|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-233 |
4.63e-106 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 308.53 E-value: 4.63e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVP 84
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 165 AGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETFI 233
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFL 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-299 |
2.82e-78 |
|
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: 240.37 E-value: 2.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 12 KTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVPQEFNFNP 91
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 92 FETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 171
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 172 RRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETFILDLAAKSPLPQLEGYHYR 251
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLKVEVSMLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 252 LVDTSTLEVEVLR-------------EQGINSVFSQLSAQGIQVLSMRNKANRLEELFVSL 299
Cdd:TIGR01188 240 ELGETGLGLLAVTvdsdrikilvpdgDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-223 |
5.35e-75 |
|
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: 229.18 E-value: 5.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVP 84
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 165 AGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-214 |
1.92e-74 |
|
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: 226.12 E-value: 1.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVP 84
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQivvnqagyygverkeaidrsekYLKqldlwekrnerarmLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03230 80 EEPSLYENLTVRE----------------------NLK--------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992389469 165 AGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-232 |
1.38e-71 |
|
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: 221.27 E-value: 1.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVP 84
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 165 AGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETF 232
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-215 |
1.24e-67 |
|
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: 210.44 E-value: 1.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLV 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEP 163
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992389469 164 TAGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-303 |
2.11e-59 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 191.86 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVnakRQLGLV 83
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR---RRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPFETVQQivvnQAGYY----GVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLI 159
Cdd:COG4152 77 PEERGLYPKMKVGE----QLVYLarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 160 LDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETFILDL-AA 238
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEAdGD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 239 KSPLPQLEGYHYRLVDTSTLEVEVLREQGINSVFSQLSAQGiQVLSMRNKANRLEELFVSLVHEK 303
Cdd:COG4152 233 AGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARG-PVREFEEVRPSLNEIFIEVVGEK 296
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-215 |
5.08e-58 |
|
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: 186.00 E-value: 5.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLGLV 83
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQefnfNP-----FETVQQIV----VNQagyyGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVafgpENL----GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-215 |
1.19e-56 |
|
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: 182.18 E-value: 1.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTY---PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLG 81
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-215 |
1.65e-54 |
|
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: 176.61 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVqALRGIDLQVEAGdFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVP 84
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992389469 165 AGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03264 159 AGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-215 |
1.70e-54 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 177.10 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLV 83
Cdd:TIGR03864 1 ALEVAGLSFRY-GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEP 163
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 164 TAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNIgIIQHGELV 215
Cdd:TIGR03864 160 TVGLDPASRAAITAHVRALaRDQGLSVLWATHLVDEIEASDRLV-VLHRGRVL 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-212 |
7.90e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 175.66 E-value: 7.90e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvvnAKRQL 80
Cdd:COG1121 3 MMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----ARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFN---PFeTVQQIV-------VNQAGYYGVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARA 150
Cdd:COG1121 78 GYVPQRAEVDwdfPI-TVRDVVlmgrygrRGLFRRPSRADREAVDEA---LERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEA-----EMLCRNIGIIQHG 212
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVreyfdRVLLLNRGLVAHG 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-278 |
1.07e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 172.58 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLV------------PQ 85
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfgqrsqlwwdlpAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 86 EfnfnPFETVQQIvvnqagyYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:COG4586 115 D----SFRLLKAI-------YRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 166 GVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETFI-LDLAAKSPLP 243
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIvLELAEPVPPL 263
|
250 260 270
....*....|....*....|....*....|....*..
