|
Name |
Accession |
Description |
Interval |
E-value |
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-314 |
8.32e-180 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 500.00 E-value: 8.32e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 4 AIEVNQLRKEFKAYSSRSGLKGAFRDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT 83
Cdd:COG4586 1 IIEVENLSKTYRVYEKEPGLKGALKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 84 VNGMNPHKEREKFAQTIGVVFGQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQR 163
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVFGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 164 MRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQ 243
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 244 KLRSNWGDLKQVTFEFGTAPNKEQLKLLtqgmpVNWIEGDQKYLWtaqLQ-NKGDLMSQLIAKVVAKHEIND 314
Cdd:COG4586 241 ELKERFGPYKTIVLELAEPVPPLELPRG-----GEVIEREGNRVR---LEvDPRESLAEVLARLLARYPVRD 304
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-240 |
1.84e-126 |
|
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: 361.65 E-value: 1.84e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKAYSSRSGLKGAFRDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:cd03267 1 IEVSNLSKSYRVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NGMNPHKEREKFAQTIGVVFGQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRM 164
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 165 RCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-247 |
8.51e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 255.76 E-value: 8.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFkayssrsglkGAFrdlftrnyrvmKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:COG1131 1 IEVRGLTKRY----------GDK-----------TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NGMNPHKEREKFAQTIGVVFgQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRM 164
Cdd:COG1131 60 LGEDVARDPAEVRRRIGYVP-QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 165 RCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQK 244
Cdd:COG1131 139 RLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
...
gi 504274718 245 LRS 247
Cdd:COG1131 218 LKA 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
32-251 |
2.60e-68 |
|
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: 213.95 E-value: 2.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSqLW 111
Cdd:COG4555 8 SKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDERG-LY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:COG4555 87 DRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 192 VKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGD 251
Cdd:COG4555 167 ARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
32-236 |
1.13e-62 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 196.85 E-value: 1.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFgQRSQLW 111
Cdd:cd03230 7 SKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP-EEPSLY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESFrllkkvykvsdedynahmehviqtldigplldkpvrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:cd03230 86 ENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504274718 192 VKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:cd03230 130 SRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
40-246 |
2.23e-60 |
|
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: 192.72 E-value: 2.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFgQRSQLWWDIAVQES 119
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCP-QFDALFDELTVREH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQF 199
Cdd:cd03263 96 LRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504274718 200 LKEinEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLR 246
Cdd:cd03263 176 ILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-246 |
3.38e-59 |
|
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: 189.89 E-value: 3.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSqLW 111
Cdd:cd03265 7 VKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLS-VD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:cd03265 86 DELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 192 VKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLR 246
Cdd:cd03265 166 TRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
31-240 |
7.79e-57 |
|
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: 183.72 E-value: 7.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSqL 110
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTG-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:cd03266 90 YDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 191 LVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03266 170 MATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
39-251 |
5.63e-56 |
|
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: 184.13 E-value: 5.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSqLWWDIAVQE 118
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYAS-VDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQ 198
Cdd:TIGR01188 86 NLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504274718 199 FLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGD 251
Cdd:TIGR01188 166 YIRALKEE-GVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGK 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
39-254 |
3.20e-53 |
|
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: 174.83 E-value: 3.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKE-REKFAQTIGVVFgQ--RSQL----- 110
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKVGLVF-QnpDDQLfaptv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAvqesFRLLKkvYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:COG1122 94 EEDVA----FGPEN--LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 191 LVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQ 254
Cdd:COG1122 168 RGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-248 |
2.23e-52 |
|
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: 180.48 E-value: 2.23e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKayssrsglkgafrdlfTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:COG1123 261 LEVRNLSKRYP----------------VRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NGMN----PHKEREKFAQTIGVVFgQ--RSQL--WWDIA--VQESFRLLKKVykvSDEDYNAHMEHVIQTLDIGP-LLDK 153
Cdd:COG1123 325 DGKDltklSRRSLRELRRRVQMVF-QdpYSSLnpRMTVGdiIAEPLRLHGLL---SRAERRERVAELLERVGLPPdLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 154 PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDE 233
Cdd:COG1123 401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD 480
|
250
....*....|....*
gi 504274718 234 GSIIYDGSLQKLRSN 248
Cdd:COG1123 481 GRIVEDGPTEEVFAN 495
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-234 |
2.10e-49 |
|
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: 164.18 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKER-EKFAQTIGVVF 104
Cdd:cd03225 2 LKNLsFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSlKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 gQ--RSQL-----WWDIAvqesFRLLKkvYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPP 177
Cdd:cd03225 82 -QnpDDQFfgptvEEEVA----FGLEN--LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 178 LLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
32-246 |
4.97e-49 |
|
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: 166.10 E-value: 4.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVfGQRSQLW 111
Cdd:TIGR03522 9 TKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYL-PEHNPLY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:TIGR03522 88 LDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEPTTGLDPN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 192 VKLKIRQFLKEINEkyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLR 246
Cdd:TIGR03522 168 QLVEIRNVIKNIGK--DKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELS 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
39-269 |
5.95e-49 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 165.67 E-value: 5.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmnpHKEREKFAQTIG----------------- 101
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRRIGylpeerglypkmkvgeq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 102 -VVFGQRSQLWWDIAVQESFRLLKKvykvsdedynahmehviqtLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:COG4152 92 lVYLARLKGLSKAEAKRRADEWLER-------------------LGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 181 LDEPTIGLD-VLVKLkIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSnwgDLKQVTFEF 259
Cdd:COG4152 153 LDEPFSGLDpVNVEL-LKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR---QFGRNTLRL 227
|
250
....*....|
gi 504274718 260 GTAPNKEQLK 269
Cdd:COG4152 228 EADGDAGWLR 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
32-240 |
7.29e-49 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 162.77 E-value: 7.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQtIGV------VFG 105
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGAlieapgFYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSqlwwdiaVQESFRLLKKVYKVSDEDYNahmehviQTLDIGPLL---DKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:cd03268 86 NLT-------ARENLRLLARLLGIRKKRID-------EVLDVVGLKdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 183 EPTIGLDVLVKLKIRQFLKEINeKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
41-241 |
9.45e-49 |
|
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: 164.06 E-value: 9.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKERekfAQTIGVVFgQRSQLWWDIAV 116
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlaslSRREL---ARRIAYVP-QEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRL-----LKKVYKVSDEDYNAhMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:COG1120 93 RELVALgryphLGLFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 192 VKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-236 |
2.64e-47 |
|
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: 159.19 E-value: 2.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKAYSSRSglkgafrdlftrnyrvmKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:cd03255 1 IELKNLSKTYGGGGEKV-----------------QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NGMNPHK----EREKF-AQTIGVVFgQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLS 159
Cdd:cd03255 64 DGTDISKlsekELAAFrRRHIGFVF-QSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 160 LGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLaDIEALCERVVMLDEGSI 236
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
31-247 |
4.02e-47 |
|
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: 159.58 E-value: 4.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFAQTIGVVFgQ--- 106
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvTRRRRKAFRRRVQMVF-Qdpy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 107 -----RSQLWWDIAvqESFRLLKKvykvsdEDYNAHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:COG1124 90 aslhpRHTVDRILA--EPLRIHGL------PDREERIAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALILEPELLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 181 LDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRS 247
Cdd:COG1124 162 LDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
27-240 |
1.04e-46 |
|
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: 157.67 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL---FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREKFAQT 99
Cdd:cd03257 4 VKNLsvsFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklSRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 100 IGVVFgQ------------RSQLWwdiavqESFRLLKKVYKVSDEDynahmEHVIQTLDIGPL----LDKPVRKLSLGQR 163
Cdd:cd03257 84 IQMVF-QdpmsslnprmtiGEQIA------EPLRIHGKLSKKEARK-----EAVLLLLVGVGLpeevLNRYPHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 164 MRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
32-240 |
4.71e-46 |
|
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: 155.43 E-value: 4.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGeMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVV---FGQRS 108
Cdd:cd03264 7 TKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLpqeFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 QlwwdIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:cd03264 86 N----FTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 189 DVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03264 162 DPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
39-248 |
1.20e-45 |
|
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: 155.97 E-value: 1.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHK-EREKFAQT------------- 99
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditgLPPHRiARLGIARTfqnprlfpeltvl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 100 ----IGVVFGQRSQLWWDIavqesFRLLKkvYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHN 175
Cdd:COG0411 98 envlVAAHARLGRGLLAAL-----LRLPR--ARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504274718 176 PPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:COG0411 171 PKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRAD 243
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
40-241 |
1.33e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.63 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKfaqtIGVVfGQRSQLWWD--IAVQ 117
Cdd:COG1121 21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR----IGYV-PQRAEVDWDfpITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 E-----------SFRLLKKVYKvsdedynAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:COG1121 96 DvvlmgrygrrgLFRRPSRADR-------EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 187 GLDVLVKLKIRQFLKEINeKYNTTILLTTHDLADIEALCERVVMLDEGsIIYDGS 241
Cdd:COG1121 169 GVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGP 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-240 |
7.02e-45 |
|
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: 152.43 E-value: 7.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmnpHKEREKFAQTIGVVFGQRSqL 110
Cdd:cd03269 6 VTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNRIGYLPEERG-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:cd03269 82 YPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 191 LVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03269 162 VNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-241 |
2.56e-44 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 152.16 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKAYSSRSG-LKGAFRDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTS 79
Cdd:COG1134 1 MSSMIEVENVSKSYRLYHEPSRsLKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 80 GDITVN-----------GMNPhkerekfaqtigvvfgqrsqlwwDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIG 148
Cdd:COG1134 81 GRVEVNgrvsallelgaGFHP-----------------------ELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 149 PLLDKPVRKLSLGQRMRceLA-AALIH-NPPLLFLDEptiGL---DVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEA 223
Cdd:COG1134 138 DFIDQPVKTYSSGMRAR--LAfAVATAvDPDILLVDE---VLavgDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRR 211
|
250
....*....|....*...
gi 504274718 224 LCERVVMLDEGSIIYDGS 241
Cdd:COG1134 212 LCDRAIWLEKGRLVMDGD 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
41-240 |
6.64e-44 |
|
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: 149.12 E-value: 6.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKERekfAQTIGVVfgqrSQlwwdiav 116
Cdd:cd03214 15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslSPKEL---ARKIAYV----PQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 qesfrllkkvykvsdedynahmehVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:cd03214 81 ------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
39-248 |
2.33e-43 |
|
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: 149.51 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT-----VNGMNPHkerEKFAQTIGVVFgQRSQLWWD 113
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdgedITGLPPH---EIARLGIGRTF-QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQE----------SFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:cd03219 90 LTVLEnvmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 184 PTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
39-240 |
8.72e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.51 E-value: 8.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREKFAQTIGVVFgqrsqlwwdi 114
Cdd:COG2884 16 EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlKRREIPYLRRRIGVVF---------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 avQEsFRLL--KKVYK----------VSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:COG2884 86 --QD-FRLLpdRTVYEnvalplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 183 EPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-246 |
1.58e-42 |
|
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: 147.43 E-value: 1.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFkayssrsglkGAFrdlftrnyrvmKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG1127 2 SEPMIEVRNLTKSF----------GDR-----------VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNGMN----PHKEREKFAQTIGVVFgQRSQLWWDIAVQE--SFRLLKKvYKVSDEDYNAHMEHVIQTLDIGPLLDKP 154
Cdd:COG1127 61 EILVDGQDitglSEKELYELRRRIGMLF-QGGALFDSLTVFEnvAFPLREH-TDLSEAEIRELVLEKLELVGLPGAADKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 155 VRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:COG1127 139 PSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250
....*....|..
gi 504274718 235 SIIYDGSLQKLR 246
Cdd:COG1127 219 KIIAEGTPEELL 230
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
39-234 |
3.04e-42 |
|
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: 144.64 E-value: 3.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN---PHKEREKFAQTIGVVFgQRSQLWwdia 115
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDltdLEDELPPLRRRIGMVF-QDFALF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 116 vqesfrllkkvykvsdedynAHMEhVIQTLDIGplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:cd03229 89 --------------------PHLT-VLENIALG---------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 504274718 196 IRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:cd03229 139 VRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
31-240 |
1.88e-41 |
|
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: 143.81 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKERekfaqtIGVVFG 105
Cdd:cd03259 6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgVPPERRN------IGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSqLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd03259 80 DYA-LFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-239 |
2.99e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 143.65 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKayssrsglkgafrdlfTRNYRVmKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG1136 1 MSPLLELRNLTKSYG----------------TGEGEV-TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNGMN----PHKEREKF-AQTIGVVFgQRSQLwwdIA---VQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLD 152
Cdd:COG1136 64 EVLIDGQDisslSERELARLrRRHIGFVF-QFFNL---LPeltALENVALPLLLAGVSRKERRERARELLERVGLGDRLD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 153 KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD------VLvklkirQFLKEINEKYNTTILLTTHDLaDIEALCE 226
Cdd:COG1136 140 HRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeeVL------ELLRELNRELGTTIVMVTHDP-ELAARAD 212
|
250
....*....|...
gi 504274718 227 RVVMLDEGSIIYD 239
Cdd:COG1136 213 RVIRLRDGRIVSD 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-255 |
7.10e-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: 149.67 E-value: 7.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKAyssrsglkgafrdlftrnyRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPT-- 78
Cdd:COG1123 1 MTPLLEVRDLSVRYPG-------------------GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgr 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 79 -SGDITVNGMNPHKEREKF-AQTIGVVFGQ-RSQL-----WWDIAvqESFRLLKkvykVSDEDYNAHMEHVIQTLDIGPL 150
Cdd:COG1123 62 iSGEVLLDGRDLLELSEALrGRRIGMVFQDpMTQLnpvtvGDQIA--EALENLG----LSRAEARARVLELLEAVGLERR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 151 LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVM 230
Cdd:COG1123 136 LDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVV 215
|
250 260
....*....|....*....|....*
gi 504274718 231 LDEGSIIYDGSLQKLRSNWGDLKQV 255
Cdd:COG1123 216 MDDGRIVEDGPPEEILAAPQALAAV 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
35-240 |
3.02e-40 |
|
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: 140.36 E-value: 3.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKfaqtIGVVfGQRSQLWWD- 113
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----IGYV-PQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 -IAVQE--SFRLLKKV---YKVSDEDYNAHMEhVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:cd03235 84 pISVRDvvLMGLYGHKglfRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504274718 188 LDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDeGSIIYDG 240
Cdd:cd03235 163 VDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
5-240 |
3.54e-40 |
|
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: 140.75 E-value: 3.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKAYSSRSG-LKGAFRDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT 83
Cdd:cd03220 1 IELENVSKSYPTYKGGSSsLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 84 VNGmnphkereKFAQTIGVVFGQRSQLwwdiAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQR 163
Cdd:cd03220 81 VRG--------RVSSLLGLGGGFNPEL----TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 164 MRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
41-185 |
1.51e-39 |
|
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: 136.62 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVFgQRSQLWWDIAVQES 119
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVF-QDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRK----LSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
41-240 |
1.72e-39 |
|
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: 139.83 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGditvngmnphkerekfaQTIgVVFGQRSQLW--WDI---- 114
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG-----------------NDV-RLFGERRGGEdvWELrkri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 -----AVQESFRLLKKVYKV---------------SDEDYnAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIH 174
Cdd:COG1119 81 glvspALQLRFPRDETVLDVvlsgffdsiglyrepTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 175 NPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-239 |
2.37e-39 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKayssrsGLKGAFRdlftrnyrvmkAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG1116 4 AAPALELRGVSKRFP------TGGGGVT-----------ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNGmnphKEREKFAQTIGVVFgqrsqlwwdiavQEsFRLL--KKVY----------KVSDEDYNAHMEHVIQTLDIG 148
Cdd:COG1116 67 EVLVDG----KPVTGPGPDRGVVF------------QE-PALLpwLTVLdnvalglelrGVPKAERRERARELLELVGLA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 149 PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLAdiEA--LCE 226
Cdd:COG1116 130 GFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVD--EAvfLAD 207
|
250
....*....|....*
gi 504274718 227 RVVMLDE--GSIIYD 239
Cdd:COG1116 208 RVVVLSArpGRIVEE 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
42-246 |
2.64e-39 |
|
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: 138.79 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPH----KEREKFAQTIGVVFgQRSQLWWDIAVQ 117
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMGMLF-QSGALFDSLTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 E--SFRLLKKvYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:cd03261 96 EnvAFPLREH-TRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 196 IRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLR 246
Cdd:cd03261 175 IDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
27-234 |
5.48e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.45 E-value: 5.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDLfTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVFG 105
Cdd:cd00267 2 IENL-SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 qrsqlwwdiavqesfrllkkvykvsdedynahmehviqtldigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:cd00267 109 SGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
27-233 |
8.59e-39 |
|
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: 136.45 E-value: 8.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL-FTRNYRVmkAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVfG 105
Cdd:COG4133 5 AENLsCRRGERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL-G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSQLWWDIAVQESFRLLKKVYKVSDEDYNAhmEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREAI--DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504274718 186 IGLD-----VLVKLkIRQFLKEinekyNTTILLTTHDLADIEALceRVVMLDE 233
Cdd:COG4133 160 TALDaagvaLLAEL-IAAHLAR-----GGAVLLTTHQPLELAAA--RVLDLGD 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
31-248 |
8.12e-38 |
|
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: 134.63 E-value: 8.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREKFAQTIGVVFgQ 106
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltllSGKELRKARRRIGMIF-Q 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 107 RSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:cd03258 90 HFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 187 GLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:cd03258 170 ALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
43-240 |
2.18e-37 |
|
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: 133.19 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKqGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----------MNPHKERekfaqtIGVVFgQRSQLW 111
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinLPPQQRK------IGLVF-QQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESFRL-LKKVYKVSDEDYnahMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:cd03297 88 PHLNVRENLAFgLKRKRNREDRIS---VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 191 LVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03297 165 ALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-236 |
5.19e-37 |
|
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: 131.99 E-value: 5.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MN--PHKEREkfaqtIGVVFgQR 107
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGrdVTdlPPKDRD-----IAMVF-QN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 SQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504274718 188 LDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-250 |
5.67e-37 |
|
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: 140.74 E-value: 5.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 11 RKEFKAYSSRSGLKGA--FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM 87
Cdd:COG2274 458 REEGRSKLSLPRLKGDieLENVsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 88 NPHK-EREKFAQTIGVVFgQRSQLW----WD-IAVQESFRLLKKVYKVSDEdynAHMEHVIQTLDIGplLDKPV----RK 157
Cdd:COG2274 538 DLRQiDPASLRRQIGVVL-QDVFLFsgtiREnITLGDPDATDEEIIEAARL---AGLHDFIEALPMG--YDTVVgeggSN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 158 LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEIneKYNTTILLTTHDLADIeALCERVVMLDEGSII 237
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTI-RLADRIIVLDKGRIV 688
|
250
....*....|...
gi 504274718 238 YDGSLQKLRSNWG 250
Cdd:COG2274 689 EDGTHEELLARKG 701
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-230 |
1.50e-36 |
|
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: 134.03 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKayssrsglkgafrdlfTRNYRVmKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGD 81
Cdd:COG0444 2 LEVRNLKVYFP----------------TRRGVV-KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 82 ITVNGMN----PHKEREKF-AQTIGVVFgqrsqlwwdiavQESFRLLKKVYKVSD---EDYNAH--------MEHVIQTL 145
Cdd:COG0444 65 ILFDGEDllklSEKELRKIrGREIQMIF------------QDPMTSLNPVMTVGDqiaEPLRIHgglskaeaRERAIELL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 146 DI-GplLDKPVRK-------LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHD 217
Cdd:COG0444 133 ERvG--LPDPERRldrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
|
250
....*....|....
