPEVKLTCERVIIINNG 207
Cdd:PRK13546 188 EFKEQNK------TIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
127-213 |
7.77e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 127 DRICGRLSKGYRQRVGLAQALIHN-PPVL-ILDEPTSGLDPKQIIEVRELIKGL--AGeHTVIVSTHIlPEVKLTCERVI 202
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLrdLG-NTVLVVEHD-EDTIRAADHVI 209
|
90
....*....|....*..
gi 931518567 203 II------NNGWIVAQG 213
Cdd:cd03270 210 DIgpgagvHGGEIVAQG 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
133-218 |
3.21e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 38.63 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931518567 133 LSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPKQIIEVRELIKGLAGEH--TVIVSTHILPEVKLTCERVIIINNGWIV 210
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWADKINVLYCGQTV 238
|
....*...
gi 931518567 211 AQGTPENL 218
Cdd:PRK15093 239 ETAPSKEL 246
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
133-164 |
4.12e-03 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 38.08 E-value: 4.12e-03
10 20 30
....*....|....*....|....*....|..
gi 931518567 133 LSKGYRQRVGLAQALIHNPPVLILDEPTSGLD 164
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
133-168 |
4.80e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.35 E-value: 4.80e-03
10 20 30
....*....|....*....|....*....|....*....
gi 931518567 133 LSKGYRQRVGLAQALIHNPPVLILDEPTSGLDPK---QI 168
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTtqaQI 197
|
|
| |