gi 992389469 244 QLEGYhYRLVDTS--TLEVEVLREQGINSVFSQLSAQ 278
Cdd:COG4586 264 ELPRG-GEVIEREgnRVRLEVDPRESLAEVLARLLAR 299
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-214 |
3.39e-51 |
|
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: 168.05 E-value: 3.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAK---- 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 -RQLGLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIgIIQHGEL 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRII-ELRDGKI 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-203 |
1.00e-50 |
|
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: 166.87 E-value: 1.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 6 ELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL-GLV 83
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFN---FNPfeTVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:cd03225 81 FQNPDdqfFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLC 203
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELA 201
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-215 |
3.05e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 166.77 E-value: 3.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKRQ 79
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLVPQEFNFNPFETVQQIVVN-QAGYYGVER-------KEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARAL 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAgRLGRTSTWRsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 152 MHEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLC-RNIGiIQHGELV 215
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYAdRIIG-LRDGRVV 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
3.42e-50 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.99 E-value: 3.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDV 73
Cdd:COG1136 1 MSPLLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 74 VNAKRQ-LGLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:COG1136 81 ARLRRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIgIIQHGELVENTS 219
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVI-RLRDGRIVSDER 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-203 |
4.17e-50 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 166.80 E-value: 4.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYP---GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAK 77
Cdd:COG1116 4 AAPALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGLVPQEFNFNPFETVQQ---IVVNQAGyygVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDnvaLGLELRG---VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLC 203
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLA 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-216 |
1.42e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 161.37 E-value: 1.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKRQL 80
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQ------IVVnqagyyGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:COG2884 82 GVVFQDFRLLPDRTVYEnvalplRVT------GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-215 |
2.34e-48 |
|
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: 160.52 E-value: 2.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDvvnAKRQLGLVP 84
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992389469 165 AGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
6.16e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 162.67 E-value: 6.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL 80
Cdd:PRK13537 4 SVAPIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHG 212
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-212 |
9.77e-48 |
|
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: 159.24 E-value: 9.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 6 ELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVvnakRQLGLVPQ 85
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER----KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 86 EFNFNP-FE-TVQQIV-------VNQAGYYGVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:cd03235 76 RRSIDRdFPiSVRDVVlmglyghKGLFRRLSKADKAKVDEA---LERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEA-----EMLCRNIGIIQHG 212
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVleyfdRVLLLNRTVVASG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-206 |
1.02e-47 |
|
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: 159.17 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAKRQLG 81
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 992389469 162 EPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNI 206
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRV 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
16-198 |
6.40e-47 |
|
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: 157.94 E-value: 6.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSG-RVSVFGYDLEK-DVVNAKRQLGLVPQEF--NFNP 91
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGeDVWELRKRIGLVSPALqlRFPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 92 FETVQQIVVnqAGYY---GVERK---EAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:COG1119 94 DETVLDVVL--SGFFdsiGLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190
....*....|....*....|....*....|....
gi 992389469 166 GVDIELRRSMWGFLKDLNDKG-TTIILTTHYLEE 198
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-217 |
1.78e-46 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 155.84 E-value: 1.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDvVNAKRQLGLVP 84
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVeRKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGI-RKKRIDEV---LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 165 AGVD----IELRRsmwgFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVEN 217
Cdd:cd03268 155 NGLDpdgiKELRE----LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-216 |
2.04e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 155.76 E-value: 2.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLeKDVVNAKRQLGLVP 84
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 165 AGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:cd03259 159 SALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-212 |
3.25e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 159.23 E-value: 3.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLG 81
Cdd:PRK13536 39 TVAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHG 212
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-216 |
1.24e-45 |
|
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: 161.22 E-value: 1.24e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYP----GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL 80
Cdd:COG1123 261 LEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 ----GLVPQefN----FNPFETVQQIV---VNQAGyyGVERKEAIDRSEKYLKQLDLWEK-RNERARMLSGGMKRRLMIA 148
Cdd:COG1123 341 rrrvQMVFQ--DpyssLNPRMTVGDIIaepLRLHG--LLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 149 RALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-215 |
1.26e-45 |
|
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: 154.41 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVPQE-----FNFNPF 92
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQktqlwWDLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 ETVQQIvvnqAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELR 172