gi 504274718 218 LADIEALCERV-VM 230
Cdd:COG0444 211 LGVVAEIADRVaVM 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
35-241 |
4.95e-36 |
|
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: 129.97 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKERekfAQtIGVVF-GQRSQ 109
Cdd:cd03218 10 YGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitklPMHKR---AR-LGIGYlPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 LWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:cd03218 86 IFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 190 VLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:cd03218 166 PIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
39-236 |
2.29e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.35 E-value: 2.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT-----VNGMNPhKEREkfaqtIGVVFgQRSQLWWD 113
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrdVTDLPP-KDRN-----IAMVF-QSYALYPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQE--SFRLlkKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:COG3839 90 MTVYEniAFPL--KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504274718 192 VKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:COG3839 168 LRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
43-248 |
2.58e-35 |
|
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: 128.22 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKERekfaqtIGVVFgQRSQLWWDIAVQ 117
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnLPPEKRD------ISYVP-QNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIR 197
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 198 QFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
41-245 |
6.21e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 129.15 E-value: 6.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmNPHKEREKFA-QTIGVVfGQRSQLWWDIAVQES 119
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHArQRVGVV-PQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQF 199
Cdd:PRK13537 101 LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504274718 200 LKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK13537 181 LRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
39-231 |
8.08e-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: 126.43 E-value: 8.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM---NPHKERekfaqtiGVVFGQRSQLWWdIA 115
Cdd:cd03293 18 TALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtGPGPDR-------GYVFQQDALLPW-LT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 116 VQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:cd03293 90 VLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 504274718 196 IRQFLKEINEKYNTTILLTTHDLAdiEA--LCERVVML 231
Cdd:cd03293 170 LQEELLDIWRETGKTVLLVTHDID--EAvfLADRVVVL 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
39-255 |
8.21e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.63 E-value: 8.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFA---QTIGVVFG-QRSQLWW-- 112
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirKKVGLVFQyPEYQLFEet 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 ---DIAVQESFRLLkkvykvSDEDYN----AHMEHViqTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK13637 101 iekDIAFGPINLGL------SEEEIEnrvkRAMNIV--GLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQV 255
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESI 242
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
27-234 |
1.28e-34 |
|
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: 124.42 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFAQTIGVVF 104
Cdd:cd03228 3 FKNVsFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlRDLDLESLRKNIAYVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 gqrsqlwwdiavQESFrllkkvykvsdedynahmehviqtldigpLLDKPVRK--LSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:cd03228 83 ------------QDPF-----------------------------LFSGTIREniLSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 183 EPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEaLCERVVMLDEG 234
Cdd:cd03228 122 EATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-237 |
1.53e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFkayssrsglkGAFRdlftrnyrvmkAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG3842 2 AMPALELENVSKRY----------GDVT-----------ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNG-----MNPHKERekfaqtIGVVFgQRSQLW-----WD-IAvqesFRLlkKVYKVSDEDYNAHMEHVIQTLDIGP 149
Cdd:COG3842 61 RILLDGrdvtgLPPEKRN------VGMVF-QDYALFphltvAEnVA----FGL--RMRGVPKAEIRARVAELLELVGLEG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 150 LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVV 229
Cdd:COG3842 128 LADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIA 207
|
....*...
gi 504274718 230 MLDEGSII 237
Cdd:COG3842 208 VMNDGRIE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
39-241 |
6.81e-34 |
|
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: 124.72 E-value: 6.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKEREKfaqtIGVVFgQRSQLWWD 113
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireQDPVELRRK----IGYVI-QQIGLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGP--LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:cd03295 90 MTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 192 VKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:cd03295 170 TRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
39-245 |
7.51e-34 |
|
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: 124.60 E-value: 7.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQT----IGVVF---------- 104
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqIGMIFqqfnlierls 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 ----------GQRSqLWWDIavqesFRLLKKvykvsdEDYNAHMEhVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIH 174
Cdd:cd03256 95 vlenvlsgrlGRRS-TWRSL-----FGLFPK------EEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 175 NPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
42-234 |
1.61e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.62 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKEREKfaqtIGVVFgQRSQlWWDIAV 116
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsaMPPPEWRRQ----VAYVP-QEPA-LWGGTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLlkkVYKVSDEDYN-AHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:COG4619 91 RDNLPF---PFQLRERKFDrERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504274718 195 KIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
40-245 |
1.66e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 124.96 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKERE---KFAQTIGVVFGQRSQLWWDIAV 116
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVGMVFQDPDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK13636 181 MKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
32-245 |
3.43e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 125.33 E-value: 3.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMnPHKEREKFAQT-IGVVfGQRSQL 110
Cdd:PRK13536 48 SKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV-PVPARARLARArIGVV-PQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK13536 126 DLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 191 LVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK13536 206 HARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
40-248 |
3.44e-33 |
|
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: 128.72 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVfGQRSQLwwdIA--V 116
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWV-PQNPYL---FAgtI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKvyKVSDEDYN-----AHMEHVIQTLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:COG4988 428 RENLRLGRP--DASDEELEaaleaAGLDEFVAALPDG--LDTPLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 188 LDV----LVKLKIRQFLKeinekyNTTILLTTHDLADIeALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:COG4988 504 LDAeteaEILQALRRLAK------GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
40-245 |
4.62e-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: 128.73 E-value: 4.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREK-FAQTIGVVfGQRSQLWwDIAVQE 118
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdLRRRIAVV-PQRPHLF-DTTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFRLLKKvyKVSDEDynahMEHVIQTLDIGPL-------LDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:COG4987 428 NLRLARP--DATDEE----LWAALERVGLGDWlaalpdgLDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 188 LDVLVKlkiRQFLKEINEKY-NTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKL 245
Cdd:COG4987 502 LDAATE---QALLADLLEALaGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-242 |
6.32e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.80 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFkayssrSGLKGAFRdlftrnyrvmkAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:COG1135 2 IELENLSKTF------PTKGGPVT-----------ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NGMN----PHKEREKFAQTIGVVFgqrsqlwwdiavqESFRLL--KKVY----------KVSDEDYNahmEHVIQTLDIG 148
Cdd:COG1135 65 DGVDltalSERELRAARRKIGMIF-------------QHFNLLssRTVAenvalpleiaGVPKAEIR---KRVAELLELV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 149 PLLDK----PvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD------VLvklkirQFLKEINEKYNTTILLTTHDL 218
Cdd:COG1135 129 GLSDKadayP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettrsIL------DLLKDINRELGLTIVLITHEM 201
|
250 260
....*....|....*....|....
gi 504274718 219 ADIEALCERVVMLDEGSIIYDGSL 242
Cdd:COG1135 202 DVVRRICDRVAVLENGRIVEQGPV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-245 |
2.36e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.33 E-value: 2.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFkayssrsglkGAFrdlftrnyrvmKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:COG1118 3 IEVRNISKRF----------GSF-----------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NG------MNPHKERekfaqtIGVVFgQRSQLWWDIAVQE--SFRLlkKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVR 156
Cdd:COG1118 62 NGrdlftnLPPRERR------VGFVF-QHYALFPHMTVAEniAFGL--RVRPPSKAEIRARVEELLELVQLEGLADRYPS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 157 KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
....*....
gi 504274718 237 IYDGSLQKL 245
Cdd:COG1118 213 EQVGTPDEV 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
35-237 |
2.25e-31 |
|
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: 116.97 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKfaqTIGVVFgQ--RSQLW 111
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPiKAKERRK---SIGYVM-QdvDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDiAVQESFRLLKKVYkvsdEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:cd03226 86 TD-SVREELLLGLKEL----DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504274718 192 VKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:cd03226 161 NMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
32-245 |
2.79e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 117.59 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREkfaqtIGVVFgQR 107
Cdd:TIGR00968 7 SKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDatrvHARDRK-----IGFVF-QH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 SQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 188 LDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEV 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
44-245 |
2.84e-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: 2.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHK--------EREKF-----AQTIGvvFG 105
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltaLPPAErpvsmlfqENNLFphltvAQNIG--LG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSQLwwdiavqesfrllkkvyKVSDEDyNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:COG3840 96 LRPGL-----------------KLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:COG3840 158 SALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
40-241 |
1.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.01 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQT-IGVVFGQRSQLWWDIAVQE 118
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKkIGIIFQNPDNQFIGATVED 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 --SFRLLKKvyKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK13632 104 diAFGLENK--KVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLADIeALCERVVMLDEGSIIYDGS 241
Cdd:PRK13632 182 KKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
41-237 |
1.48e-30 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 116.44 E-value: 1.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPhKEREKFAQTIGVVF-------GQRS 108
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlyqLDR-KQRRAFRRDVQLVFqdspsavNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 QLWWDIAvqESFRLLKKVYKVSDEdynAHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:TIGR02769 106 TVRQIIG--EPLRHLTSLDESEQK---ARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 188 LDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
39-236 |
1.99e-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: 114.81 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREKFAQTIGVVFgQRSQLWWDI 114
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlRGRAIPYLRRKIGVVF-QDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:cd03292 94 NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504274718 195 KIRQFLKEINeKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:cd03292 174 EIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-237 |
6.48e-30 |
|
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: 119.40 E-value: 6.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKayssrsgLKgafRDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGDITV 84
Cdd:COG4172 276 LEARDLKVWFP-------IK---RGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NGMN----PHKEREKFAQTIGVVF-------------GQrsqlwwdIaVQESFRLLKKvykvsDEDYNAHMEHVIQTL-D 146
Cdd:COG4172 345 DGQDldglSRRALRPLRRRMQVVFqdpfgslsprmtvGQ-------I-IAEGLRVHGP-----GLSAAERRARVAEALeE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 147 IGplLDKPVR-----KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADI 221
Cdd:COG4172 412 VG--LDPAARhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVV 489
|
250
....*....|....*.
gi 504274718 222 EALCERVVMLDEGSII 237
Cdd:COG4172 490 RALAHRVMVMKDGKVV 505
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
11-248 |
6.77e-30 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.97 E-value: 6.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 11 RKEFKAYSSRSGLKGA--FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM 87
Cdd:TIGR03375 448 RPEGTRFLHRPRLQGEieFRNVsFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGV 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 88 NPHK-EREKFAQTIGVVfGQRSQLWW-----DIAVQESFrllkkvykVSDEDynahmehVIQTLDIGPL----------L 151
Cdd:TIGR03375 528 DIRQiDPADLRRNIGYV-PQDPRLFYgtlrdNIALGAPY--------ADDEE-------ILRAAELAGVtefvrrhpdgL 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 152 DKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKynTTILLTTHDLADIEaLCER 227
Cdd:TIGR03375 592 DMQIgergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLD-LVDR 668
|
250 260
....*....|....*....|....*
gi 504274718 228 VVMLDEGSIIYDGS----LQKLRSN 248
Cdd:TIGR03375 669 IIVMDNGRIVADGPkdqvLEALRKG 693
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
46-271 |
1.07e-29 |
|
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: 113.02 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 46 FTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKfaqtIGVVfGQRSQLWWD--IAVQESF--- 120
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH----IGYV-PQRHEFAWDfpISVAHTVmsg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 121 --RLLKKVYKVSDEDYNAhMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQ 198
Cdd:TIGR03771 76 rtGHIGWLRRPCVADFAA-VRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504274718 199 FLKEINEKyNTTILLTTHDLADIEALCERVVMLDeGSIIYDGSLQKLRsnwgDLKQVTFEFGTAPNKEQLKLL 271
Cdd:TIGR03771 155 LFIELAGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQ----DPAPWMTTFGVSDSSPLLRIV 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
41-241 |
1.70e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.33 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVfGQRSQLWWDIAVQES 119
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAVL-PQHSSLSFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALI------HNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK13548 97 VAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 194 LKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK13548 177 HHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
42-240 |
2.89e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 117.47 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITvngMNPHKEREKFAQT---------IGVVFGQRSQLWw 112
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS---IPKGLRIGYLPQEppldddltvLDTVLDGDAELR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 diAVQESFRLLKKVYKVSDEDYN------AHMEH------------VIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALI 173
Cdd:COG0488 91 --ALEAELEELEAKLAEPDEDLErlaelqEEFEAlggweaearaeeILSGLGFPEeDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 174 HNPPLLFLDEPTIGLDVLVKLKIRQFLKeineKYNTTILLTTHDLADIEALCERVVMLDEGSII-YDG 240
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLESIEWLEEFLK----NYPGTVLVVSHDRYFLDRVATRILELDRGKLTlYPG 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
41-237 |
3.13e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.24 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK----EREKFAQTIGVVF-------GQRSQ 109
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIQMVFqdsisavNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 LWWDIAvqESFRLLKKVykvSDEDYNAHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK10419 108 VREIIR--EPLRHLLSL---DKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504274718 189 DVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-239 |
3.79e-29 |
|
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: 109.83 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM--NPHKEREKFAQTIGVVFgQrsq 109
Cdd:cd03216 7 TKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGIAMVY-Q--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 lwwdiavqesfrllkkvykvsdedynahmehviqtldigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:cd03216 83 ------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 190 VlvkLKIRQFLKEINE--KYNTTILLTTHDLADIEALCERVVMLDEGSIIYD 239
Cdd:cd03216 115 P---AEVERLFKVIRRlrAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
35-248 |
4.06e-29 |
|
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: 111.37 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHkerEKFAQTIGVVFgQRSQ 109
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditgLPPH---ERARAGIGYVP-EGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 LWWDIAVQESFRLlkKVYKVSDEDYNAHMEHViqtLDIGPLL----DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd03224 86 IFPELTVEENLLL--GAYARRRAKRKARLERV---YELFPRLkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 186 IGLD-VLVKlKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:cd03224 161 EGLApKIVE-EIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
39-237 |
4.51e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 4.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKerekfAQT--IGVVFgQRSQLW 111
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvrfRSPRD-----AQAagIAIIH-QELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQES-F--RLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:COG1129 92 PNLSVAENiFlgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504274718 189 -----DVLVKLkIRQFLKEinekyNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:COG1129 172 terevERLFRI-IRRLKAQ-----GVAIIYISHRLDEVFEIADRVTVLRDGRLV 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
26-240 |
6.07e-29 |
|
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: 109.71 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 26 AFRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVf 104
Cdd:cd03247 2 SINNVsFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 gqrSQlwwdiavqesfrllkKVYKVSDEDYNahmehviqtlDIGplldkpvRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:cd03247 81 ---NQ---------------RPYLFDTTLRN----------NLG-------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 185 TIGLDVLVKLKI-RQFLKEINEKyntTILLTTHDLADIEALcERVVMLDEGSIIYDG 240
Cdd:cd03247 126 TVGLDPITERQLlSLIFEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-240 |
1.22e-28 |
|
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: 109.89 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNpHKEREKFAQTIGVVFgQRSQLWWDIAVQESFRL 122
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD-VTAAPPADRPVSMLF-QENNLFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 123 -LKKVYKVSDEDYNAhMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLK 201
Cdd:cd03298 94 gLSPGLKLTAEDRQA-IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 504274718 202 EINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03298 173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
35-248 |
1.68e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 110.50 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREKFaqtiGVvfG---QR 107
Cdd:COG1137 13 YGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlPMHKRARL----GI--GylpQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 SQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:COG1137 87 ASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 188 LDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:COG1137 167 VDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNN 226
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
40-245 |
2.10e-28 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 109.77 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP----TSGDITVNGM--NPHKEREKFAQTI--------GVVFG 105
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRplLPLSIRGRHIATImqnprtafNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSQLwwdiavQESFRLLKKVYKVSDEDYNAHMEHViqTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:TIGR02770 81 MGNHA------IETLRSLGKLSKQARALILEALEAV--GLPDPEeVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 185 TIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEI 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
40-234 |
3.21e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.22 E-value: 3.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPH----KERekfaqtigVvfGQRSQ---L 110
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGdiatRRR--------V--GYMSQafsL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD- 189
Cdd:NF033858 351 YGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDp 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504274718 190 --------VLVKLKIRQflkeinekyNTTILLTTHDLAdiEAL-CERVVMLDEG 234
Cdd:NF033858 431 vardmfwrLLIELSRED---------GVTIFISTHFMN--EAErCDRISLMHAG 473
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-241 |
3.25e-28 |
|
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: 109.74 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 4 AIEVNQLRKEFkayssrsglkGAFRdlftrnyrvmkAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT 83
Cdd:cd03296 2 SIEVRNVSKRF----------GDFV-----------ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 84 VNGMN----PHKEREkfaqtIGVVFgQRSQLWWDIAVQES----FRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPV 155
Cdd:cd03296 61 FGGEDatdvPVQERN-----VGFVF-QHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 156 RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGS 235
Cdd:cd03296 135 AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
....*.
gi 504274718 236 IIYDGS 241
Cdd:cd03296 215 IEQVGT 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
41-241 |
8.53e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 109.05 E-value: 8.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKERekfAQTIGVVfGQRSQLWWDIAV 116
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlaawSPWEL---ARRRAVL-PQHSSLAFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAAL--IHNPP-----LLFLDEPTIGLD 189
Cdd:COG4559 93 EEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggprWLFLDEPTSALD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 190 VLVKLKIRQFLKEINEKyNTTILLTTHDL------ADiealceRVVMLDEGSIIYDGS 241
Cdd:COG4559 173 LAHQHAVLRLARQLARR-GGGVVAVLHDLnlaaqyAD------RILLLHQGRLVAQGT 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
40-236 |
9.09e-28 |
|
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: 108.09 E-value: 9.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-----PHKERekfaqtIGVVFgQRSQLWWDI 114
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRP------VNTVF-QNYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:cd03300 88 TVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504274718 195 KIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:cd03300 168 DMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
41-240 |
1.60e-27 |
|
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: 106.48 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP--TSGDITVNGMNphKEREKFAQTIGVVfGQRSQLWWDIAVQE 118
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP--LDKRSFRKIIGYV-PQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFrllkkvykvsdeDYNAHMehviqtldigplldkpvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQ 198
Cdd:cd03213 102 TL------------MFAAKL-----------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504274718 199 FLKEInEKYNTTILLTTHDL-ADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03213 153 LLRRL-ADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
39-256 |
2.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.71 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFA----QTIGVVFG-QRSQLWW 112
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITiTHKTKDKYIrpvrKRIGMVFQfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DiAVQESFRLLKKVYKVSDEDYNAHMEHVIqtLDIG---PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:PRK13646 101 D-TVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 190 VLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLrsnWGDLKQVT 256
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL---FKDKKKLA 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-305 |
3.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.90 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKAYSSRSGLkgafrdlftrnyrvmkavNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTL------------------NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNGM-----NPHKEREKfaqtIGVVFGQRSQLWWDIAVQE--SFRLLKKvyKVSDEDYNAHMEHVIQTLDIGPLLDK 153
Cdd:PRK13650 63 QIIIDGDllteeNVWDIRHK----IGMVFQNPDNQFVGATVEDdvAFGLENK--GIPHEEMKERVNEALELVGMQDFKER 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 154 PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIeALCERVVMLDE 233
Cdd:PRK13650 137 EPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKN 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 234 GSIIYDGSLQKLRSNWGDLKQVTFEFgtaPNKEQLK--LLTQGMPVnwiegDQKYLWTAQLQNKgdlMSQLIAK 305
Cdd:PRK13650 216 GQVESTSTPRELFSRGNDLLQLGLDI---PFTTSLVqsLRQNGYDL-----PEGYLTEKELEEQ---LWELISK 278
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
43-237 |
4.70e-27 |
|
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: 106.36 E-value: 4.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK----EREKF-AQTIGVVFgqrsqlwwdiavq 117
Cdd:COG4181 30 GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedARARLrARHVGFVF------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ESFRLLkkvykvsdedynAHM---EHVIQTLDI-------------------GPLLDKPVRKLSLGQRMRCELAAALIHN 175
Cdd:COG4181 97 QSFQLL------------PTLtalENVMLPLELagrrdarararallervglGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 176 PPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIeALCERVVMLDEGSII 237
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLV 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
45-236 |
5.89e-27 |
|
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: 105.71 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 45 SFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNpHKEREKFAQTIGVVFgQRSQLWWDIAVQESFRL-L 123
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HTGLAPYQRPVSMLF-QENNLFAHLTVRQNIGLgL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYKVSDEDyNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEI 203
Cdd:TIGR01277 96 HPGLKLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180 190
....*....|....*....|....*....|...