Cdd:cd03267 114 DSFYLL----AAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992389469 173 RSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03267 190 ENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-226 |
1.83e-45 |
|
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: 153.89 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAK 77
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKL 157
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 158 LILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-215 |
4.18e-45 |
|
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: 153.11 E-value: 4.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKRQL 80
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETV-QQIVVNQAGYYGVER-------KEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:cd03256 81 GMIFQQFNLIERLSVlENVLSGRLGRRSTWRslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-194 |
5.67e-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: 153.27 E-value: 5.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL 80
Cdd:COG0411 1 SDPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLV-----PQEF-NFNPFETVQqIVVNQAGYYGV------------ERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMK 142
Cdd:COG0411 80 GIArtfqnPRLFpELTVLENVL-VAAHARLGRGLlaallrlprarrEEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 143 RRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTH 194
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEH 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-213 |
6.91e-45 |
|
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: 149.70 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 6 ELQQLKKTYPGGVqALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGLVP 84
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QefnfnpfetvqqivvnqagyygverkeaidrsekylkqldlwekrnerarmLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992389469 165 AGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGE 213
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-216 |
1.37e-44 |
|
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: 151.50 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAK 77
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGLVPQE--FNFNPFETVQQIVVNQAGYYGVERKEAI--DRSEKYLKQLDLWEKR-NERARMLSGGMKRRLMIARALM 152
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEArkEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-194 |
2.38e-44 |
|
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: 151.05 E-value: 2.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLV- 83
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 ----PQEF-NFNPFETVQQIVVNQAGYYGV------ERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:cd03219 80 tfqiPRLFpELTVLENVMVAAQARTGSGLLlararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-213 |
4.44e-44 |
|
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: 148.49 E-value: 4.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG---YDLEKDVVNAKRQLG 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedlTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQIVVnqagyYGverkeaidrsekylkqldlwekrnerarmLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIA-----LG-----------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGE 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-282 |
2.36e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 151.38 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAK 77
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGLVPQefNFNPFE--TVQQivvNQAgyY-----GVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARA 150
Cdd:COG1135 82 RKIGMIFQ--HFNLLSsrTVAE---NVA--LpleiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHyleeaEM-----LCRNIGIIQHGELVENTSMKNLL 224
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH-----EMdvvrrICDRVAVLENGRIVEQGPVLDVF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 225 SKLKSET---FI-LDLAAKSPLPQLEGYHYRLVDTSTLEVEVLREQGINSVFSQLSAQ-GIQV 282
Cdd:COG1135 230 ANPQSELtrrFLpTVLNDELPEELLARLREAAGGGRLVRLTFVGESADEPLLSELARRfGVDV 292
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
5.20e-43 |
|
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: 148.27 E-value: 5.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvVNAK---RQL 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS--LSRRelaRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVV----NQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVAlgryPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-215 |
7.14e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 150.63 E-value: 7.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVN---AK 77
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGlppEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGLVPQEFN-FnPFETVQQIVvnqaGYY----GVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:COG3842 77 RNVGMVFQDYAlF-PHLTVAENV----AFGlrmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-283 |
2.54e-42 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 152.36 E-value: 2.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGG-VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKS---SGRVSVFGYDL-EKDVVN 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLlELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 76 AKRQLGLVPQEF--NFNPfETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:COG1123 81 RGRRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSetf 232
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA--- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 992389469 233 ildLAAkspLPQLEGYHYRLVDTSTLEVEVLREQGINSVFSQLSAQGIQVL 283
Cdd:COG1123 237 ---LAA---VPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRGKGGVRAV 281
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
2.34e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 142.23 E-value: 2.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVP 84
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVNQAGYYGVER-KEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEP 163
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRAdREAIDEA---LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 992389469 164 TAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAE 200
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-225 |
5.92e-41 |
|
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: 141.80 E-value: 5.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVN------AKR 78
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDITGlppherARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQEFNFNPFETVQQivvN-QAGYYgVERKEAIDRSEKYLKQL--DLWEKRNERARMLSGGMKRRLMIARALMHEP 155
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEE---NlLLGAY-ARRRAKRKARLERVYELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 156 KLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-194 |
3.08e-40 |
|
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: 139.59 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL---EKDVVNAKRQLG 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETV-QQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:cd03262 80 MVFQQFNLFPHLTVlENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
1.58e-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: 135.85 E-value: 1.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNA-KRQLGLVPQEFNFNPFETVQQIV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 100 VNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARM----LSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-230 |
3.05e-39 |