gi 504274718 204 NEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
40-248 |
6.29e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.09 E-value: 6.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmNPHKEREK----FAQTIGVVFGQRSQLWWDIA 115
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKYDKKslleVRKTVGIVFQNPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 116 VQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504274718 196 IRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK13639 176 IMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
33-248 |
7.37e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.13 E-value: 7.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVN----GMNPHKEREKfaQTIGVVfGQRS 108
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdediSLLPLHARAR--RGIGYL-PQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 QLWWDIAVQESFRLLKKVYK-VSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 188 LDVLVKLKIRQFLKEINEkYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
40-248 |
8.08e-27 |
|
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: 105.83 E-value: 8.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHK-----------EREkfaqtigvV 103
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGeditgLPPHRiarlgigyvpeGRR--------I 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 FGQRSqlwwdiaVQESFRL---LKKVYKVSDEDynahMEHViqtLDIGPLL----DKPVRKLSLGQRMRCELAAALIHNP 176
Cdd:COG0410 90 FPSLT-------VEENLLLgayARRDRAEVRAD----LERV---YELFPRLkerrRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504274718 177 PLLFLDEPTIGLD-VLVKlKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:COG0410 156 KLLLLDEPSLGLApLIVE-EIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAD 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
45-247 |
1.07e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.43 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 45 SFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNpHKEREKFAQTIGVVFgQRSQLWWDIAVQESFRL-L 123
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLF-QENNLFSHLTVAQNIGLgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYKVSDEDyNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEI 203
Cdd:PRK10771 97 NPGLKLNAAQ-REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504274718 204 NEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRS 247
Cdd:PRK10771 176 CQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
40-289 |
1.66e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.87 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKE-----REKfaqtIGVVFGQRSQLWWDI 114
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtvwdvRRQ----VGMVFQNPDNQFVGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQE--SFRLLKKvyKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK13635 98 TVQDdvAFGLENI--GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 193 KLKIRQFLKEINEKYNTTILLTTHDLaDIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQVTFEFgtaPNKEQLK-LL 271
Cdd:PRK13635 176 RREVLETVRQLKEQKGITVLSITHDL-DEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQEIGLDV---PFSVKLKeLL 251
|
250 260
....*....|....*....|...
gi 504274718 272 TQG---MPVNWI--EGDQKYLWT 289
Cdd:PRK13635 252 KRNgilLPNTYLtmESLVDELWT 274
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-230 |
1.98e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 106.74 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKAyssRSGLkgafrdlFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:COG4608 8 LEVRDLKKHFPV---RGGL-------FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NG-----MNPHKEREK-----------FA-----QTIG-------VVFGQRSQLWWDIAVQEsfrLLKKVyKVSDEDYN- 135
Cdd:COG4608 78 DGqditgLSGRELRPLrrrmqmvfqdpYAslnprMTVGdiiaeplRIHGLASKAERRERVAE---LLELV-GLRPEHADr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 136 -AHMehviqtldigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLT 214
Cdd:COG4608 154 yPHE-------------------FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFI 214
|
250
....*....|....*..
gi 504274718 215 THDLADIEALCERV-VM 230
Cdd:COG4608 215 SHDLSVVRHISDRVaVM 231
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
39-240 |
4.36e-26 |
|
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: 103.50 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGDITVNGMNPHkeREKFAQTIGVVfGQRSQLWWDIA 115
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK--PDQFQKCVAYV-RQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 116 VQES------FRL----LKKVYKVSDEDYnahmehVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd03234 98 VRETltytaiLRLprksSDAIRKKRVEDV------LLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKyNTTILLTTHD-LADIEALCERVVMLDEGSIIYDG 240
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-230 |
5.66e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 5.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFkayssrsglkGAFRdlftrnyrvmkAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG3845 2 MPPALELRGITKRF----------GGVV-----------ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNG--MNPHKEREKFAQTIGVVF-------------------GQRSQLWWDIAvqesfRLLKKVYKVSDEdYNahme 139
Cdd:COG3845 61 EILIDGkpVRIRSPRDAIALGIGMVHqhfmlvpnltvaenivlglEPTKGGRLDRK-----AARARIRELSER-YG---- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 140 hviqtLDIGPllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL-----DVLVKLkIRQFLKEinekyNTTILLT 214
Cdd:COG3845 131 -----LDVDP--DAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqeaDELFEI-LRRLAAE-----GKSIIFI 197
|
250
....*....|....*..
gi 504274718 215 THDLADIEALCERV-VM 230
Cdd:COG3845 198 THKLREVMAIADRVtVL 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
38-231 |
6.48e-26 |
|
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: 107.76 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 38 MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFAQTIGVVfGQRSQLWWDiAV 116
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADADSWRDQIAWV-PQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVykVSDEDYNAHMEHV-----IQTLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:TIGR02857 413 AENIRLARPD--ASDAEIREALERAgldefVAALPQG--LDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 188 LD----VLVKLKIRQFLKeinekyNTTILLTTHDLADIEaLCERVVML 231
Cdd:TIGR02857 489 LDaeteAEVLEALRALAQ------GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-263 |
6.65e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 28 RDLfTRNYRV-MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKER-EKFAQTIGVVFG 105
Cdd:PRK13652 7 RDL-CYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENiREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK13652 86 NPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQVTFEFGTAP 263
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLDLPSLP 243
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
42-236 |
6.96e-26 |
|
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: 102.82 E-value: 6.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK----EREKFA-QTIGVVFgQRSQLWWDIAV 116
Cdd:TIGR02211 22 KGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlssnERAKLRnKKLGFIY-QFHHLLPDFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:TIGR02211 101 LENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLADIEALcERVVMLDEGSI 236
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
39-241 |
8.24e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 107.94 E-value: 8.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVFgqrsqlwwdiavQ 117
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVP------------Q 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ESF----------RLLKKvyKVSDEDY-----NAHMEHVIQTLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPL 178
Cdd:COG1132 422 DTFlfsgtireniRYGRP--DATDEEVeeaakAAQAHEFIEALPDG--YDTVVgergVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504274718 179 LFLDEPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGS 241
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-245 |
9.88e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.48 E-value: 9.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFkayssrSGLKGAFRDLFTRNYrvmkAVNDISFTVKQGEMVGYIGENGAGKSTT-IKMLTgiLTPTSGDIT 83
Cdd:PRK15134 276 LDVEQLQVAF------PIRKGILKRTVDHNV----VVKNISFTLRPGETLGLVGESGSGKSTTgLALLR--LINSQGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 84 VNGMNPHKEREK----FAQTIGVVFGQ-RSQLWWDIAVQEsfrLLKKVYKVSDEDYNAHM--EHVIQTL-DIGplLDKPV 155
Cdd:PRK15134 344 FDGQPLHNLNRRqllpVRHRIQVVFQDpNSSLNPRLNVLQ---IIEEGLRVHQPTLSAAQreQQVIAVMeEVG--LDPET 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 156 R-----KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVM 230
Cdd:PRK15134 419 RhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIV 498
|
250
....*....|....*
gi 504274718 231 LDEGSIIYDGSLQKL 245
Cdd:PRK15134 499 LRQGEVVEQGDCERV 513
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
40-255 |
1.15e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKERE--KFAQTIGVVF-GQRSQLWWDIaV 116
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFqNPDNQIVATI-V 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK13633 104 EEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLAD-IEAlcERVVMLDEGSIIYDGSLQKLRSNWGDLKQV 255
Cdd:PRK13633 184 VNTIKELNKKYGITIILITHYMEEaVEA--DRIIVMDSGKVVMEGTPKEIFKEVEMMKKI 241
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
39-219 |
1.16e-25 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 101.35 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKERE---KFAQTIGVVFGQRSQ------ 109
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllERRQRVGLVFQDPDDqlfaad 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 LWWDIAvqesFRLLKkvYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:TIGR01166 86 VDQDVA----FGPLN--LGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|
gi 504274718 190 VLVKLKIRQFLKEINEKyNTTILLTTHDLA 219
Cdd:TIGR01166 160 PAGREQMLAILRRLRAE-GMTVVISTHDVD 188
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
41-243 |
1.46e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 1.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDItvngmnphkereKFAQTIGV-VFGQRsqlwwdiavQES 119
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------------KLGETVKIgYFDQH---------QEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYK-VSDEDYNAHMEHVIQTLdiGPLL------DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDvlv 192
Cdd:COG0488 390 LDPDKTVLDeLRDGAPGGTEQEVRGYL--GRFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD--- 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 193 kLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSII-YDGSLQ 243
Cdd:COG0488 465 -IETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVReYPGGYD 515
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-241 |
1.60e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKAYSsrsglkgafrdlftrnyRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:PRK11153 2 IELKNISKVFPQGG-----------------RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NGMN----PHKEREKFAQTIGVVFgqrsqlwwdiavqESFRLL--KKVY----------KVSDEDYNAHmehVIQTLDIG 148
Cdd:PRK11153 65 DGQDltalSEKELRKARRQIGMIF-------------QHFNLLssRTVFdnvalplelaGTPKAEIKAR---VTELLELV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 149 PLLDKPVR---KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALC 225
Cdd:PRK11153 129 GLSDKADRypaQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRIC 208
|
250
....*....|....*.
gi 504274718 226 ERVVMLDEGSIIYDGS 241
Cdd:PRK11153 209 DRVAVIDAGRLVEQGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
40-237 |
1.65e-25 |
|
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: 103.11 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKE-REKFAQTIGVVFgQRSQLWWDI 114
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamSRKElRELRRKKISMVF-QSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504274718 195 KIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:cd03294 198 EMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
37-240 |
1.83e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.63 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 37 VMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK------------------------- 91
Cdd:PRK13651 19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekekvleklviqktrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 92 ----------------EREKFAQTI--GVVFGQRSqlwWDIAVQESFRLLKKVYKVS--DEDYnahmehviqtldigplL 151
Cdd:PRK13651 99 kikeirrrvgvvfqfaEYQLFEQTIekDIIFGPVS---MGVSKEEAKKRAAKYIELVglDESY----------------L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 152 DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVML 231
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFF 238
|
....*....
gi 504274718 232 DEGSIIYDG 240
Cdd:PRK13651 239 KDGKIIKDG 247
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
40-245 |
2.22e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 106.58 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVFgQRSQLwWDIAVQE 118
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVF-QDAGL-FNRSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFRLLKKvyKVSDEDYNAHMEHViQTLDIgpLLDKPV----------RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK13657 428 NIRVGRP--DATDEEMRAAAERA-QAHDF--IERKPDgydtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 189 DVLVKLKIRQFLKEINEkyNTTILLTTHDLADI-EAlcERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK13657 503 DVETEAKVKAALDELMK--GRTTFIIAHRLSTVrNA--DRILVFDNGRVVESGSFDEL 556
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
41-234 |
2.23e-25 |
|
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: 101.77 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN---PHKEREkfaqtigVVFGQRSQLWWDIAVQ 117
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQitePGPDRM-------VVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ESFRLLKKVYK-VSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:TIGR01184 74 NIALAVDRVLPdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
40-230 |
5.13e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 102.88 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGDITVNGMN----PHKEREKF-AQTIGVVFgqrsqlw 111
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREilnlPEKELNKLrAEQISMIF------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 wdiavQESFRLLKKVYKVSDEDYNAHMEHviQTLDIGPLLDKPVRKL-------------------SLGQRMRCELAAAL 172
Cdd:PRK09473 104 -----QDPMTSLNPYMRVGEQLMEVLMLH--KGMSKAEAFEESVRMLdavkmpearkrmkmyphefSGGMRQRVMIAMAL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 173 IHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERV-VM 230
Cdd:PRK09473 177 LCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVlVM 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
39-236 |
5.52e-25 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 100.30 E-value: 5.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM---NPHKEREKFAQTIGVVFgQRSQLWWDIA 115
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltDDKKNINELRQKVGMVF-QQFNLFPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 116 VQESFRL-LKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV-LVK 193
Cdd:cd03262 93 VLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPeLVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504274718 194 --LK-IRQFLKEinekyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:cd03262 173 evLDvMKDLAEE-----GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-258 |
7.43e-25 |
|
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: 105.87 E-value: 7.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVV--FGQRSQLwwdIAVQ 117
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCpqFDAIDDL---LTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIR 197
Cdd:TIGR01257 2031 EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 198 QFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQVTFE 258
Cdd:TIGR01257 2111 NTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMK 2170
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
33-236 |
9.40e-25 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 102.81 E-value: 9.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREkfaqtIGVVFgQRS 108
Cdd:TIGR03265 12 KRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDitrlPPQKRD-----YGIVF-QSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 QLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:TIGR03265 86 ALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSAL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 189 DVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:TIGR03265 166 DARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
37-240 |
1.20e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 104.11 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 37 VMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG-----------DITVNGMNphkEREKFAQTIGVVFg 105
Cdd:TIGR03269 296 VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvDMTKPGPD---GRGRAKRYIGILH- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSQLWWDIAVQESfrlLKKVYKVSDEDYNAHMEHVIQTLDIG-------PLLDKPVRKLSLGQRMRCELAAALIHNPPL 178
Cdd:TIGR03269 372 QEYDLYPHRTVLDN---LTEAIGLELPDELARMKAVITLKMVGfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 179 LFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-243 |
2.25e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.33 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGV-VFGQRSQL 110
Cdd:PRK09700 12 GKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIgIIYQELSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESF---RLL-KKVYKVSDEDYNAHMEHVIQTLDIGPL---LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:PRK09700 92 IDELTVLENLyigRHLtKKVCGVNIIDWREMRVRAAMMLLRVGLkvdLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 184 PTIGL-----DVLVkLKIRQFLKEinekyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQ 243
Cdd:PRK09700 172 PTSSLtnkevDYLF-LIMNQLRKE-----GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
40-218 |
3.89e-24 |
|
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: 102.82 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSQLwWDIAVQES 119
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTTVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKvyKVSDEDYNAHMEHV-----IQTLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:TIGR02868 429 LRLARP--DATDEELWAALERVgladwLRALPDG--LDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*....
gi 504274718 191 LVKLK-IRQFLKEINEKyntTILLTTHDL 218
Cdd:TIGR02868 505 ETADElLEDLLAALSGR---TVVLITHHL 530
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
40-248 |
5.23e-24 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT-----VNGMNPHKEREKfaqtiGVV--FgQRSQLWW 112
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhIEGLPGHQIARM-----GVVrtF-QHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DIAVQESFR--------------LLK-KVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPP 177
Cdd:PRK11300 94 EMTVIENLLvaqhqqlktglfsgLLKtPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 178 LLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
39-240 |
5.27e-24 |
|
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: 97.66 E-value: 5.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKERekfaQTIGVVfGQRSQLWWD 113
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqLDPADLR----RNIGYV-PQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 iavqeSFR---LLKKVYkVSDEDynahMEHVIQTLDIGPL-------LDKPV----RKLSLGQRMRCELAAALIHNPPLL 179
Cdd:cd03245 93 -----TLRdniTLGAPL-ADDER----ILRAAELAGVTDFvnkhpngLDLQIgergRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 180 FLDEPTIGLD----VLVKLKIRQFLKEinekynTTILLTTHDLAdIEALCERVVMLDEGSIIYDG 240
Cdd:cd03245 163 LLDEPTSAMDmnseERLKERLRQLLGD------KTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
39-239 |
8.02e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKERE-KFAQTIGVVF------------- 104
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEyKRAKYIGRVFqdpmmgtapsmti 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 ----------GQRSQLwwdiavqeSFRLLKKVYkvsdedynAHMEHVIQTLDIGpL---LDKPVRKLSLGQRMRCELAAA 171
Cdd:COG1101 100 eenlalayrrGKRRGL--------RRGLTKKRR--------ELFRELLATLGLG-LenrLDTKVGLLSGGQRQALSLLMA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 172 LIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYD 239
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
27-245 |
8.08e-24 |
|
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: 97.64 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDLfTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGIL-----TPTSGDITVNGMN---PHKEREKFAQ 98
Cdd:cd03260 3 LRDL-NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDiydLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 99 TIGVVFGQRSQLwwDIAVQESFRLLKKVYKVSDEDynAHMEHVIQTLDIGPLLDK-----PVRKLSLGQRMRCELAAALI 173
Cdd:cd03260 82 RVGMVFQKPNPF--PGSIYDNVAYGLRLHGIKLKE--ELDERVEEALRKAALWDEvkdrlHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 174 HNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYntTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
41-241 |
1.16e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREkFAQTIGVVfGQRSQLWWDIAVQE 118
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpISMLSSRQ-LARRLALL-PQHHLTPEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFRLLKKVY-----KVSDEDyNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK11231 96 LVAYGRSPWlslwgRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 194 LKIRQFLKEINEKYNTTILLtTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK11231 175 VELMRLMRELNTQGKTVVTV-LHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
38-234 |
1.39e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.14 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 38 MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmNPHK---EREKFAQTIGVVFgQRSQLWWDI 114
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-QEMRfasTTAALAAGVAIIY-QELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESF---RLLKKVYKVSDEDYNAHMEHVIQTL--DIGPllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL- 188
Cdd:PRK11288 95 TVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLgvDIDP--DTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLs 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 189 ----DVLVKLkIRQFLKEinekyNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:PRK11288 173 areiEQLFRV-IRELRAE-----GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
39-239 |
1.63e-23 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 98.24 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKEREK----------F-----AQ 98
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGedirdLDPVELRRRigyviqqiglFphmtvAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 99 TIGVVFgqrsqlwwdiavqesfRLLKkvykVSDEDYNAHMEHVIQT--LDIGPLLDKPVRKLSLGQRMRCELAAALIHNP 176
Cdd:COG1125 96 NIATVP----------------RLLG----WDKERIRARVDELLELvgLDPEEYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 177 PLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLaDiEA--LCERVVMLDEGSII-YD 239
Cdd:COG1125 156 PILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDI-D-EAlkLGDRIAVMREGRIVqYD 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
42-236 |
1.95e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 99.33 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MN--PHKEREkfaqtIGVVFgQRSQLWWDIAVQ 117
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrMNdvPPAERG-----VGMVF-QSYALYPHLSVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 E--SFRLlkKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK11000 94 EnmSFGL--KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504274718 196 IRQFLKEINEKYNTTILLTTHDlaDIEA--LCERVVMLDEGSI 236
Cdd:PRK11000 172 MRIEISRLHKRLGRTMIYVTHD--QVEAmtLADKIVVLDAGRV 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
41-236 |
2.89e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.15 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSQLWWDIAVQESF 120
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 121 RLLKKVYK----VSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK09536 99 EMGRTPHRsrfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504274718 197 RQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK09536 179 LELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
40-231 |
3.81e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.61 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmnphkerekfAQTIGVVFgQRSQLWWD--IAVQ 117
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVP-QRSEVPDSlpLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ES-----FRLLKKVYKVSDEDyNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:NF040873 76 DLvamgrWARRGLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 504274718 193 KLKIRQFLKEINEKyNTTILLTTHDLADIeALCERVVML 231
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
42-234 |
4.92e-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: 92.90 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmnphkerekfaqtiGVVFGQRSQLwwdiavqesfr 121
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS--------------TVKIGYFEQL----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 122 llkkvykvsdedynahmehviqtldigplldkpvrklSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLK 201
Cdd:cd03221 72 -------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|...
gi 504274718 202 EinekYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:cd03221 115 E----YPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
41-245 |
5.76e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 5.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKeREKFAQTIGVVFgQRSQLWWDIAVQESF 120
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-RSIQQRDICMVF-QSYALFPHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 121 RLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFL 200
Cdd:PRK11432 100 GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504274718 201 KEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK11432 180 RELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-235 |
1.08e-22 |
|
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: 94.42 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFkayssrsglkgafrDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:COG4778 1 MTTLLEVENLSKTF--------------TLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNgmnpHK----------EREKFA---QTIGVVfgqrSQlwwdiavqesFrlLKKVYKVSdedynahmehviqTLDI 147
Cdd:COG4778 67 SILVR----HDggwvdlaqasPREILAlrrRTIGYV----SQ----------F--LRVIPRVS-------------ALDV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 148 --GPLLDKPV---------RKL------------------SLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQ 198
Cdd:COG4778 114 vaEPLLERGVdreeararaRELlarlnlperlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVE 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 504274718 199 FLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGS 235
Cdd:COG4778 194 LIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
37-254 |
1.10e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 99.03 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 37 VMKavnDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMnPHKERE-KFAQTIGVVFGQRSQLW---- 111
Cdd:TIGR00958 496 VLK---GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV-PLVQYDhHYLHRQVALVGQEPVLFsgsv 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 -WDIAVQESFRLLKKVYKVSDE----DYNAHMEHVIQTlDIGPlldkPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:TIGR00958 572 rENIAYGLTDTPDEEIMAAAKAanahDFIMEFPNGYDT-EVGE----KGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 187 GLDVlvklKIRQFLKEINEKYNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKLRSNWGDLKQ 254
Cdd:TIGR00958 647 ALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
39-254 |
1.41e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV------NGMNPhKEREKFAQTIGVVFgQ--RSQL 110
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKN-KKLKPLRKKVGIVF-QfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WwDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:PRK13634 99 F-EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 190 VLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQ 254
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEA 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
40-295 |
1.42e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGD---ITVNGMNPHKE-----REKfaqtIGVVFGQRSQLW 111
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKtvwdiREK----VGIVFQNPDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 192 VKLKIRQFLKEINEKYNTTILLTTHDLaDIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQVTFEFGTApNKEQLKLL 271
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDI-DEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEIGLDIPFV-YKLKNKLK 255
|
250 260
....*....|....*....|....*...
gi 504274718 272 TQGMPV----NWIEGDQKYLWtaQLQNK 295
Cdd:PRK13640 256 EKGISVpqeiNTEEKLVQYLC--QLNSK 281
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
40-230 |
1.98e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG---MNPHKERekfaqtiGVVFGQRSQLWWdIAV 116
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvTGPGADR-------GVVFQKDALLPW-LNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:COG4525 94 LDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLAdiEAL---CERVVM 230
Cdd:COG4525 174 QELLLDVWQRTGKGVFLITHSVE--EALflaTRLVVM 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-245 |
3.04e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.20 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREK-FAQTIGVVf 104
Cdd:PRK11160 341 LNNVsFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAaLRQAISVV- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 GQRSQLWWDiAVQESFRLLKKvyKVSDEdynaHMEHVIQTLDIGPLL--DKPV--------RKLSLGQRMRCELAAALIH 174
Cdd:PRK11160 420 SQRVHLFSA-TLRDNLLLAAP--NASDE----ALIEVLQQVGLEKLLedDKGLnawlgeggRQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 175 NPPLLFLDEPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEALcERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-236 |
3.11e-22 |
|
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: 92.11 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFgqrsqlww 112
Cdd:cd03215 8 RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 diavqesfrllkkvykVSdEDYNAHmehviqtldiGPLLDKPVRK-------LSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:cd03215 80 ----------------VP-EDRKRE----------GLVLDLSVAEnialsslLSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
40-245 |
6.48e-22 |
|
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: 92.29 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVFgQRSQLWWDiAVQE 118
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVL-QDTFLFSG-TIME 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFRLLKKVYKvsDEDYN-----AHMEHVIQTLDIGplLDKPVRK----LSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:cd03254 96 NIRLGRPNAT--DEEVIeaakeAGAHDFIMKLPNG--YDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 190 VLVKLKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKL 245
Cdd:cd03254 172 TETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
44-230 |
6.84e-22 |
|
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: 91.79 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIgVVFGQRSQLWWDIAVQESFRLL 123
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL-LYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYkvSDEdynaHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEI 203
Cdd:cd03231 98 HADH--SDE----QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170 180
....*....|....*....|....*..
gi 504274718 204 NEKYNTTILLTTHDLADIEALCERVVM 230
Cdd:cd03231 172 CARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
32-240 |
9.28e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 92.59 E-value: 9.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN---------PHKEREKFAQTIGV 102
Cdd:TIGR02323 10 SKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqlSEAERRRLMRTEWG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 103 VFGQRSQLWWDIAVQESFRLLKKVYKVSDEDY-----NAH--MEHViqTLDIGPLLDKPvRKLSLGQRMRCELAAALIHN 175
Cdd:TIGR02323 90 FVHQNPRDGLRMRVSAGANIGERLMAIGARHYgniraTAQdwLEEV--EIDPTRIDDLP-RAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 176 PPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
39-241 |
1.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.87 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTS-----GDITVNGMNPHKEREKFAQTIGVVFGQRSQLWWD 113
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEgkvtvGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504274718 193 KLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK13643 180 RIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
28-241 |
1.47e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 28 RDLfTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKERekfaqTIGVV 103
Cdd:PRK11607 23 RNL-TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDlshvPPYQR-----PINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 FgQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:PRK11607 97 F-QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 184 PTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
2.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.11 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVnqlrkefkayssrsglkgafRDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:PRK13647 1 MDNIIEV--------------------EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNGMNPHKEREKFAQT-IGVVFGQ------RSQLWWDIAVQESFRLLKKvykvsdEDYNAHMEHVIQTLDIGPLLDK 153
Cdd:PRK13647 61 RVKVMGREVNAENEKWVRSkVGLVFQDpddqvfSSTVWDDVAFGPVNMGLDK------DEVERRVEEALKAVRMWDFRDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 154 PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDE 233
Cdd:PRK13647 135 PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKE 213
|
....*..
gi 504274718 234 GSIIYDG 240
Cdd:PRK13647 214 GRVLAEG 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
32-239 |
2.08e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.66 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDItVNGMNP-HKEREKfaqtIGVVFgqrsql 110
Cdd:PRK11247 19 SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPlAEARED----TRLMF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 wwdiavQESfRLL--KKVYKvsdedyNAHM-------EHVIQTLDIGPLLDK----PVrKLSLGQRMRCELAAALIHNPP 177
Cdd:PRK11247 88 ------QDA-RLLpwKKVID------NVGLglkgqwrDAALQALAAVGLADRanewPA-ALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 178 LLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYD 239
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
41-240 |
2.34e-21 |
|
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: 90.01 E-value: 2.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPT---SGDITVNGMNPHKEREKFAQTIgvvfgqrsqlwwdiavq 117
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEI----------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 esfrllkkVYkVSDEDYnaHMEH--VIQTLDIGPLL--DKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:cd03233 86 --------IY-VSEEDV--HFPTltVRETLDFALRCkgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 194 LKIRQFLKEINEKYNTTILLTTHDLAD-IEALCERVVMLDEGSIIYDG 240
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFVSLYQASDeIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-236 |
3.06e-21 |
|
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: 90.61 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 23 LKG--AFRDLfTRNYRVMKAVN---DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFA 97
Cdd:cd03248 8 LKGivKFQNV-TFAYPTRPDTLvlqDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 98 QTIGVVFGQRSQLWWDiAVQE--SFRLLKKVY-KVSDEDYNAHMEHVIQTLDIGPLLDKPVR--KLSLGQRMRCELAAAL 172
Cdd:cd03248 87 HSKVSLVGQEPVLFAR-SLQDniAYGLQSCSFeCVKEAAQKAHAHSFISELASGYDTEVGEKgsQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 173 IHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSI 236
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-241 |
5.78e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.62 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKaysSRSGLkgafrdlFTRNYrvMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG 80
Cdd:PRK15112 1 VETLLEVRNLSKTFR---YRTGW-------FRRQT--VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 DITVNGMNPHKEREKF-AQTIGVVFG---------QR-SQLwwdiaVQESFRLlkkvykVSDEDYNAHMEHVIQTL-DIG 148
Cdd:PRK15112 69 ELLIDDHPLHFGDYSYrSQRIRMIFQdpstslnprQRiSQI-----LDFPLRL------NTDLEPEQREKQIIETLrQVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 149 PLLDKPV---RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALC 225
Cdd:PRK15112 138 LLPDHASyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIS 217
|
250
....*....|....*.
gi 504274718 226 ERVVMLDEGSIIYDGS 241
Cdd:PRK15112 218 DQVLVMHQGEVVERGS 233
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
58-250 |
6.80e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.86 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 58 GENGAGKSTTIKMLTGILTPTSGDITVNG-----------MNPHKERekfaqtIGVVFgQRSQLWWDIAVQESFRllkkv 126
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaekgicLPPEKRR------IGYVF-QDARLFPHYKVRGNLR----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 127 YKVSDEDyNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEK 206
Cdd:PRK11144 99 YGMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504274718 207 YNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLrsnWG 250
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV---WA 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
41-236 |
9.02e-21 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 87.66 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVfgqrsqlwwdiavqes 119
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL---------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 frllkkvykvsdedynahMEHVIqtldigpLLDKPVRK--LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIR 197
Cdd:cd03246 82 ------------------PQDDE-------LFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 504274718 198 QFLKEINEKYNTTILLtTHDLADIEAlCERVVMLDEGSI 236
Cdd:cd03246 137 QAIAALKAAGATRIVI-AHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
40-245 |
1.08e-20 |
|
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: 89.08 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFAQTIGVVFgqRSQLWWDIAVQE 118
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDlALADPAWLRRQVGVVL--QENVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFRLLKKVYKVSDEDYNAHM---EHVIQTLDIG--PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:cd03252 95 NIALADPGMSMERVIEAAKLagaHDFISELPEGydTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 194 LKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKL 245
Cdd:cd03252 175 HAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
40-236 |
1.08e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.44 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT-----VNGMNPhKEREkfaqtIGVVFgQRSQLWWDI 114
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvVNELEP-ADRD-----IAMVF-QNYALYPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLD-KPvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDvlVK 193
Cdd:PRK11650 92 SVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDrKP-RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD--AK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504274718 194 LKI--RQFLKEINEKYNTTILLTTHDlaDIEA--LCERVVMLDEGSI 236
Cdd:PRK11650 169 LRVqmRLEIQRLHRRLKTTSLYVTHD--QVEAmtLADRVVVMNGGVA 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
41-292 |
1.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.15 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKERE-KFAQTIGVVFGQRSQLWWDIAVQES 119
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQF 199
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 200 LKEINEKYNTTILLTTHDLaDIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQVTFEFGTAPNkeqlklLTQGMPVNW 279
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDL-DEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDVPFSSN------LMKDLRKNG 255
|
250
....*....|...
gi 504274718 280 IEGDQKYLWTAQL 292
Cdd:PRK13642 256 FDLPEKYLSEDEL 268
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
39-233 |
1.62e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.02 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITvngmNPHKERekfaqtIGVVfgqRSQLWWDIAVQ- 117
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----RNGKLR------IGYV---PQKLYLDTTLPl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 --ESFRLLKKVYKVSDedynahMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLK 195
Cdd:PRK09544 85 tvNRFLRLRPGTKKED------ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 504274718 196 IRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDE 233
Cdd:PRK09544 159 LYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
44-236 |
1.81e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 88.30 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREK-----FAQTIGVVFgQRSQLWWDIAVQE 118
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraklRAKHVGFVF-QSFMLIPTLNALE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQ 198
Cdd:PRK10584 108 NVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*...
gi 504274718 199 FLKEINEKYNTTILLTTHDlADIEALCERVVMLDEGSI 236
Cdd:PRK10584 188 LLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-241 |
2.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM-----NPHKEREKFAQTIGVVFG-QRSQLwW 112
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitstSKNKDIKQIRKKVGLVFQfPESQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504274718 192 VKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK13649 180 GRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
38-250 |
2.36e-20 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 88.37 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 38 MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKEREKfaqtIGVVfGQRSQLwW 112
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdLNLRWLRSQ----IGLV-SQEPVL-F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DIAVQESFRLLKKVYKVSDED-----YNAHmeHVIQTLDIGplLDKPV----RKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:cd03249 90 DGTIAENIRYGKPDATDEEVEeaakkANIH--DFIMSLPDG--YDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 184 PTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKLRSNWG 250
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
27-254 |
2.41e-20 |
|
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: 88.06 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmnpHKEREKFAQT----IG 101
Cdd:cd03251 3 FKNVtFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDG---HDVRDYTLASlrrqIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 102 VVfGQRSQLWWDiAVQESFRllkkvYKVSDEDY--------NAHMEHVIQTLDIGplLDKPV----RKLSLGQRMRCELA 169
Cdd:cd03251 80 LV-SQDVFLFND-TVAENIA-----YGRPGATReeveeaarAANAHEFIMELPEG--YDTVIgergVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 170 AALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKLRSNW 249
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQG 227
|
....*
gi 504274718 250 GDLKQ 254
Cdd:cd03251 228 GVYAK 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-250 |
2.43e-20 |
|
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: 92.38 E-value: 2.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVfGQRSQLWWDIAVQES 119
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC-PQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQF 199
Cdd:TIGR01257 1024 ILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 200 LkeINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWG 250
Cdd:TIGR01257 1104 L--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFG 1152
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
39-234 |
2.78e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREK----FAQTIGVVFgQRSQLWWDI 114
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIF-QDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESFRLLKKVYKVSDEDYNahmEHVIQTLDIGPLLDK----PVrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIR---RRVSAALDKVGLLDKaknfPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504274718 191 LVKLKIRQFLKEINeKYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:PRK10908 171 ALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
35-240 |
3.86e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG------MNPH-KEREKFAQTIGVVFgQR 107
Cdd:PRK11124 12 YGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSdKAIRELRRNVGMVF-QQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 SQLWWDIAVQESfrLLK---KVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:PRK11124 91 YNLWPHLTVQQN--LIEapcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 185 TIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
28-230 |
4.12e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 89.25 E-value: 4.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 28 RDLfTRNYRV----------MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKER 93
Cdd:PRK11308 9 IDL-KKHYPVkrglfkperlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkaDPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 94 EKFAQTIGVVFgqrsqlwwdiavQESFRLL---KKVYKVSDEdynahmehviqTLDIGPLLDKPVRK------------- 157
Cdd:PRK11308 88 KLLRQKIQIVF------------QNPYGSLnprKKVGQILEE-----------PLLINTSLSAAERRekalammakvglr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 158 ----------LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCER 227
Cdd:PRK11308 145 pehydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADE 224
|
....
gi 504274718 228 V-VM 230
Cdd:PRK11308 225 VmVM 228
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-245 |
4.19e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 90.93 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMnPHKE------REKFAQT 99
Cdd:TIGR02203 333 FRNVtFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH-DLADytlaslRRQVALV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 100 igvvfGQRSQLWWD-IAVQESFRLLKKV--YKVSDEDYNAHMEHVIQTLDIGplLDKPV----RKLSLGQRMRCELAAAL 172
Cdd:TIGR02203 412 -----SQDVVLFNDtIANNIAYGRTEQAdrAEIERALAAAYAQDFVDKLPLG--LDTPIgengVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504274718 173 IHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKL 245
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNEL 554
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
44-254 |
1.01e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.90 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILtPTSGDITVNGMNPHK-EREKFAQTIGVVfGQRSQLwwdiaVQESFR- 121
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWV-GQNPQL-----PHGTLRd 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 122 --LLKKVyKVSDEDYNAHME--HVIQTLDIGPL-LDKPVRK----LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK11174 442 nvLLGNP-DASDEQLQQALEnaWVSEFLPLLPQgLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 193 KLKIRQFLKEINEkyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKLRSNWGDLKQ 254
Cdd:PRK11174 521 EQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGGLFAT 579
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-232 |
1.10e-19 |
|
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: 89.84 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 47 TVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDItvngmnphKEREKFA---QTIGVVFgqrsqlwwDIAVQEsfrLL 123
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLKISykpQYISPDY--------DGTVEE---FL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYKvsdEDYNAHM--EHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLK 201
Cdd:COG1245 423 RSANT---DDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|.
gi 504274718 202 EINEKYNTTILLTTHDLADIEALCERVVMLD 232
Cdd:COG1245 500 RFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
42-245 |
2.51e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGDITVNGMNPHKE----REKFAQTIGVVFGQ---RSQLw 111
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKemraISAYVQQDDLFIPTltvREHL- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 wdiAVQESFRLLKKVYKVSDEdynAHMEHVIQTLDIGPLLD------KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:TIGR00955 121 ---MFQAHLRMPRRVTKKEKR---ERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKyNTTILLTTHD-LADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-241 |
3.00e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.81 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 19 SRSGLKGafrDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFA 97
Cdd:PRK10253 4 SVARLRG---EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 98 QTIGVVfGQRSQLWWDIAVQE-------SFRLLKKVYKVSDEDynaHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAA 170
Cdd:PRK10253 81 RRIGLL-AQNATTPGDITVQElvargryPHQPLFTRWRKEDEE---AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 171 ALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
43-232 |
3.51e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.87 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFA---QTIGVVFgQRSQLWWDIAVQ 117
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpMSKLSSAAKAElrnQKLGFIY-QFHHLLPDFTAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIR 197
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIF 185
|
170 180 190
....*....|....*....|....*....|....*
gi 504274718 198 QFLKEINEKYNTTILLTTHDLADIEALCERVVMLD 232
Cdd:PRK11629 186 QLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRD 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-229 |
3.58e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 88.33 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 47 TVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNgmnphkerEKFA---QTIGVVFgqrsqlwwDIAVQEsfrLL 123
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE--------LKISykpQYIKPDY--------DGTVED---LL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYKVSDEDYnaHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEI 203
Cdd:PRK13409 422 RSITDDLGSSY--YKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180
....*....|....*....|....*.
gi 504274718 204 NEKYNTTILLTTHDLADIEALCERVV 229
Cdd:PRK13409 500 AEEREATALVVDHDIYMIDYISDRLM 525
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
44-241 |
3.81e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 85.28 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGDITVNGMN----PHKErekFAQtigvvfgQRSQLwwdiAVQES 119
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPlsdwSAAE---LAR-------HRAYL----SQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVY---------KVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLG--QRMRceLAAAL--IH---NPP--LLFL 181
Cdd:COG4138 80 PPFAMPVFqylalhqpaGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGewQRVR--LAAVLlqVWptiNPEgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 182 DEPTIGLDVLVKLKIRQFLKEINEKYNtTILLTTHDL------ADiealceRVVMLDEGSIIYDGS 241
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQQGI-TVVMSSHDLnhtlrhAD------RVWLLKQGKLVASGE 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-232 |
4.06e-19 |
|
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: 85.15 E-value: 4.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 47 TVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVngmnphkEREKFA---QTIGVVFgqrsqlwwDIAVQEsfrLL 123
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-------ELDTVSykpQYIKADY--------EGTVRD---LL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYKVSDEDYNAHMEhVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEI 203
Cdd:cd03237 83 SSITKDFYTHPYFKTE-IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRF 161
|
170 180
....*....|....*....|....*....