|
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: 138.01 E-value: 3.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNA-KRQ 79
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLVPQ--EFNFNPFETVQQIV---VNQAGYYGVERkeaidRSEKYLKQLDLWEK-RNERARMLSGGMKRRLMIARALMH 153
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILaepLRIHGLPDREE-----RIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSE 230
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-216 |
1.19e-38 |
|
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: 136.16 E-value: 1.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKtYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KSSGRVSVFG---YDLEKDVVNA 76
Cdd:cd03260 1 IELRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdiYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 77 KRQLGLVPQEFNfnPFE-TVQQIVVNQAGYYGVERKEAID-RSEKYLKQLDLWE--KRNERARMLSGGMKRRLMIARALM 152
Cdd:cd03260 80 RRRVGMVFQKPN--PFPgSIYDNVAYGLRLHGIKLKEELDeRVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKgTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-215 |
2.31e-38 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 133.32 E-value: 2.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLvp 84
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 qefnfnpfETVQQivvnqagyygverkeaidrsekylkqldlwekrnerarmLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03216 78 --------AMVYQ---------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 992389469 165 AGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-214 |
7.99e-38 |
|
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: 133.30 E-value: 7.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNA----KRQL 80
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-201 |
1.29e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.58 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL---EKDVVNAKRQLG 81
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdsKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQ------IVVNqagyyGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEP 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLEnvtlapIKVK-----KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 992389469 156 KLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHyleeaEM 201
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH-----EM 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-224 |
1.78e-37 |
|
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: 133.58 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYD-LEKDVVNAKRQLGLV 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDL--WEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLL 224
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-216 |
2.70e-37 |
|
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: 132.75 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVN---AKRQLG 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDITNlppHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-225 |
3.78e-37 |
|
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: 132.41 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVN------AKR 78
Cdd:COG0410 4 LEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDITGlpphriARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQE---FnfnPFETVQQivvN-QAGYYGVERKEAIDRSEKYLKQL--DLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:COG0410 79 GIGYVPEGrriF---PSLTVEE---NlLLGAYARRDRAEVRADLERVYELfpRLKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-230 |
9.35e-37 |
|
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: 131.30 E-value: 9.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpgGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNA---KRQLG 81
Cdd:cd03299 1 LKVENLSKDW--KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLppeKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQivvNQAgyYGVeRKEAIDRSEKYLKQLDLWEKR------NERARMLSGGMKRRLMIARALMHEP 155
Cdd:cd03299 75 YVPQNYALFPHMTVYK---NIA--YGL-KKRKVDKKEIERKVLEIAEMLgidhllNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 156 KLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSE 230
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-216 |
2.74e-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: 132.48 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYP---GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLV---NKSSGRVSVFGydleKDVVNAK- 77
Cdd:COG0444 2 LEVRNLKVYFPtrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDG----EDLLKLSe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 --------RQLGLVPQE-FN-FNPFETV-QQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRnERARM----LSGGMK 142
Cdd:COG0444 78 kelrkirgREIQMIFQDpMTsLNPVMTVgDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPE-RRLDRypheLSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 143 RRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVE 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-215 |
3.06e-36 |
|
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: 128.32 E-value: 3.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 6 ELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvVNAK---RQLGL 82
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--LSPKelaRKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQefnfnpfetvqqivvnqagyygverkeaidrsekYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:cd03214 78 VPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 163 PTAGVDIELRRSMWGFLKDLND-KGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
3.51e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.53 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGgVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE-KDVVNAKRQ 79
Cdd:COG1129 1 AEPLLEMRGISKSFGG-VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 -LGLVPQEFNFNPFETVQQ-IVVNQ--AGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEP 155
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAEnIFLGRepRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 156 KLLILDEPTA---GVDIElrrSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:COG1129 160 RVLILDEPTAsltEREVE---RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-214 |
1.12e-35 |
|
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: 136.68 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 15 PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVPQEFNFNPFET 94
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 95 VQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 174
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992389469 175 MWGFLKDLNdKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:TIGR01257 1100 IWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-214 |
1.99e-35 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 127.52 E-value: 1.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLGLV 83
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtRKDLHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPFETVQQIVVNQagyyGVERKeaidRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEP 163
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLL----GLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 164 TAGVDI----ELRRsmwgFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:TIGR03740 152 TNGLDPigiqELRE----LIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
4.85e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.89 E-value: 4.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG----YDlEKDVVNAKRQL 80
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikYD-KKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLV---PQEFNFNPfeTVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKL 157
Cdd:PRK13639 81 GIVfqnPDDQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 158 LILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-214 |
1.00e-34 |
|
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: 125.73 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGL-- 82
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFNFnpFE--TVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:cd03218 80 LPQEASI--FRklTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 161 DEPTAGVD----IELRRsmwgFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:cd03218 158 DEPFAGVDpiavQDIQK----IIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
1.20e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.90 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIalELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-------EKDV 73
Cdd:COG4161 1 MSI--QLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 74 VNAKRQLGLVPQEFNFNPFETV-QQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVmENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-278 |
2.58e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.61 E-value: 2.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 6 ELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKR 78
Cdd:PRK11153 3 ELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQEFNFNPFETVQQIV---VNQAGyygvERKEAID-RSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:PRK11153 83 QIGMIFQHFNLLSSRTVFDNValpLELAG----TPKAEIKaRVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSET-- 231
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLtr 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 232 -FILD----------LAAKSPLPQLEGYH-YRL------VDTSTLEvEVLREQGINsvFSQLSAQ 278
Cdd:PRK11153 239 eFIQStlhldlpedyLARLQAEPTTGSGPlLRLeftgesVDAPLLS-ETARRFGVD--FNILSGQ 300
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-215 |
2.61e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.88 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVN---AKRQL 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDlppKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEF-NFnPFETVQQivvN------QAGYYGVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:COG3839 78 AMVFQSYaLY-PHMTVYE---NiafplkLRKVPKAEIDRRVREA---AELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-218 |
7.67e-34 |
|
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: 123.70 E-value: 7.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK---DVVN 75
Cdd:COG4181 6 APIIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 76 A--KRQLGLVPQEFNFNPFETVQQIV---VNQAGyygveRKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARA 150
Cdd:COG4181 86 RlrARHVGFVFQSFQLLPTLTALENVmlpLELAG-----RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMlCRNIGIIQHGELVENT 218
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-216 |
1.16e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.59 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIalELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG--YDL-----EKDV 73
Cdd:PRK11124 1 MSI--QLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFsktpsDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 74 VNAKRQLGLVPQEFNFNPFETVQQIVVNQ-AGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-194 |
1.34e-33 |
|
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: 121.76 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 14 YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE---KDVVNAKRQLGLVPQEFNFN 90
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrKGLLERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 91 PFE-TVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDI 169
Cdd:TIGR01166 81 LFAaDVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*
gi 992389469 170 ELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-203 |
1.62e-33 |
|
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: 121.98 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 13 TYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAKRQ--LGLVPQEFNFN 90
Cdd:cd03226 8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRksIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 91 PF-ETVQQIVvnqagYYGVERKEA-IDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:cd03226 84 LFtDSVREEL-----LLGLKELDAgNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 992389469 169 IELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLC 203
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHDYEFLAKVC 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-228 |
2.72e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 123.66 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 20 ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYD--LEKDVVNAKRQLGLVPQefnfNP-FETVQ 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsDEENLWDIRNKAGMVFQ----NPdNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 97 QIVVNQAGY----YGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELR 172
Cdd:PRK13633 101 TIVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 173 RSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIgIIQHGELVENTSMKNLLSKLK 228
Cdd:PRK13633 181 REVVNTIKELNKKyGITIILITHYMEEAVEADRII-VMDSGKVVMEGTPKEIFKEVE 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-219 |
2.81e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.45 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVN--AKRQLGL 82
Cdd:COG1137 4 LEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHkrARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEfnfnP--FE--TVQQ---IVVNQAGyygVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEP 155
Cdd:COG1137 83 LPQE----AsiFRklTVEDnilAVLELRK---LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 156 KLLILDEPTAGVD----IELRRsmwgFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGE-LVENTS 219
Cdd:COG1137 156 KFILLDEPFAGVDpiavADIQK----IIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKvLAEGTP 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 |
3.41e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 127.45 E-value: 3.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE----KDVVNA 76
Cdd:COG3845 2 MPPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 77 KrqLGLVPQEFN-FNPFeTVQQIVVnqagyYGVE--------RKEAIDR----SEKYLKQLDLwekrNERARMLSGGMKR 143
Cdd:COG3845 81 G--IGMVHQHFMlVPNL-TVAENIV-----LGLEptkggrldRKAARARirelSERYGLDVDP----DAKVEDLSVGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 144 RLMIARALMHEPKLLILDEPTAG-----VDiELrrsmWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG3845 149 RVEILKALYRGARILILDEPTAVltpqeAD-EL----FEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
4.40e-33 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 121.63 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNA 76
Cdd:COG1127 2 SEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 77 KRQLGLVPQE---F-NFNPFETVQ----QivvnqagYYGVERKEAIDRSEKYLKQLDLwekRNERARM---LSGGMKRRL 145
Cdd:COG1127 81 RRRIGMLFQGgalFdSLTVFENVAfplrE-------HTDLSEAEIRELVLEKLELVGL---PGAADKMpseLSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 146 MIARALMHEPKLLILDEPTAGVD-------IELrrsmwgfLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVEN 217
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDpitsaviDEL-------IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
....*..