gi 504274718 204 NEKYNTTILLTTHDLADIEALCERVVMLD 232
Cdd:cd03237 162 AENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
57-241 |
4.22e-19 |
|
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: 86.39 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 57 IGENGAGKSTTIKMLTGILTPTSGDITVNGMN-----PHKerekfaQTIGVVFgQRSQLWWDIAVQESFRLLKKVYKVSD 131
Cdd:TIGR01187 2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDvtnvpPHL------RHINMVF-QSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 132 EDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTI 211
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180 190
....*....|....*....|....*....|
gi 504274718 212 LLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
44-223 |
4.73e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.56 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIgVVFGQRSQLWWDIAVQESFRLL 123
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI-LYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYkvSDEDYNAHmeHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEI 203
Cdd:TIGR01189 98 AAIH--GGAQRTIE--DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170 180
....*....|....*....|
gi 504274718 204 NEKYNTTILLTTHDLADIEA 223
Cdd:TIGR01189 174 LARGGIVLLTTHQDLGLVEA 193
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
41-248 |
5.02e-19 |
|
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: 87.88 E-value: 5.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVfGQRSQLWwDIAVQES 119
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYL-PQDVELF-DGTIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 F-RLLK----KVYKVSDEdynAHMEHVIQTL------DIGPLLdkpvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:COG4618 426 IaRFGDadpeKVVAAAKL---AGVHEMILRLpdgydtRIGEGG----ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 189 DVLVKLKIRQFLKEINEKyNTTILLTTHDLAdIEALCERVVMLDEGSIIYDGS----LQKLRSN 248
Cdd:COG4618 499 DDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPrdevLARLARP 560
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
39-248 |
7.52e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 85.27 E-value: 7.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPH---KEREKFAQTIGVVFG-QRSQLWW 112
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPEtgnKNLKKLRKKVSLVFQfPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DiAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK13641 101 N-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 192 VKLKIRQFLKEInEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK13641 180 GRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
39-236 |
1.01e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNP---H-KEREkfaqtIGVVFgQRSQLWWDI 114
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlHaRDRK-----VGFVF-QHYALFRHM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQE--SF--RLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK10851 90 TVFDniAFglTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504274718 191 LVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK10851 170 QVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
40-243 |
1.27e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 84.03 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREkFAQTIGVVFGQR------SQLW 111
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaITDDNFEK-LRKHIGIVFQNPdnqfvgSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAvqesFRLlkKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK13648 103 YDVA----FGL--ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504274718 192 VKLKIRQFLKEINEKYNTTILLTTHDLAdiEAL-CERVVMLDEGSIIYDGSLQ 243
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTPT 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-237 |
1.42e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTIGVV------- 103
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVpedrkge 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 --FGQRSqlwwdiaVQE-----SFRLLKKVYKVSDEDYNAHMEHVIQTLDI-GPLLDKPVRKLSLGQRMRCELAAALIHN 175
Cdd:COG1129 340 glVLDLS-------IREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 176 PPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
40-248 |
2.95e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 2.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM---NPHKEREkFAQTIGVVFGQRSQLWWDIAV 116
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQG-IRKLVGIVFQNPETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 197 RQFLKEINEKyNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK13644 176 LERIKKLHEK-GKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
41-241 |
3.39e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKER-EKFAQTIGVVfGQRSQLWWDIAVQE- 118
Cdd:COG4604 17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsRELAKRLAIL-RQENHINSRLTVREl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 -SF--------RLlkkvykvSDEDYnAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:COG4604 96 vAFgrfpyskgRL-------TAEDR-EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 190 VLVKLKIRQFLKEINEKYNTTILLTTHDL------ADiealceRVVMLDEGSIIYDGS 241
Cdd:COG4604 168 MKHSVQMMKLLRRLADELGKTVVIVLHDInfascyAD------HIVAMKDGRVVAQGT 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-245 |
4.02e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 85.12 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 28 RDL---FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTT----IKMLTGILTPTSGDITVNG--MNPHKEREKFA- 97
Cdd:COG4172 10 EDLsvaFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGqdLLGLSERELRRi 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 98 --QTIGVVFgqrsqlwwdiavQESFRLLKKVYKVSD---EDYNAHM--------EHVIQTLD-IGplLDKPVRK------ 157
Cdd:COG4172 90 rgNRIAMIF------------QEPMTSLNPLHTIGKqiaEVLRLHRglsgaaarARALELLErVG--IPDPERRldayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 158 -LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:COG4172 156 qLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
....*....
gi 504274718 237 IYDGSLQKL 245
Cdd:COG4172 236 VEQGPTAEL 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
41-236 |
4.28e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTI----------GVVFGqrs 108
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDGLANGIvyisedrkrdGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 qlwwdIAVQESFRLL------KKVYKVSDEDYNAHMEHVIQTLDI-GPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:PRK10762 345 -----MSVKENMSLTalryfsRAGGSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 182 DEPTIGLDVLVKLKIRQFlkeINE--KYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-247 |
4.70e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKS-TTIKMLTGILTP----TSGDITVNGMNPHKEREkfaQTIGVVFG 105
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASE---QTLRGVRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRsqlwwdIAV--QESFRLLKKVYKVSDEDYNAHMEH-----------VIQTLD-------IGPLLDKPvRKLSLGQRMR 165
Cdd:PRK15134 92 NK------IAMifQEPMVSLNPLHTLEKQLYEVLSLHrgmrreaargeILNCLDrvgirqaAKRLTDYP-HQLSGGERQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 166 CELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244
|
..
gi 504274718 246 RS 247
Cdd:PRK15134 245 FS 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
31-245 |
5.74e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTptsGDITVN------GMNPHKE-------REKFA 97
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT---GDKSAGshiellGRTVQREgrlardiRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 98 QTiGVVFGQ------------------------RSQLWWDIAVQESfRLLKKVYKVSdedyNAHMEHviqtldigplldK 153
Cdd:PRK09984 87 NT-GYIFQQfnlvnrlsvlenvligalgstpfwRTCFSWFTREQKQ-RALQALTRVG----MVHFAH------------Q 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 154 PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDE 233
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQ 228
|
250
....*....|..
gi 504274718 234 GSIIYDGSLQKL 245
Cdd:PRK09984 229 GHVFYDGSSQQF 240
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
39-241 |
7.12e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 81.51 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVfGQRSQLWWD-IAv 116
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV-PQDTVLFNDtIG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 qesfrllkkvYKVSDEDYNAHMEHVIQTLDIGPLLDKPVR--------------KLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:cd03253 93 ----------YNIRYGRPDATDEEVIEAAKAAQIHDKIMRfpdgydtivgerglKLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 183 EPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIeALCERVVMLDEGSIIYDGS 241
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGT 218
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
41-236 |
1.21e-17 |
|
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: 83.55 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-EREKFAQTIGVVfGQRSQLW-----WDI 114
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHIGYL-PQDVELFpgtvaENI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESFRLLKKVY---KVSDedynAHmeHVIQTL------DIGPlldkPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:TIGR01842 413 ARFGENADPEKIIeaaKLAG----VH--ELILRLpdgydtVIGP----GGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKYNTTILLtTHDLADIEALcERVVMLDEGSI 236
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKARGITVVVI-THRPSLLGCV-DKILVLQDGRI 531
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
40-234 |
1.84e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM---NPHKERekfaqtiGVVFGQRSQLWWDiAV 116
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpveGPGAER-------GVVFQNEGLLPWR-NV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
42-236 |
2.07e-17 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 79.68 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPH----KEREKFAQTIGVVFGQRSQLWWDIA-- 115
Cdd:TIGR02982 22 FDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHgaskKQLVQLRRRIGYIFQAHNLLGFLTArq 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 116 -VQESFRLLKKVykvSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKL 194
Cdd:TIGR02982 102 nVQMALELQPNL---SYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504274718 195 KIRQFLKEINEKYNTTILLTTHDlADIEALCERVVMLDEGSI 236
Cdd:TIGR02982 179 DVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-260 |
2.43e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.76 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDL-FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKE-----REKFAqti 100
Cdd:PRK11176 344 FRNVtFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYtlaslRNQVA--- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 101 gvVFGQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHV---IQTLDIGplLDKPVRK----LSLGQRMRCELAAALI 173
Cdd:PRK11176 421 --LVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAmdfINKMDNG--LDTVIGEngvlLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 174 HNPPLLFLDEPTIGLDVLVKLKIRQFLKEIneKYNTTILLTTHDLADIEALCERVVmLDEGSIIYDGSLQKLRSNWGDLK 253
Cdd:PRK11176 497 RDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEILV-VEDGEIVERGTHAELLAQNGVYA 573
|
....*...
gi 504274718 254 QV-TFEFG 260
Cdd:PRK11176 574 QLhKMQFG 581
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
40-241 |
2.68e-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: 79.46 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-----PHKEREKFAqTI--------GVV--- 103
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskigLHDLRSRIS-IIpqdpvlfsGTIrsn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 ---FGQRS--QLWwdiavqesfRLLKKVykvsdedynaHMEHVIQTLDIGplLDKPV----RKLSLGQRMRCELAAALIH 174
Cdd:cd03244 98 ldpFGEYSdeELW---------QALERV----------GLKEFVESLPGG--LDTVVeeggENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 175 NPPLLFLDEPTIGLDVLVKLKIRQFLKEinEKYNTTILLTTHDLADIeALCERVVMLDEGSIIYDGS 241
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTI-IDSDRILVLDKGRVVEFDS 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
42-244 |
2.75e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 83.23 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGDITVNGmnpHKEREKFAQTIGVVFGQrsqlwwDI---- 114
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNG---RPLDSSFQRSIGYVQQQ------DLhlpt 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 -AVQESFRL---LKKVYKVSDEDYNAHMEHVIQTLDIGPLLDK----PVRKLSLGQRMRCELAAALIHNPPLL-FLDEPT 185
Cdd:TIGR00956 851 sTVRESLRFsayLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLlFLDEPT 930
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 186 IGLDVLVKLKIRQFLKEInEKYNTTILLTTHD-LADIEALCERVVMLDEGS-IIYDGSLQK 244
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKL-ADHGQAILCTIHQpSAILFEEFDRLLLLQKGGqTVYFGDLGE 990
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
44-241 |
2.76e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.98 E-value: 2.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGDITVNGMN----PHKE----REKFAQTIGVVFGQRSQLWWDIA 115
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPleawSAAElarhRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 116 VQESFRLlkkvykvsdEDYNAHMEHVIQTLDIGPLLDKPVRKLSLG--QRMRceLAAAL--IH---NP--PLLFLDEPTI 186
Cdd:PRK03695 94 QPDKTRT---------EAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVR--LAAVVlqVWpdiNPagQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 187 GLDVLVKLKIRQFLKEINEKyNTTILLTTHDL------ADiealceRVVMLDEGSIIYDGS 241
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLnhtlrhAD------RVWLLKQGKLLASGR 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-241 |
2.85e-17 |
|
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: 82.54 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGI--LTPTSGDITVN-GMNP---HKEREKFAQTIGVVFG 105
Cdd:TIGR03269 7 TKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvALCEkcgYVERPSKVGEPCPVCG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSQL----WWDIAVQESFRLLKKV-------YKVSDEDynAHMEHVIQTL-DIGPLLDKPV------------------ 155
Cdd:TIGR03269 87 GTLEPeevdFWNLSDKLRRRIRKRIaimlqrtFALYGDD--TVLDNVLEALeEIGYEGKEAVgravdliemvqlshrith 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 156 --RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDE 233
Cdd:TIGR03269 165 iaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
....*...
gi 504274718 234 GSIIYDGS 241
Cdd:TIGR03269 245 GEIKEEGT 252
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
40-240 |
3.34e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMnphKEREKFAQTIGVVFGQRSQLWW------- 112
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ---PTRQALQKNLVAYVPQSEEVDWsfpvlve 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DIAVQESFRLLKKVYKVSDEDyNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:PRK15056 99 DVVMMGRYGHMGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 193 KLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLdEGSIIYDG 240
Cdd:PRK15056 178 EARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASG 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-240 |
3.80e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 28 RDLfTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT----------VNGMnPHKEREKFA 97
Cdd:PRK11701 10 RGL-TKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqlrdLYAL-SEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 98 QT-IGVVF-----GQRSQLWWDIAVQEsfRLLKkvykVSDEDYN---AHMEHVIQTLDIGPL-LDKPVRKLSLGQRMRCE 167
Cdd:PRK11701 88 RTeWGFVHqhprdGLRMQVSAGGNIGE--RLMA----VGARHYGdirATAGDWLERVEIDAArIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504274718 168 LAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
34-225 |
4.03e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 78.45 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 34 NYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVfGQRSQLWWD 113
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFV-GHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFrllkkVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVK 193
Cdd:PRK13540 89 LTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 504274718 194 LKIRQFLKEiNEKYNTTILLTTH-DL----ADIEALC 225
Cdd:PRK13540 164 LTIITKIQE-HRAKGGAVLLTSHqDLplnkADYEEYH 199
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
47-238 |
4.67e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.78 E-value: 4.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 47 TVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNgmnPHKER--EKFAQTigvvfgqrsqlwwdiAVQESFRLLK 124
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEE---PSWDEvlKRFRGT---------------ELQNYFKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 125 -----------------KVYK--VSDE----DYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:PRK13409 157 ngeikvvhkpqyvdlipKVFKgkVRELlkkvDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 182 DEPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIEALCERVVmldegsIIY 238
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVH------IAY 285
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
47-219 |
5.37e-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: 81.75 E-value: 5.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 47 TVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDItvnGMNPHKER--EKFAQTigvvfgqrsqlwwdiAVQESFR--- 121
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEvlKRFRGT---------------ELQDYFKkla 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 122 --------------LLKKVYK--VSD--EDYNAH--MEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:COG1245 157 ngeikvahkpqyvdLIPKVFKgtVREllEKVDERgkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*...
gi 504274718 182 DEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLA 219
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLA 273
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-275 |
6.58e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 81.48 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKAYSSRSGlkgAFRDLF--TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPT 78
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMYNKPFD---KLKDLFfrSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 79 SGDITVNGMnphkerekfAQTIGVVFGQRSQLwwdiAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKL 158
Cdd:PRK13545 78 KGTVDIKGS---------AALIAISSGLNGQL----TGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 159 SLGQRMRCELAAALIHNPPLLFLDEptiGLDVLVKLKIRQFLKEINE--KYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK13545 145 SSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNEfkEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 504274718 237 IYDGSLQKLRSNWGDL----KQVTFEFGTAPNKEQLKLLTQGM 275
Cdd:PRK13545 222 KEYGDIKEVVDHYDEFlkkyNQMSVEERKDFREEQISQFQHGL 264
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
31-250 |
7.46e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.16 E-value: 7.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTiKMLTGILTPTSGDITVNGMNPHKEREKFAQTIG----VVFGQ 106
Cdd:NF000106 19 LVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hrpVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 107 RSQLwwdiAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:NF000106 98 RESF----SGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 187 GLDVLVKLKIRQFLKEInEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWG 250
Cdd:NF000106 174 GLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-269 |
8.67e-17 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 81.69 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 20 RSGLKGAFRDLFTRNYRVMKAVNDIsftVKQGEMVGYIGENGAGKSTTIKMLT----GILTPTSGDITVNGMNPHkEREK 95
Cdd:TIGR00956 59 TRGFRKLKKFRDTKTFDILKPMDGL---IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPE-EIKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 96 FAQTIGVVFGQRSQLWWDIAVQESFRLLKK-------VYKVSDEDYNAHMEHVIQT---LDI------GpllDKPVRKLS 159
Cdd:TIGR00956 135 HYRGDVVYNAETDVHFPHLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVYMAtygLSHtrntkvG---NDFVRGVS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 160 LGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLA-DIEALCERVVMLDEGSIIY 238
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSqDAYELFDKVIVLYEGYQIY 291
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504274718 239 DGSLQKLRSNWGDL------KQVTFEFGTA---PNKEQLK 269
Cdd:TIGR00956 292 FGPADKAKQYFEKMgfkcpdRQTTADFLTSltsPAERQIK 331
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
43-216 |
9.59e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQT---IGVVFGQRSQLwwdiAVQES 119
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllyLGHQPGIKTEL----TALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 FRLLKKVYKVSDEDynaHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL-VKLKIRQ 198
Cdd:PRK13538 95 LRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQgVARLEAL 171
|
170
....*....|....*...
gi 504274718 199 FLKEINEkyNTTILLTTH 216
Cdd:PRK13538 172 LAQHAEQ--GGMVILTTH 187
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-248 |
1.02e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.46 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKAYSSRSGL---KGAFRDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP 77
Cdd:PRK10070 1 MAIKLEIKNLYKIFGEHPQRAFKyieQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 78 TSGDITVNGMNPHK-----EREKFAQTIGVVFgQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLD 152
Cdd:PRK10070 81 TRGQVLIDGVDIAKisdaeLREVRRKKIAMVF-QSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 153 KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLD 232
Cdd:PRK10070 160 SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQ 239
|
250
....*....|....*.