gi 992389469 218 TSMKNLL 224
Cdd:COG1127 224 GTPEELL 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-216 |
4.71e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 124.49 E-value: 4.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIalELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL 80
Cdd:COG1118 1 MSI--EVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQivvNQAgyYGVE-----RKEAIDRSEKYLK--QLDLWEKRneRARMLSGGMKRRLMIARALMH 153
Cdd:COG1118 78 GFVFQHYALFPHMTVAE---NIA--FGLRvrppsKAEIRARVEELLElvQLEGLADR--YPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-226 |
5.48e-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: 127.57 E-value: 5.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLG 81
Cdd:COG4988 335 PSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQE---FN---------FNPFETVQQIvvnqagyygverKEAIDRS--EKYLKQL-DLWEKR-NERARMLSGGMKRRL 145
Cdd:COG4988 415 WVPQNpylFAgtirenlrlGRPDASDEEL------------EAALEAAglDEFVAALpDGLDTPlGEGGRGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 146 MIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAEmLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLA 560
|
.
gi 992389469 226 K 226
Cdd:COG4988 561 K 561
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-216 |
9.98e-33 |
|
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: 120.05 E-value: 9.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLeKDVVNAKRQLGLVP 84
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQivvNQAgyYGVE----RKEAID-RSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLI 159
Cdd:cd03301 79 QNYALYPHMTVYD---NIA--FGLKlrkvPKDEIDeRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 160 LDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-230 |
1.48e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.58 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL---EKDVVNAKRQLG 81
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFET-VQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK09493 81 MVFQQFYLFPHLTaLENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSE 230
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-214 |
3.02e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLGLV 83
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEfnfnPF---ETVQQIVvnQAGYYGVERKEAIDRSEKYLKQLDL----WEKRNERarmLSGGMKRRLMIARALMHEPK 156
Cdd:COG4619 80 PQE----PAlwgGTVRDNL--PFPFQLRERKFDRERALELLERLGLppdiLDKPVER---LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-213 |
4.83e-32 |
|
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: 117.10 E-value: 4.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGG-VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKR-QLGL 82
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFN-FNpfETVqqivvnqagyygverKEAIdrsekylkqldlwekrnerarmLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03228 81 VPQDPFlFS--GTI---------------RENI----------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLnDKGTTIILTTHYLEEAEMlCRNIGIIQHGE 213
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
1.57e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 123.68 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYD---LEKDVV 74
Cdd:PRK10535 1 MTALLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 75 NAKRQ--LGLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:PRK10535 81 AQLRRehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGiIQHGELVENTSMKN 222
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIE-IRDGEIVRNPPAQE 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
5.64e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKR-Q 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLVPQE-----FNFNPFETVQQIVVNQagyyGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:PRK13647 81 VGLVFQDpddqvFSSTVWDDVAFGPVNM----GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-216 |
7.52e-31 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 115.83 E-value: 7.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLV- 83
Cdd:TIGR04406 2 LVAENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 -PQEFN-FNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:TIGR04406 81 lPQEASiFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 162 EPTAGVD----IELRRsmwgFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:TIGR04406 161 EPFAGVDpiavGDIKK----IIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLA 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-226 |
1.76e-30 |
|
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: 121.09 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPG-GVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLG 81
Cdd:COG2274 473 DIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQE---FN---------FNPFETVQQIV--VNQAGyygVErkEAIDR-SEKYLKQLdlwekrNERARMLSGGMKRRLM 146
Cdd:COG2274 553 VVLQDvflFSgtirenitlGDPDATDEEIIeaARLAG---LH--DFIEAlPMGYDTVV------GEGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 147 IARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLnDKGTTIILTTHYLEEAEmLCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-223 |
5.89e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 113.39 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVN--AKRQLGL 82
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHerARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFNFNPFETVQQivvN-QAGYYGVERKEAIDRSEKY-----LKQLdlwekRNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:TIGR03410 80 VPQGREIFPRLTVEE---NlLTGLAALPRRSRKIPDEIYelfpvLKEM-----LGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 157 LLILDEPTAGV------DIElrrsmwGFLKDLND-KGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:TIGR03410 152 LLLLDEPTEGIqpsiikDIG------RVIRRLRAeGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-230 |
1.86e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.54 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGvQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL--------EKDVVN 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQ-TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 76 AKRQ-LGLVPQEFNFNPFETV-QQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK11264 82 QLRQhVGFVFQNFNLFPHRTVlENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSE 230
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-226 |
2.78e-29 |
|
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: 117.17 E-value: 2.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLG 81
Cdd:COG4987 333 SLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQE---FNfnpfETVQQ---IVVNQAGyygvERK--EAIDRSekylkQLDLWEKRN---------ERARMLSGGMKRR 144
Cdd:COG4987 413 VVPQRphlFD----TTLREnlrLARPDAT----DEElwAALERV-----GLGDWLAALpdgldtwlgEGGRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 145 LMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLnDKGTTIILTTHYLEEAEMLCRnIGIIQHGELVENTSMKNLL 224
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDR-ILVLEDGRIVEQGTHEELL 557
|
..