gi 504274718 233 EGSIIYDGSLQKLRSN 248
Cdd:PRK10070 240 NGEVVQVGTPDEILNN 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-237 |
1.07e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 80.74 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILtPT---SGDITVNGmnphkeREKFAQTIG------- 101
Cdd:PRK13549 12 TKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEG------EELQASNIRdteragi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 102 VVFGQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAhMEHVIQTL------DIGPllDKPVRKLSLGQRMRCELAAALIHN 175
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGGIMDYDA-MYLRAQKLlaqlklDINP--ATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 176 PPLLFLDEPTIGL---DVLVKLKIRQFLKeineKYNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:PRK13549 162 ARLLILDEPTASLtesETAVLLDIIRDLK----AHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
31-245 |
1.08e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMnphKEREKFAQTIGVVFGQRSQL 110
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM---LLRRRSRQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 W----WDIAV--QESFRLLKKVYKVSD---EDYNAH--------------MEHVIQTLDIGPLLDKPVRKLSLGQRMRCE 167
Cdd:PRK10261 99 RhvrgADMAMifQEPMTSLNPVFTVGEqiaESIRLHqgasreeamveakrMLDQVRIPEAQTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 168 LAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
36-248 |
1.36e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 36 RVMKAvndISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGV-VFGQRSQLWWDI 114
Cdd:PRK15439 25 EVLKG---IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIyLVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQES--FRLLKKvykvsdEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL---- 188
Cdd:PRK15439 102 SVKENilFGLPKR------QASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLtpae 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 189 -DVLVKlKIRQFLKEinekyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK15439 176 tERLFS-RIRELLAQ-----GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
38-241 |
1.79e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.74 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 38 MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM--NPH---------------KEREKFAQTI 100
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyiGDKknnhelitnpyskkiKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 101 GVVFG-QRSQLWWDiAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIG-PLLDKPVRKLSLGQRMRCELAAALIHNPPL 178
Cdd:PRK13631 119 SMVFQfPEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504274718 179 LFLDEPTIGLDVLVKLKIRQFLKEiNEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
27-248 |
2.49e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.06 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDLfTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN---PHKEREKFAQTIGVV 103
Cdd:PRK09493 4 FKNV-SKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndPKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 FgQRSQLWWDIAVQESFRL-LKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:PRK09493 83 F-QQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 183 EPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
44-239 |
2.68e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 79.46 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHkEREKFAQTIGVVFGQrsqlwwdiavqesFR 121
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpVTAD-NREAYRQLFSAVFSD-------------FH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 122 LLKKVYKVSDEDYNAHMEHVIQTLDigplLDKPVR---------KLSLGQRMRCELAAALIHNPPLLFLDE------PTi 186
Cdd:COG4615 417 LFDRLLGLDGEADPARARELLERLE----LDHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPE- 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 187 gldvlvklkIRQF--------LKEINeKyntTILLTTHD-----LADiealceRVVMLDEGSIIYD 239
Cdd:COG4615 492 ---------FRRVfytellpeLKARG-K---TVIAISHDdryfdLAD------RVLKMDYGKLVEL 538
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
39-240 |
2.85e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILT-P---TSGDITVNGMNPHKEREKfaqtigvvfgQRSQL-WWD 113
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEK----------ERRNLvGAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAV--QESFRLLKKVYKVS---DEDYNAHM--------EHVIQTL------DIGPLLDKPVRKLSLGQRMRCELAAALIH 174
Cdd:PRK11022 91 VAMifQDPMTSLNPCYTVGfqiMEAIKVHQggnkktrrQRAIDLLnqvgipDPASRLDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 175 NPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDG 240
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
39-258 |
3.84e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVN------GMNPHKEREKFAQTIGVVFG-QRSQLW 111
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQfPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQE-SFRLLKKvykvsDEDYNAHMEHVIQTLDIGPLLDKPVRK----LSLGQRMRCELAAALIHNPPLLFLDEPTI 186
Cdd:PRK13645 105 QETIEKDiAFGPVNL-----GENKQEAYKKVPELLKLVQLPEDYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 187 GLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSNWGDLKQVTFE 258
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEID 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
44-245 |
4.06e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREK-FAQTIGVVFGQRSQlwwdiAVQESFRL 122
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLPQQLPA-----AEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 123 LKKV-----------YKVSDEDynaHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:PRK10575 105 LVAIgrypwhgalgrFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504274718 192 VKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
38-248 |
5.01e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.64 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 38 MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTS---------GDITVNGMNPHKEREKFAQTIGVVFGQRS 108
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWhvtadrfrwNGIDLLKLSPRERRKIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 -----------QL------------WWDIAVQESFRLLKKVYKVSDEDYNAHME---HviqtldigplldkpvrKLSLGQ 162
Cdd:COG4170 100 scldpsakigdQLieaipswtfkgkWWQRFKWRKKRAIELLHRVGIKDHKDIMNsypH----------------ELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 163 RMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSL 242
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPT 243
|
....*.
gi 504274718 243 QKLRSN 248
Cdd:COG4170 244 EQILKS 249
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
43-190 |
5.28e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEReKFAQTigVVFGQRSQLWWDIAVQESFRL 122
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD-VAEAC--HYLGHRNAMKPALTVAENLEF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 123 LKKVYKvsdeDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK13539 97 WAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
42-234 |
5.35e-16 |
|
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: 74.97 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKML-----TGILTptsGDITVNGmnpHKEREKFAQTIGVVfgqrsqlwwdiav 116
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILING---RPLDKNFQRSTGYV------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 qESFRLLKKVYKVsdedynahmehvIQTLDIGPLLdkpvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:cd03232 85 -EQQDVHSPNLTV------------REALRFSALL----RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 504274718 197 RQFLKEINEKyNTTILLTTHD-LADIEALCERVVMLDEG 234
Cdd:cd03232 148 VRFLKKLADS-GQAILCTIHQpSASIFEKFDRLLLLKRG 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-236 |
1.09e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 75.62 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 1 MKNAIEVNQLRKEFKAYSSRsglKGAFRDLFTRNYR--VMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPT 78
Cdd:PRK13546 1 MNVSVNIKNVTKEYRIYRTN---KERMKDALIPKHKnkTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 79 SGDITVNGMnphkerekfAQTIGVVFGQRSQLwwdIAVQE-SFRLLKKVYKvsDEDYNAHMEHVIQTLDIGPLLDKPVRK 157
Cdd:PRK13546 78 VGKVDRNGE---------VSVIAISAGLSGQL---TGIENiEFKMLCMGFK--RKEIKAMTPKIIEFSELGEFIYQPVKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 158 LSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK13546 144 YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
32-241 |
1.37e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.91 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN----PHKEREkfaqtIGVVFgQR 107
Cdd:PRK09452 21 SKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDithvPAENRH-----VNTVF-QS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 SQLWWDIAVQE--SFRLlkKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK09452 95 YALFPHMTVFEnvAFGL--RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
43-262 |
1.40e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVF----GQRSQLWWDIAV-- 116
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYlpedRQSSGLYLDAPLaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 --------QESFRLLKKVYKVSDEDYNAHMEhvIQTLDIgpllDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK15439 361 nvcalthnRRGFWIKPARENAVLERYRRALN--IKFNHA----EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 189 DVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIiyDGSLQKLRSNWGDLKQVTFEFGTA 262
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI--SGALTGAAINVDTIMRLAFGEHQA 505
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
26-241 |
1.65e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 75.43 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 26 AFRDLFTRnYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFA--QTIGV 102
Cdd:PRK13638 3 ATSDLWFR-YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPlDYSKRGLLAlrQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 103 VFGQRSQ--LWWDIAVQESFRLlkKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:PRK13638 82 VFQDPEQqiFYTDIDSDIAFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 181 LDEPTIGLDVLVKLKIRQFLKEINEKYNtTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-248 |
2.76e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.40 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 3 NAIEVNQLRKEFKAyssRSGLKGafrdlftrnyrvmkavndISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG-- 80
Cdd:PRK11264 2 SAIEVKNLVKKFHG---QTVLHG------------------IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGti 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 81 ---DITVNGMNPHKERE----KFAQTIGVVFgQRSQLWWDIAVQESF----RLLKKVYKvsdEDYNAHMEHVIQTLDIGP 149
Cdd:PRK11264 61 rvgDITIDTARSLSQQKglirQLRQHVGFVF-QNFNLFPHRTVLENIiegpVIVKGEPK---EEATARARELLAKVGLAG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 150 LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD------VLVklKIRQFLKEinekyNTTILLTTHDLADIEA 223
Cdd:PRK11264 137 KETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgeVLN--TIRQLAQE-----KRTMVIVTHEMSFARD 209
|
250 260
....*....|....*....|....*
gi 504274718 224 LCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK11264 210 VADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
39-237 |
2.85e-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: 73.60 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNP-----HKEREK----------FAQTIgvv 103
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIstiplEDLRSSltiipqdptlFSGTI--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 fgqRSQLwwDIAVQESFRLLKKVYKVSDEDYNahmehviqtldigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:cd03369 99 ---RSNL--DPFDEYSDEEIYGALRVSEGGLN----------------------LSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504274718 184 PTIGLDVLVKLKIRQFLKEinEKYNTTILLTTHDLADIeALCERVVMLDEGSII 237
Cdd:cd03369 152 ATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTI-IDYDKILVMDAGEVK 202
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
41-233 |
3.39e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.28 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP---TSGDITVNG-----MNPHKERekfaqtIGVVFgQRSQLW- 111
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltaLPAEQRR------IGILF-QDDLLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 -WDIAVQESFRLLKKVYKvsdedyNAHMEHVIQTLD---IGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:COG4136 90 hLSVGENLAFALPPTIGR------AQRRARVEQALEeagLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504274718 188 LDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEAlCERVVMLDE 233
Cdd:COG4136 164 LDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLGN 208
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
41-245 |
6.02e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.58 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP----TSGDITVNGM--NPHKEREKFAQTI--------GVVFGQ 106
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKpvAPCALRGRKIATImqnprsafNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 107 RSQlwwdiaVQESFRLLKKvykvsdEDYNAHMEHVIQtlDIGplLDKPVRKLSL-------G--QRMRceLAAALIHNPP 177
Cdd:PRK10418 99 HTH------ARETCLALGK------PADDATLTAALE--AVG--LENAARVLKLypfemsgGmlQRMM--IALALLCEAP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 178 LLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
47-219 |
7.84e-15 |
|
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: 73.17 E-value: 7.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 47 TVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDitvngmnpHKEREKFAQTIGVVFGQRSQLWWDIAVQESFRLLKKV 126
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 127 Y-----------KVSD----EDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVL 191
Cdd:cd03236 94 QyvdlipkavkgKVGEllkkKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*...
gi 504274718 192 VKLKIRQFLKEINEKYNtTILLTTHDLA 219
Cdd:cd03236 174 QRLNAARLIRELAEDDN-YVLVVEHDLA 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
42-235 |
1.09e-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: 71.73 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGmnphkereKFA---Q-------TI--GVVFGQRsq 109
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAyvsQepwiqngTIreNILFGKP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 lwWDIavqesfRLLKKVYKVS--DEDYNAhMEHVIQTlDIGpllDKPVrKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:cd03250 92 --FDE------ERYEKVIKACalEPDLEI-LPDGDLT-EIG---EKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504274718 188 LDV-----LVKLKIRQFLKEinekyNTTILLTTHDLADIEAlCERVVMLDEGS 235
Cdd:cd03250 158 VDAhvgrhIFENCILGLLLN-----NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-246 |
2.19e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTI------------ 100
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGgdMADARHRRAVCPRIaympqglgknly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 101 ------------GVVFGQ-RSQLWWDIAvqesfRLLKKvykvsdedynahmehviqT-LDigPLLDKPVRKLSLGQRMRC 166
Cdd:NF033858 91 ptlsvfenldffGRLFGQdAAERRRRID-----ELLRA------------------TgLA--PFADRPAGKLSGGMKQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 167 ELAAALIHNPPLLFLDEPTIGLDVLVKlkiRQFLKEIN----EKYNTTILLTThdlADIE--ALCERVVMLDEGSIIYDG 240
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSR---RQFWELIDriraERPGMSVLVAT---AYMEeaERFDWLVAMDAGRVLATG 219
|
....*.
gi 504274718 241 SLQKLR 246
Cdd:NF033858 220 TPAELL 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-234 |
2.78e-14 |
|
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: 73.32 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILT--PTSGDITVNG--MNPHKEREKFAQTIgVVFGQR 107
Cdd:TIGR02633 8 VKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGspLKASNIRDTERAGI-VIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 SQLWWDIAVQESFRLLKKV-YKVSDEDYNAhMEHVIQTL------DIGPlLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:TIGR02633 87 LTLVPELSVAENIFLGNEItLPGGRMAYNA-MYLRAKNLlrelqlDADN-VTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 181 LDEPTIGL---DVLVKLKIRQFLKeineKYNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:TIGR02633 165 LDEPSSSLtekETEILLDIIRDLK----AHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
29-241 |
3.54e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 29 DLFTRNYRVMkavNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPT--------SGDITVNGMNPHKEREKFAQTI 100
Cdd:PRK13547 8 HVARRHRAIL---RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 101 GVVFGQRSQLWWDIAVQEsFRLLKKVYKVSDEDYNAHME-----HVIQTLDIGPLLDKPVRKLSLGQRMRCELAAAL--- 172
Cdd:PRK13547 85 RAVLPQAAQPAFAFSARE-IVLLGRYPHARRAGALTHRDgeiawQALALAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 173 ------IHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHD--LADIEAlcERVVMLDEGSIIYDGS 241
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDpnLAARHA--DRIAMLADGAIVAHGA 238
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
31-248 |
3.81e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMkaVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-PHKEREKFAQT---IGVVFgQ 106
Cdd:PRK11831 15 FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENiPAMSRSRLYTVrkrMSMLF-Q 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 107 RSQLWWDIAVQE--SFRLlkkvykvsdEDYNAHMEHVIQTLDIGPLLDKPVR--------KLSLGQRMRCELAAALIHNP 176
Cdd:PRK11831 92 SGALFTDMNVFDnvAYPL---------REHTQLPAPLLHSTVMMKLEAVGLRgaaklmpsELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 177 PLLFLDEPTIGLD-----VLVKLkirqfLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK11831 163 DLIMFDEPFVGQDpitmgVLVKL-----ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-235 |
5.90e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGiltptsgditvngmnphkeREKFAQTIGVVFGQRSQLW 111
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-------------------ALKGTPVAGCVDVPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESFrllkkvykVSDEDYNAHMEhVIQTLDIG--PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:COG2401 98 REASLIDAI--------GRKGDFKDAVE-LLNAVGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 190 VL----VKLKIRQFLKEInekyNTTILLTTHDLADIEALC-ERVVMLDEGS 235
Cdd:COG2401 169 RQtakrVARNLQKLARRA----GITLVVATHHYDVIDDLQpDLLIFVGYGG 215
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-230 |
7.23e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.28 E-value: 7.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKEFKAYSSRSglkgafrdLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:PRK15079 9 LEVADLKVHFDIKDGKQ--------WFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 NG-----MNPHKEREKFAQ----------------TIGvvfgqrsqlwwDIaVQESFRLLKKvyKVSDEDYNAHMEHVIQ 143
Cdd:PRK15079 81 LGkdllgMKDDEWRAVRSDiqmifqdplaslnprmTIG-----------EI-IAEPLRTYHP--KLSRQEVKDRVKAMML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 144 TLDIGP-LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIE 222
Cdd:PRK15079 147 KVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK 226
|
....*....
gi 504274718 223 ALCERV-VM 230
Cdd:PRK15079 227 HISDRVlVM 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
39-236 |
7.45e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.12 E-value: 7.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTIGVVFGQRSQ------- 109
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdISPRSPLDAVKKGMAYITESRRDngffpnf 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 -LWWDIAVQESFRLLKkvYKVSDEDYNAHMEHVIQTLDIGPL------LDKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:PRK09700 357 sIAQNMAISRSLKDGG--YKGAMGLFHEVDEQRTAENQRELLalkchsVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504274718 183 EPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
39-239 |
8.96e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.06 E-value: 8.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN---------PHKEREKFaqtiGVVFgQRSQ 109
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldadalAQLRREHF----GFIF-QRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 LWWDIAVQESFRlLKKVYK-VSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK10535 97 LLSHLTAAQNVE-VPAVYAgLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 189 DVLVKLKIRQFLKEINEKYNTTILLtTHDlADIEALCERVVMLDEGSIIYD 239
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDRGHTVIIV-THD-PQVAAQAERVIEIRDGEIVRN 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-244 |
1.13e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.91 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 46 FTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG------DITVNGM--NPHKEREkfaqtiGVVFG------------ 105
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGriiyeqDLIVARLqqDPPRNVE------GTVYDfvaegieeqaey 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 --QRSQLWWDIAVQESFRLLKKVYKVSD--EDYNA-HME----HVIQTLDIGPllDKPVRKLSLGQRMRCELAAALIHNP 176
Cdd:PRK11147 98 lkRYHDISHLVETDPSEKNLNELAKLQEqlDHHNLwQLEnrinEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 177 PLLFLDEPTIGLDVLVKLKIRQFLKEinekYNTTILLTTHDLADIEALCERVVMLDEGSII-YDGSLQK 244
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMATRIVDLDRGKLVsYPGNYDQ 240
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
42-236 |
1.76e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.10 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTI----------GVVFGQRSQ 109
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGImlcpedrkaeGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 LWWDIAVQESFRLLKKVYKVSDEDYNAhmEHVIQTLDI-GPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEAENA--DRFIRSLNIkTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 189 DVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK11288 428 DVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
48-232 |
2.36e-13 |
|
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: 67.21 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 48 VKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPhkerekfaqtigvvfgqrsqlwwdiavqesfrllkkVY 127
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP------------------------------------VY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 128 KVsdedynahmehviQTLDigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKY 207
Cdd:cd03222 66 KP-------------QYID-----------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....*
gi 504274718 208 NTTILLTTHDLADIEALCERVVMLD 232
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-254 |
2.53e-13 |
|
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: 70.73 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVN-------DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG------DITVnGMNPHKEREKFAQTI- 100
Cdd:TIGR03719 8 NRVSKVVPpkkeilkDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpGIKV-GYLPQEPQLDPTKTVr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 101 GVVFgqrsqlwwdIAVQESFRLLKKVYKVS------DEDYN------AHMEHVIQT---------LDIG------PLLDK 153
Cdd:TIGR03719 87 ENVE---------EGVAEIKDALDRFNEISakyaepDADFDklaaeqAELQEIIDAadawdldsqLEIAmdalrcPPWDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 154 PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEinekYNTTILLTTHDLADIEALCERVVMLDE 233
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE----YPGTVVAVTHDRYFLDNVAGWILELDR 233
|
250 260
....*....|....*....|..
gi 504274718 234 G-SIIYDGSLqklrSNWGDLKQ 254
Cdd:TIGR03719 234 GrGIPWEGNY----SSWLEQKQ 251
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-217 |
3.32e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 18 SSRSGlKGAFrDLFTRNYRV--MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVngmNPHKEREK 95
Cdd:PRK11147 312 ASRSG-KIVF-EMENVNYQIdgKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC---GTKLEVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 96 FAQtigvvfgQRSQLWWDIAVQESFRLLKKVYKVsdedyNAHMEHViqtldIGPLLD---------KPVRKLSLGQRMRC 166
Cdd:PRK11147 387 FDQ-------HRAELDPEKTVMDNLAEGKQEVMV-----NGRPRHV-----LGYLQDflfhpkramTPVKALSGGERNRL 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 167 ELAAALIHNPPLLFLDEPTIGLDVlvklKIRQFLKEINEKYNTTILLTTHD 217
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
39-236 |
3.42e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.24 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPT-SGDITVNG--MNPHKEREKFAQTIGVVFGQRSQ--LWWD 113
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQAIRAGIAMVPEDRKRhgIVPI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFRL--LKKVYKVSDEDYNAHMEHV---IQTLDI---GPLLdkPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:TIGR02633 354 LGVGKNITLsvLKSFCFKMRIDAAAELQIIgsaIQRLKVktaSPFL--PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
40-183 |
9.67e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.85 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKE-REKFAQTIGVVF----------GQRS 108
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFSAVFtdfhlfdqllGPEG 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 109 QLWWDIAVQESFRLLKKVYKVSDEDynahmeHVIQTLdigplldkpvrKLSLGQRMRCELAAALIHNPPLLFLDE 183
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLELED------GRISNL-----------KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
43-272 |
9.70e-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: 69.17 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTpTSGDITVNGMN-----PHKEREKFA---QTIGVVFGQ-RSQL--- 110
Cdd:TIGR01271 1237 DLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSwnsvtLQTWRKAFGvipQKVFIFSGTfRKNLdpy 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 --WWDiavqesfrllKKVYKVSDE-DYNAHMEHVIQTLDIgpLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:TIGR01271 1316 eqWSD----------EEIWKVAEEvGLKSVIEQFPDKLDF--VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 188 LDVLVKLKIRQFLKEINEkyNTTILLTTHdlaDIEAL--CERVVMLDEGSIIYDGSLQKLRSNWGDLKQVtfeFGTApnk 265
Cdd:TIGR01271 1384 LDPVTLQIIRKTLKQSFS--NCTVILSEH---RVEALleCQQFLVIEGSSVKQYDSIQKLLNETSLFKQA---MSAA--- 1452
|
....*..
gi 504274718 266 EQLKLLT 272
Cdd:TIGR01271 1453 DRLKLFP 1459
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
35-237 |
1.07e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.11 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLT--GILTP---TSGDITVNGMN---PHKEREKFAQTIGVVFGQ 106
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNiysPRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 107 RSQLWWDIAVQESFRLlkKVYKVSDEdynAHMEHVIQTLDIGPLLDKPVRK--------LSLGQRMRCELAAALIHNPPL 178
Cdd:PRK14239 95 PNPFPMSIYENVVYGL--RLKGIKDK---QVLDEAVEKSLKGASIWDEVKDrlhdsalgLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 179 LFLDEPTIGLDVLVKLKIRQFLKEINEKYntTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
38-231 |
1.22e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.52 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 38 MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGIlTPTSGDITVNGM----------NPHKEREKFAQTIGVVFGQR 107
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMrfddidllrlSPRERRKLVGHNVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 S-----------QL------------WWDIAVQESFRLLKKVYKVSDEDYNAHMEHViqtldigPLldkpvrKLSLGQRM 164
Cdd:PRK15093 99 QscldpservgrQLmqnipgwtykgrWWQRFGWRKRRAIELLHRVGIKDHKDAMRSF-------PY------ELTEGECQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 165 RCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVML 231
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-237 |
1.36e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 9 QLRKEFKAYSSRSGLkgafrdlFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN 88
Cdd:PRK10261 315 QVRNLVTRFPLRSGL-------LNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 89 ----PHKEREKFAQTIGVVFGQ-------RSQLWWDIavQESFRllkkVYKVSDEDynAHMEHVIQTLD-IGPLLDKPVR 156
Cdd:PRK10261 388 idtlSPGKLQALRRDIQFIFQDpyasldpRQTVGDSI--MEPLR----VHGLLPGK--AAAARVAWLLErVGLLPEHAWR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 157 ---KLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDE 233
Cdd:PRK10261 460 yphEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL 539
|
....
gi 504274718 234 GSII 237
Cdd:PRK10261 540 GQIV 543
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
42-220 |
1.46e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.12 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGIlTPT--SGDITVNGmnphKEREK------FAQTIGVVfgqRSQLWWD 113
Cdd:PRK10938 277 HNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgySNDLTLFG----RRRGSgetiwdIKKHIGYV---SSSLHLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFR--LLKK------VYK-VSDedynAHMEHVIQTLDI----GPLLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:PRK10938 349 YRVSTSVRnvILSGffdsigIYQaVSD----RQQKLAQQWLDIlgidKRTADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504274718 181 LDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLAD 220
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAED 464
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
34-248 |
1.85e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 34 NYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTIGVVFGQRsQLW 111
Cdd:PRK11614 14 HYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkdITDWQTAKIMREAVAIVPEGR-RVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 112 WDIAVQESfrLLKKVYKVSDEDYNAHMEHViqtLDIGP-LLDKPVRK---LSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK11614 93 SRMTVEEN--LAMGGFFAERDQFQERIKWV---YELFPrLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 188 LDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
42-240 |
2.30e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.86 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGI--LTPTSGDITVNG-----MNPHkEREK------FAQTI---GVvfg 105
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGedileLSPD-ERARagiflaFQYPVeipGV--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 qrsqlwwdiavqeSFR-LLKKVY------KVSDEDYNAHMEHVIQTLDIGP-LLDKPV-RKLSLGQRMRCELAAALIHNP 176
Cdd:COG0396 93 -------------SVSnFLRTALnarrgeELSAREFLKLLKEKMKELGLDEdFLDRYVnEGFSGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 177 PLLFLDEPTIGLDV----LVKLKIRQFLKEinekyNTTILLTTHD---LADIEAlcERVVMLDEGSIIYDG 240
Cdd:COG0396 160 KLAILDETDSGLDIdalrIVAEGVNKLRSP-----DRGILIITHYqriLDYIKP--DFVHVLVDGRIVKSG 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
41-241 |
2.48e-12 |
|
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: 64.86 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGI--LTPTSGDITVNG-----MNPHkerEKFAQTIGVVFgqrsqlwwd 113
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGeditdLPPE---ERARLGIFLAF--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 iavQESFRllkkVYKVSDEDYnahmehvIQTLDIGplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV--- 190
Cdd:cd03217 84 ---QYPPE----IPGVKNADF-------LRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIdal 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 191 -LVKLKIRQFLKEinekyNTTILLTTH--DLAD-IEAlcERVVMLDEGSIIYDGS 241
Cdd:cd03217 141 rLVAEVINKLREE-----GKSVLIITHyqRLLDyIKP--DRVHVLYDGRIVKSGD 188
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
39-231 |
2.53e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.51 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKEREKF---AQTiGVVFGQ--RS 108
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistLKPEIYRQQVsycAQT-PTLFGDtvYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 QLW--WDIAVQ--ESFRLLKkvykvsDEDYNAHMEHviqtldigpLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:PRK10247 100 NLIfpWQIRNQqpDPAIFLD------DLERFALPDT---------ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504274718 185 TIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEAlCERVVML 231
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITL 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
55-240 |
4.64e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 55 GYIGENGAGKSTTIKMLTGILTPTSGDITvngMNPHkER------EKFA----QTIGVVFGQRSQLWwdIAVQESFRllk 124
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVS---LDPN-ERlgklrqDQFAfeefTVLDTVIMGHTELW--EVKQERDR--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 125 kVY---KVSDEDYN--AHMEHVIQTLD-------IGPLL----------DKPVRKLSLGQRMRCELAAALIHNPPLLFLD 182
Cdd:PRK15064 102 -IYalpEMSEEDGMkvADLEVKFAEMDgytaearAGELLlgvgipeeqhYGLMSEVAPGWKLRVLLAQALFSNPDILLLD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 183 EPTIGLDVLVklkIRqFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI-IYDG 240
Cdd:PRK15064 181 EPTNNLDINT---IR-WLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELrVYPG 235
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-235 |
5.55e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.37 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 26 AFRDL--FTRNYRVMkaVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVngmnPHKERekfaqtigVV 103
Cdd:COG4178 364 ALEDLtlRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR----PAGAR--------VL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 F-GQRSQLwwdiaVQESFR--LLkkvYKVSDEDY-NAHMEHVIQTLDIGPL---LDKPV---RKLSLGQRMRCELAAALI 173
Cdd:COG4178 430 FlPQRPYL-----PLGTLReaLL---YPATAEAFsDAELREALEAVGLGHLaerLDEEAdwdQVLSLGEQQRLAFARLLL 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 174 HNPPLLFLDEPTIGLDVLVKLKIRQFLKEinEKYNTTILLTTHDlADIEALCERVVMLDEGS 235
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHR-STLAAFHDRVLELTGDG 560
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-236 |
5.74e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.73 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRVMkaVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDIT---------VNGMNPHKEREKFAQtigVV 103
Cdd:PRK10636 11 RGVRVL--LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPALPQPALEY---VI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 FGQRSqlwwdiavqesFRLLKKVYKVSDEDYNAH-MEHVIQTLD-----------------IG---PLLDKPVRKLSLGQ 162
Cdd:PRK10636 86 DGDRE-----------YRQLEAQLHDANERNDGHaIATIHGKLDaidawtirsraasllhgLGfsnEQLERPVSDFSGGW 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 163 RMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKeineKYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK10636 155 RMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLK----SYQGTLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
35-248 |
6.36e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.61 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVndiSFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQ--------------TI 100
Cdd:PRK10619 18 HEVLKGV---SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlrllrtRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 101 GVVFgQRSQLWWDIAVQESfrLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRK----LSLGQRMRCELAAALIHNP 176
Cdd:PRK10619 95 TMVF-QHFNLWSHMTVLEN--VMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKypvhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 177 PLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
27-248 |
9.59e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDLFTRnYR--VMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVF 104
Cdd:PLN03232 1237 FEDVHLR-YRpgLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSII 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 GQRSQLWwdiavQESFRL-LKKVYKVSDED-----YNAHMEHVIQTLDIGplLDKPV----RKLSLGQRMRCELAAALIH 174
Cdd:PLN03232 1316 PQSPVLF-----SGTVRFnIDPFSEHNDADlwealERAHIKDVIDRNPFG--LDAEVseggENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 175 NPPLLFLDEPTIGLDVLVKLKIRQFLKEinEKYNTTILLTTHDLADIeALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-237 |
1.43e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 28 RDLFTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHK----------- 91
Cdd:COG3845 261 ENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGeditgLSPRErrrlgvayipe 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 92 EREKFAqTIGvvfgqrsqlwwDIAVQESFrLLKKVYK--------VSDEDYNAHMEHVIQTLDI-GPLLDKPVRKLSLG- 161
Cdd:COG3845 341 DRLGRG-LVP-----------DMSVAENL-ILGRYRRppfsrggfLDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGn 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 162 -QRMRceLAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:COG3845 408 qQKVI--LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
41-242 |
1.69e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTS--GDITVNGMNPHKEREKfaqTIGVVfGQRSQLWWDIAVQE 118
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK---RTGFV-TQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 119 SF---RLLKKVYKVSDEDYNAHMEHVIQTLDIGP-----LLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PLN03211 160 TLvfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504274718 191 LVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSL 242
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKG 291
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
41-190 |
2.51e-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: 64.57 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNgmnphkEREKfaqtIGVVFGQRSQL------WWDI 114
Cdd:TIGR03719 338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG------ETVK----LAYVDQSRDALdpnktvWEEI 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 115 AV-QESFRLLKkvYKVSDEDYNAHMEHViqtldiGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:TIGR03719 408 SGgLDIIKLGK--REIPSRAYVGRFNFK------GSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-241 |
2.56e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKERE-------KFAQTIGVVFgQRSQLWWD 113
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifqidaiKLRKEVGMVF-QQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFRLLKKVYKVSDE-DYNAHMEHVIQTL----DIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504274718 189 DVLVKLKIRQFLKEIneKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGS 241
Cdd:PRK14246 185 DIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
42-237 |
2.74e-11 |
|
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: 64.46 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 42 NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN-----PHKERekfaQTIGVVfGQRSQLWWD--- 113
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDirdvtQASLR----AAIGIV-PQDTVLFNDtia 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 --IA----------VQESFRLlkkvykvsdedynAHMEHVIQTLDIGplLDKPV--R--KLSLGQRMRCELAAALIHNPP 177
Cdd:COG5265 450 ynIAygrpdaseeeVEAAARA-------------AQIHDFIESLPDG--YDTRVgeRglKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 178 LLFLDEPTIGLDVLVKLKIRQFLKEINEkyNTTILLTTHDLADIeALCERVVMLDEGSII 237
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTI-VDADEILVLEAGRIV 571
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
39-236 |
2.88e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILT-PTSGDITVNGM-----NPhkeREKFAQTIGVVFGQRSQ--L 110
Cdd:PRK13549 276 KRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvkirNP---QQAIAQGIAMVPEDRKRdgI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESFRL--LKKVYKVSDEDYNA---HMEHVIQTLDI-GPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEP 184
Cdd:PRK13549 353 VPVMGVGKNITLaaLDRFTGGSRIDDAAelkTILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504274718 185 TIGLDVLVKLKIrqfLKEINE--KYNTTILLTTHDLADIEALCERVVMLDEGSI 236
Cdd:PRK13549 433 TRGIDVGAKYEI---YKLINQlvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
43-221 |
2.91e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKE------REKfaqtIGVVfgQRSQLWWDIAV 116
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinlkwwRSK----IGVV--SQDPLLFSNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QE-------SFRLLKKVYKVSDEDYNAHMEH-----------------VIQTLD-------------------------- 146
Cdd:PTZ00265 477 KNnikyslySLKDLEALSNYYNEDGNDSQENknkrnscrakcagdlndMSNTTDsneliemrknyqtikdsevvdvskkv 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 147 -----IGPLLDK-------PVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLT 214
Cdd:PTZ00265 557 lihdfVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
....*..
gi 504274718 215 THDLADI 221
Cdd:PTZ00265 637 AHRLSTI 643
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
45-245 |
3.64e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 45 SFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGditvngmnphkEREK-FAQTIGVVFGQRSQLwwdiaVQESFRLL 123
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG-----------ERQSqFSHITRLSFEQLQKL-----VSDEWQRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 124 KKVYKVSDED---------------YNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PRK10938 87 NTDMLSPGEDdtgrttaeiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 189 DVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK10938 167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-190 |
4.72e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 4.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 5 IEVNQLRKefkayssrsglkgAFRDlftrnyRVMkaVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITV 84
Cdd:PRK11819 325 IEAENLSK-------------SFGD------RLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 85 ngmnphkerekfAQT--IGVVFGQRSQLWWDiavqesfrllKKVYK-VSDEdynahmehviqtLDI-------------- 147
Cdd:PRK11819 384 ------------GETvkLAYVDQSRDALDPN----------KTVWEeISGG------------LDIikvgnreipsrayv 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504274718 148 ------GPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PRK11819 430 grfnfkGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
39-237 |
5.07e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGV-VFGQRSQLWWDIAVQ 117
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIgIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 118 ESFRL------------LKKVYKVSDEdynahmehVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PRK10762 98 ENIFLgrefvnrfgridWKKMYAEADK--------LLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504274718 186 iglDVLVKLKIRQFLKEINE--KYNTTILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:PRK10762 170 ---DALTDTETESLFRVIRElkSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
43-242 |
5.23e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.10 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTP--TSGDITVNGMNphKEREKFAQTIGvvFGQRSQLWW-DIAVQES 119
Cdd:PLN03140 898 EVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFP--KKQETFARISG--YCEQNDIHSpQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 F------RLLKKVYKvsdEDYNAHMEHVIQTLDIGPLLDKPV-----RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:PLN03140 974 LiysaflRLPKEVSK---EEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 189 D----VLVKLKIRqflkeinekyNT-----TILLTTHDLA-DI-EALCERVVMLDEGSIIYDGSL 242
Cdd:PLN03140 1051 DaraaAIVMRTVR----------NTvdtgrTVVCTIHQPSiDIfEAFDELLLMKRGGQVIYSGPL 1105
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
27-248 |
5.93e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 5.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 27 FRDLFTRnYR--VMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK----EREKFAQTI 100
Cdd:PLN03130 1240 FEDVVLR-YRpeLPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmDLRKVLGII 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 101 --------GVV------FGQRS--QLWwdiavqESFRllkkvykvsdedyNAHMEHVIQTLDIGplLDKPV----RKLSL 160
Cdd:PLN03130 1319 pqapvlfsGTVrfnldpFNEHNdaDLW------ESLE-------------RAHLKDVIRRNSLG--LDAEVseagENFSV 1377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 161 GQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRqflKEINEKYNT-TILLTTHDLADIeALCERVVMLDEGSIIYD 239
Cdd:PLN03130 1378 GQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQ---KTIREEFKScTMLIIAHRLNTI-IDCDRILVLDAGRVVEF 1453
|
....*....
gi 504274718 240 GSLQKLRSN 248
Cdd:PLN03130 1454 DTPENLLSN 1462
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
11-236 |
7.61e-11 |
|
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: 63.43 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 11 RKEFKAYS--SRSGLkgafrDLFTRnyrvmkavnDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMN 88
Cdd:TIGR00957 1284 RVEFRNYClrYREDL-----DLVLR---------HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 89 PHKerekfaqtIGvVFGQRSQLwwDIAVQE------SFRL-LKKVYKVSDEDY-----NAHMEHVIQTLDIGplLDKPV- 155
Cdd:TIGR00957 1350 IAK--------IG-LHDLRFKI--TIIPQDpvlfsgSLRMnLDPFSQYSDEEVwwaleLAHLKTFVSALPDK--LDHECa 1416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 156 ---RKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV----LVKLKIR-QFlkeinekYNTTILLTTHDLADIEALcER 227
Cdd:TIGR00957 1417 eggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLetdnLIQSTIRtQF-------EDCTVLTIAHRLNTIMDY-TR 1488
|
....*....
gi 504274718 228 VVMLDEGSI 236
Cdd:TIGR00957 1489 VIVLDKGEV 1497
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-226 |
1.33e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 31 FTRNYRVMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGiLTPTSGDITVNG------MNPHKER---EKFAQTIG 101
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGrveffnQNIYERRvnlNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 102 VVFGQRSQLWWDI--AVQESFRLLKKVYKVSDEDYnahMEHVIQTLD----IGPLLDKPVRKLSLGQRMRCELAAALIHN 175
Cdd:PRK14258 92 MVHPKPNLFPMSVydNVAYGVKIVGWRPKLEIDDI---VESALKDADlwdeIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504274718 176 PPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIEALCE 226
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
39-245 |
1.35e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTIGVVFgQRSQLWWDIAV 116
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALENGISMVH-QELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRL----LKKVYKVSDEDYNaHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL---D 189
Cdd:PRK10982 91 MDNMWLgrypTKGMFVDQDKMYR-DTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 190 VLVKLKIRQFLKEinekYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK10982 170 VNHLFTIIRKLKE----RGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-247 |
2.28e-10 |
|
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: 61.85 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 30 LFTRNYR--VMKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITvngmnpHKEREKFAQ--------T 99
Cdd:TIGR01271 429 LFFSNFSlyVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK------HSGRISFSPqtswimpgT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 100 I--GVVFGQRSQLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIqtldigplldkpvrKLSLGQRMRCELAAALIHNPP 177
Cdd:TIGR01271 503 IkdNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGI--------------TLSGGQRARISLARAVYKDAD 568
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 178 LLFLDEPTIGLDVLVKlkirqflKEINEK------YNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKLRS 247
Cdd:TIGR01271 569 LYLLDSPFTHLDVVTE-------KEIFESclcklmSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQA 636
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
41-248 |
2.34e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSG-----DITVNGMNPHKERE--KFAQTIGVVFgQRSQLWwD 113
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLF-QRPNPF-P 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFRLLKKVYK-VSDEDYNAHMEHVIQTLDI-----GPLLDKPVRkLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK14271 115 MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavkDRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 188 LDVLVKLKIRQFLKEINEKYntTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
41-243 |
2.50e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.34 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVngmnphkerekfAQTIGVVFGQRSQLWW----DIAV 116
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL------------AKGIKLGYFAQHQLEFlradESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDYNAHMEHViqtldiGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDvlvkLKI 196
Cdd:PRK10636 396 QHLARLAPQELEQKLRDYLGGFGFQ------GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDM 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504274718 197 RQFLKEINEKYNTTILLTTHDLADIEALCERVVMLDEGSI-IYDGSLQ 243
Cdd:PRK10636 466 RQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVePFDGDLE 513
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-217 |
2.58e-10 |
|
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: 59.16 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRVMKAVNDISFTvkqGEMVGYIGENGAGKSTTIKMLTGILT---PTSGDITVNGMNPHKEREKFAQtIGVVFGQRSQ 109
Cdd:cd03240 7 RNIRSFHERSEIEFF---SPLTLIVGQNGAGKTTIIEALKYALTgelPPNSKGGAHDPKLIREGEVRAQ-VKLAFENANG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 110 LwwDIAVQESFRLLKKVYKVSDEDYNAhmehviqtldigPLLDKPVRkLSLGQRM------RCELAAALIHNPPLLFLDE 183
Cdd:cd03240 83 K--KYTITRSLAILENVIFCHQGESNW------------PLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDE 147
|
170 180 190
....*....|....*....|....*....|....*
gi 504274718 184 PTIGLDV-LVKLKIRQFLKEINEKYNTTILLTTHD 217
Cdd:cd03240 148 PTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
43-247 |
2.92e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 60.26 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITvngmnpHKEREKFAQ--------TI--GVVFGQRSQLWW 112
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK------HSGRISFSSqfswimpgTIkeNIIFGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DIAVQESFRLLKKVYKVSDEDYNAHMEHVIQtldigplldkpvrkLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLV 192
Cdd:cd03291 129 YKSVVKACQLEEDITKFPEKDNTVLGEGGIT--------------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504274718 193 KlkirqflKEINEK------YNTTILLTTHDLADIEAlCERVVMLDEGSIIYDGSLQKLRS 247
Cdd:cd03291 195 E-------KEIFEScvcklmANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-248 |
2.94e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.93 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 22 GLKGAFRDLftrnyRVMKAVNdisFTVKQGEMVGYIGENGAGKSTTIKMLTGI--LTP---TSGDITVNGMNPHK----E 92
Cdd:PRK14247 8 DLKVSFGQV-----EVLDGVN---LEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKmdviE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 93 REKFAQTIGVVFGQRSQL--WWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAA 170
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLsiFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 171 ALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEIneKYNTTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
44-189 |
3.59e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 44 ISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGM-NPHKEREKFAQTIGVVFGQRSqlwwDIAVQESFRL 122
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtATRGDRSRFMAYLGHLPGLKA----DLSTLENLHF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504274718 123 LKKVykvsdedynaHMEHVIQT----LDIGPLLDKP---VRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:PRK13543 106 LCGL----------HGRRAKQMpgsaLAIVGLAGYEdtlVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-237 |
4.47e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILtPT---SGDITVNGmnphkEREKF-----AQTIGVVF------ 104
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDG-----EVCRFkdirdSEALGIVIihqela 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 105 -----------------GQRSQLWWDIAVQESFRLLKKVykvsdedynahmehviqTLDIGPllDKPVRKLSLGQRMRCE 167
Cdd:NF040905 89 lipylsiaeniflgnerAKRGVIDWNETNRRARELLAKV-----------------GLDESP--DTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504274718 168 LAAALIHNPPLLFLDEPTIGL-----DVLVKLkirqfLKEINEKYNTTILLtTHDLADIEALCERVVMLDEGSII 237
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALneedsAALLDL-----LLELKAQGITSIII-SHKLNEIRRVADSITVLRDGRTI 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
43-254 |
6.83e-10 |
|
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: 59.10 E-value: 6.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTpTSGDITVNGMNPHK-EREKFAQTIGVVFGQ--------RSQL--- 110
Cdd:cd03289 22 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGVIPQKvfifsgtfRKNLdpy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 --WWDiavqesfrllKKVYKVSDE-DYNAHMEHVIQTLDIgPLLDKPVrKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:cd03289 101 gkWSD----------EEIWKVAEEvGLKSVIEQFPGQLDF-VLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 188 LDVLVKLKIRQFLKEINEkyNTTILLTTHDladIEAL--CERVVMLDEGSIIYDGSLQKLRSNWGDLKQ 254
Cdd:cd03289 169 LDPITYQVIRKTLKQAFA--DCTVILSEHR---IEAMleCQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
40-218 |
1.11e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.25 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGI--LTPT---SGDITVNGMN---PHKEREKFAQTIGVVFgQR---- 107
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNlyaPDVDPVEVRRRIGMVF-QKpnpf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 108 -SQLWWDIAvqesfrllkkvYKVSDEDYNAHMEHVIQT-LDIGPLLDKPVRK-------LSLGQRMRCELAAALIHNPPL 178
Cdd:PRK14243 104 pKSIYDNIA-----------YGARINGYKGDMDELVERsLRQAALWDEVKDKlkqsglsLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504274718 179 LFLDEPTIGLDVLVKLKIRQFLKEINEKYntTILLTTHDL 218
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-217 |
3.54e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 3.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAVN-------DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGD------ITVnGM---NPHKEREKfaq 98
Cdd:PRK11819 10 NRVSKVVPpkkqilkDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEarpapgIKV-GYlpqEPQLDPEK--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 99 TI-GVVfgqrsqlwwDIAVQESFRLLKKVYKVS------DEDYNAHMEH------VIQTLDIG---------------PL 150
Cdd:PRK11819 86 TVrENV---------EEGVAEVKAALDRFNEIYaayaepDADFDALAAEqgelqeIIDAADAWdldsqleiamdalrcPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 151 LDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEinekYNTTILLTTHD 217
Cdd:PRK11819 157 WDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD----YPGTVVAVTHD 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
40-234 |
4.44e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG--MNPHKEREKFAQTIGVVFGQRSQL----WWD 113
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkINNHNANEAINHGFALVTEERRSTgiyaYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 114 IAVQESFRLLKKvYK-----VSDEDYNAHMEHVIQTLDIG-PLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIG 187
Cdd:PRK10982 343 IGFNSLISNIRN-YKnkvglLDNSRMKSDTQWVIDSMRVKtPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 504274718 188 LDVLVKLKIRQFLKEINEKyNTTILLTTHDLADIEALCERVVMLDEG 234
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-238 |
6.21e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 2 KNAIEVNQLRKEFKAyssrsglkgafRDLFtrnyrvmkavNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGD 81
Cdd:PRK15064 317 RNALEVENLTKGFDN-----------GPLF----------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 82 I--TVN---GMNPHKEREKFAQTIgVVFGQRSQlwW------DIAVQESF-RLLkkvykVSDEDYNahmehviqtldigp 149
Cdd:PRK15064 376 VkwSENaniGYYAQDHAYDFENDL-TLFDWMSQ--WrqegddEQAVRGTLgRLL-----FSQDDIK-------------- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 150 lldKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVlvklkirQFLKEIN---EKYNTTILLTTHDLADIEALCE 226
Cdd:PRK15064 434 ---KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM-------ESIESLNmalEKYEGTLIFVSHDREFVSSLAT 503
|
250
....*....|..
gi 504274718 227 RVVMLDEGSIIY 238
Cdd:PRK15064 504 RIIEITPDGVVD 515
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-248 |
1.00e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.23 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 32 TRNYRVMKAVN----DISFTVKQGEMVGYIGENGAGKSTTIKMLTGIL-----TPTSGDITVNG-------MNPHKEREK 95
Cdd:PRK14267 7 TVNLRVYYGSNhvikGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGrniyspdVDPIEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 96 faqtIGVVFGQRS-----QLWWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDIGPLLDKPVRKLSLGQRMRCELAA 170
Cdd:PRK14267 87 ----VGMVFQYPNpfphlTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 171 ALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYntTILLTTHDLADIEALCERVVMLDEGSIIYDGSLQKLRSN 248
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-216 |
2.30e-08 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 52.93 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 30 LFTRNYRVMkaVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDItvnGMNPHKerekfaqtiGVVF-GQRS 108
Cdd:cd03223 8 LATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE---------DLLFlPQRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 109 QLwwdiaVQESFRllkkvykvsdedynahmEHVIQTLDigplldkpvRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:cd03223 74 YL-----PLGTLR-----------------EQLIYPWD---------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
|
170 180
....*....|....*....|....*...
gi 504274718 189 DVLVKLKIRQFLKEinekYNTTILLTTH 216
Cdd:cd03223 123 DEESEDRLYQLLKE----LGITVISVGH 146
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
35-245 |
4.79e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 35 YRVMKAV-NDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNG-----MNPHKEREKFA--QTIGVV--- 103
Cdd:PRK10790 350 YRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplssLSHSVLRQGVAmvQQDPVVlad 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 -FGQRSQLWWDIAVQESFRLLKKVykvsdedynaHMEHVIQTLDIG--PLLDKPVRKLSLGQRMRCELAAALIHNPPLLF 180
Cdd:PRK10790 430 tFLANVTLGRDISEEQVWQALETV----------QLAELARSLPDGlyTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 181 LDEPTIGLDVLVKLKIRQFLKEINEKynTTILLTTHDLADI-EAlcERVVMLDEGSIIYDGSLQKL 245
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIvEA--DTILVLHRGQAVEQGTHQQL 561
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
54-189 |
8.43e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 54 VGYI-GENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSqlwwDIAVQESFRLLKKVYKVSDE 132
Cdd:PRK13541 28 ITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKL----EMTVFENLKFWSEIYNSAET 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 133 DYNAhmehvIQTLDIGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLD 189
Cdd:PRK13541 104 LYAA-----IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
33-225 |
8.72e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 53.08 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRvmkAVNDISFTVKQGEMVgYIGENGAGKSTTIKMLTGILTPTSG-DITVNGMNPHKEREKFAQTIGVVFGQR-SQL 110
Cdd:COG3593 9 KNFR---SIKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSrKFDEEDFYLGDDPDLPEIEIELTFGSLlSRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTL-------------DIGPLLDK------------------PVRKLS 159
Cdd:COG3593 85 LRLLLKEEDKEELEEALEELNEELKEALKALNELLseylkelldgldlELELSLDEledllkslslriedgkelPLDRLG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 160 LGQR------MRCELA-AALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKyNTTILLTTH-----DLADIEALC 225
Cdd:COG3593 165 SGFQrlillaLLSALAeLKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEK-PNQVIITTHsphllSEVPLENIR 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
41-270 |
6.80e-07 |
|
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: 51.10 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 41 VNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTI----GVVFGQRSQLWWDIAV 116
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDslreNILFGKALNEKYYQQV 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKVYKVSDEDynahmehviQTlDIGpllDKPVrKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKI 196
Cdd:TIGR00957 734 LEACALLPDLEILPSGD---------RT-EIG---EKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504274718 197 rqFLKEINEK---YNTTILLTTHDLADIEALcERVVMLDEGSIIYDGSLQKLRSNWGDLKQvtFEFGTAPNKEQLKL 270
Cdd:TIGR00957 800 --FEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDGAFAE--FLRTYAPDEQQGHL 871
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
38-218 |
8.04e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 49.25 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 38 MKAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHKEREKFAQTIG---VVFGQRSQLWWDI 114
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 AVQESFRLL----KKVYKVSDEdyNAHMEHVIQTLDIGPLLDKPVR--KLSLGQRMRCELAAALIHNPPLLFLDEPTIGL 188
Cdd:cd03290 94 TVEENITFGspfnKQRYKAVTD--ACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 504274718 189 DV-----LVKLKIRQFLKEINEkyntTILLTTHDL 218
Cdd:cd03290 172 DIhlsdhLMQEGILKFLQDDKR----TLVLVTHKL 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
43-190 |
2.26e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITvngmnphkereKFAQTIGVVFGQRSQLWWDIAVQESFRL 122
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHHVDGLDLSSNPLLYM 595
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504274718 123 LKKVYKVSDEDYNAHMEHVIQTldiGPLLDKPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDV 190
Cdd:PLN03073 596 MRCFPGVPEQKLRAHLGSFGVT---GNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
40-245 |
2.57e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 48.94 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPTSGDITVNGMNPHK-----EREKFAqtigvVFGQRSQLWWDI 114
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqldsWRSRLA-----VVSQTPFLFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 115 -----------AVQESFRLLKKVYKVSDEdynahmehvIQTLDIGPLLDKPVR--KLSLGQRMRCELAAALIHNPPLLFL 181
Cdd:PRK10789 405 vannialgrpdATQQEIEHVARLASVHDD---------ILRLPQGYDTEVGERgvMLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504274718 182 DEPTIGLDVLVKLKIRQFLKEINEKynTTILLTTHDLAdieALCE--RVVMLDEGSIIYDGSLQKL 245
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLS---ALTEasEILVMQHGHIAQRGNHDQL 536
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-222 |
3.97e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 37 VMKAVNDISFTvkqgemvgyiGENGAGKSTTikmltgiLTPTSGDITVNGMNPHKEREKFAQTIGVVFGQRSQLWwDIAV 116
Cdd:PTZ00265 1251 GMKNVNEFSLT----------KEGGSGEDST-------VFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSI 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 117 QESFRLLKKvyKVSDEDYN-----AHMEHVIQTL------DIGPLldkpVRKLSLGQRMRCELAAALIHNPPLLFLDEPT 185
Cdd:PTZ00265 1313 YENIKFGKE--DATREDVKrackfAAIDEFIESLpnkydtNVGPY----GKSLSGGQKQRIAIARALLREPKILLLDEAT 1386
|
170 180 190
....*....|....*....|....*....|....*..
gi 504274718 186 IGLDVLVKLKIRQFLKEINEKYNTTILLTTHDLADIE 222
Cdd:PTZ00265 1387 SSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
43-240 |
4.44e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 43 DISFTVKQGEMVGYIGENGAGKSTTIKMLTGILTPT---SGDITVNGMN-----PHKEREKFAQT---IGVV-------- 103
Cdd:PLN03140 183 DASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRlnefvPRKTSAYISQNdvhVGVMtvketldf 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 104 ------FGQRSQLWWDIAVQESFR---------LLKKVYKVSDEDYNAHMEHVIQTL--DIGP---LLDKPVRKLSLGQR 163
Cdd:PLN03140 263 sarcqgVGTRYDLLSELARREKDAgifpeaevdLFMKATAMEGVKSSLITDYTLKILglDICKdtiVGDEMIRGISGGQK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 164 MRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKEINEKYNTTILLT-------THDLADiealceRVVMLDEGSI 236
Cdd:PLN03140 343 KRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSllqpapeTFDLFD------DIILLSEGQI 416
|
....
gi 504274718 237 IYDG 240
Cdd:PLN03140 417 VYQG 420
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
50-221 |
1.32e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 44.67 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 50 QGEMVGYIGENGAGKSTTIKMLTGILTPTSGditvngmnphkerekfaqtigvvfgqrsqlwwdiavqesfrllkKVYKV 129
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG--------------------------------------------GVIYI 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 130 SDEDYNAhmehviQTLDIGPLLDKPVRKLSLGQRMRCELAAALI--HNPPLLFLDEPTIGLDV-----LVKLKIRQFLKE 202
Cdd:smart00382 37 DGEDILE------EVLDQLLLIIVGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAeqealLLLLEELRLLLL 110
|
170
....*....|....*....
gi 504274718 203 INEKYNTTILLTTHDLADI 221
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDL 129
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-237 |
2.70e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 39 KAVNDISFTVKQGEMVGYIGENGAGKsTTIKML-------TGIltptSGDITVNGmnphKE------REKFAQTIGVVFG 105
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGR-TELAMSvfgrsygRNI----SGTVFKDG----KEvdvstvSDAIDAGLAYVTE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 106 QRSQ----LWWDIAVQESFRLLKKV-----------YKVSdEDYNAHMEhvIQTldigPLLDKPVRKLSLGQRMRCELAA 170
Cdd:NF040905 345 DRKGyglnLIDDIKRNITLANLGKVsrrgvideneeIKVA-EEYRKKMN--IKT----PSVFQKVGNLSGGNQQKVVLSK 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 171 ALIHNPPLLFLDEPTIGLDVLVKLKIRQFlkeINEKYNT--TILLTTHDLADIEALCERVVMLDEGSII 237
Cdd:NF040905 418 WLFTDPDVLILDEPTRGIDVGAKYEIYTI---INELAAEgkGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
34-241 |
1.06e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 34 NYRVMKAVNdisFTVKQGEMVGYIGENGAGKSTTIKMLTG--ILTPTSGDITVNGMN-PHKEREkfaqtigvvfgQRSQL 110
Cdd:CHL00131 19 ENEILKGLN---LSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESiLDLEPE-----------ERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 111 WWDIAVQESFrllkKVYKVSDED-----YNAHMEHvIQTLDIGPL--LDKPVRKLSL------------------GQRMR 165
Cdd:CHL00131 85 GIFLAFQYPI----EIPGVSNADflrlaYNSKRKF-QGLPELDPLefLEIINEKLKLvgmdpsflsrnvnegfsgGEKKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 166 CELAAALIHNPPLLFLDEPTIGLDVlvklkirQFLKEINEKYNT------TILLTTHdladIEALCERVV-----MLDEG 234
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDI-------DALKIIAEGINKlmtsenSIILITH----YQRLLDYIKpdyvhVMQNG 228
|
....*..
gi 504274718 235 SIIYDGS 241
Cdd:CHL00131 229 KIIKTGD 235
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-216 |
1.20e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 26 AFRDLFTRNYRVM----KAVNDISFTVKQGEMVGYIGENGAGKSTTIKMLT-----GIltPTSGDI-----TVNG----- 86
Cdd:PLN03073 174 AIKDIHMENFSISvggrDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQIlhveqEVVGddtta 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 87 ----MNPHKEREKFAQTIGVVFGQRSQLWWDIAVQES-------------FRLLKKVYKVSD--EDYNAHME--HVIQTL 145
Cdd:PLN03073 252 lqcvLNTDIERTQLLEEEAQLVAQQRELEFETETGKGkgankdgvdkdavSQRLEEIYKRLEliDAYTAEARaaSILAGL 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504274718 146 DIGPLLD-KPVRKLSLGQRMRCELAAALIHNPPLLFLDEPTIGLDVLVKLKIRQFLKeineKYNTTILLTTH 216
Cdd:PLN03073 332 SFTPEMQvKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
113-222 |
1.33e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.15 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 DIAVQESFRLLKKVYKVSDEDYNAHMEHVIQTLDiGPLldkPVRKLSLGQRmRCELAAALIH----NPPLLFLDEPTIGL 188
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERGLILLENGGG-GEL---PAFELSDGTK-RLLALLAALLsalpKGGLLLIDEPESGL 270
|
90 100 110
....*....|....*....|....*....|....
gi 504274718 189 DVLVKLKIRQFLKEiNEKYNTTILLTTHDLADIE 222
Cdd:pfam13304 271 HPKLLRRLLELLKE-LSRNGAQLILTTHSPLLLD 303
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-218 |
1.49e-04 |
|
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: 41.58 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 33 RNYRVMKAVNDISFTvkQGEMVGYIGENGAGKSTTIKmltgiltptsgditvngmnphkerekfaqTIGVVFGQRSQLww 112
Cdd:cd03227 5 GRFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTILD-----------------------------AIGLALGGAQSA-- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 113 diavqesfrlLKKVYKVSDEDYNAHMEHVIQTLDIGplldkpvrkLSLGQRMRCELAAALIH---NP-PLLFLDEPTIGL 188
Cdd:cd03227 52 ----------TRRRSGVKAGCIVAAVSAELIFTRLQ---------LSGGEKELSALALILALaslKPrPLYILDEIDRGL 112
|
170 180 190
....*....|....*....|....*....|
gi 504274718 189 DVLVKLKIRQFLKEINEKYNTTIlLTTHDL 218
Cdd:cd03227 113 DPRDGQALAEAILEHLVKGAQVI-VITHLP 141
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
40-222 |
4.42e-04 |
|
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: 40.38 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 40 AVNDISFTVKQGEMVGYIGENGAGKSTTIkmLTGILTPTSGDITvngmnphKEREKFAQTIGVVFGQrsqlwwdiavqes 119
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARLI-------SFLPKFSRNKLIFIDQ------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504274718 120 frlLKKVYKVSdedynahmehviqtldIGPL-LDKPVRKLSLGQRMRCELAAALIHNPP--LLFLDEPTIGLDvlvKLKI 196
Cdd:cd03238 68 ---LQFLIDVG----------------LGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH---QQDI 125
|
170 180
....*....|....*....|....*...
gi 504274718 197 RQFLKEINE--KYNTTILLTTHDLADIE 222
Cdd:cd03238 126 NQLLEVIKGliDLGNTVILIEHNLDVLS 153
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
168-230 |
6.10e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.99 E-value: 6.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504274718 168 LAAALIHN--PPLLFLDEPTIGL--DVLVKLkiRQFLKEINEKynTTILLTTH--DLADIEALCERVVM 230
Cdd:COG4637 269 LLAALLSPrpPPLLCIEEPENGLhpDLLPAL--AELLREASER--TQVIVTTHspALLDALEPEEVLVL 333
|
|
| |