gi 992389469 225 SK 226
Cdd:COG4987 558 AQ 559
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-199 |
3.06e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVQ---ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDvvNAKRql 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP--GADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEA 199
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-228 |
3.23e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 113.26 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTY----PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYD------------ 68
Cdd:PRK13651 3 IKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 69 -LEKDVV---------NAK---RQLGLVPQEFNFNPFE-TVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERA 134
Cdd:PRK13651 83 vLEKLVIqktrfkkikKIKeirRRVGVVFQFAEYQLFEqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 135 RM-LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEA------EMLCRNIG 207
Cdd:PRK13651 163 PFeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVlewtkrTIFFKDGK 242
|
250 260 270
....*....|....*....|....*....|....*
gi 992389469 208 IIQHGE----------LVEN----TSMKNLLSKLK 228
Cdd:PRK13651 243 IIKDGDtydilsdnkfLIENnmepPKLLNFVNKLE 277
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-245 |
6.59e-29 |
|
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: 117.04 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL 80
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQefnfnpFETVQQIVVNQAGYY------GVERKEaIDRSEKY-LKQLDLWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:TIGR01257 2015 GYCPQ------FDAIDDLLTGREHLYlyarlrGVPAEE-IEKVANWsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLkSETFI 233
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKF-GDGYI 2166
|
250
....*....|....*.
gi 992389469 234 LDLAAKSP----LPQL 245
Cdd:TIGR01257 2167 VTMKIKSPkddlLPDL 2182
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-215 |
3.31e-28 |
|
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: 108.15 E-value: 3.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 24 IDLQVEaGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG---YDLEK--DVVNAKRQLGLVPQEFNFNPFETVQQI 98
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkiNLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 99 VVnqAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGF 178
Cdd:cd03297 96 LA--FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 992389469 179 LKDL-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03297 174 LKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-232 |
3.74e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.69 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpgGVQALRgIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVnAKRQLGLVP 84
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIV---VNQAGYYGVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:COG3840 78 QENNLFPHLTVAQNIglgLRPGLKLTAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETF 232
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-225 |
5.39e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.53 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-----EKDVVNAKRQLGLVPQEFNFNPFE 93
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 94 -TVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARM-LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 171
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 172 RRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
3-227 |
5.57e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.45 E-value: 5.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTYPGGV----QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-----EKDV 73
Cdd:PRK13649 1 MGINLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 74 VNAKRQLGLVPQEFNFNPF-ETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARM-LSGGMKRRLMIARAL 151
Cdd:PRK13649 81 KQIRKKVGLVFQFPESQLFeETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFeLSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 152 MHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKL 227
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDV 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-200 |
5.63e-28 |
|
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: 113.15 E-value: 5.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLG 81
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQefnfNPFETVQQIVVNQAGYYGVERKEAIDRSekyLKQLDLWE-----------KRNERARMLSGGMKRRLMIARA 150
Cdd:TIGR02857 400 WVPQ----HPFLFAGTIAENIRLARPDASDAEIREA---LERAGLDEfvaalpqgldtPIGEGGAGLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAE 200
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAA 521
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
8-216 |
8.19e-28 |
|
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: 108.50 E-value: 8.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 8 QQLKKTypGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKRQ-LGL 82
Cdd:cd03294 29 EILKKT--GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRKkISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:cd03294 107 VFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 163 PTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-269 |
9.08e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 9.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQ-LGLV 83
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 ---PQEFNFNPfeTVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK13652 84 fqnPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELV------ENTSMKNLLSKLKsetfi 233
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVaygtveEIFLQPDLLARVH----- 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 992389469 234 LDLaakSPLPQLegyhyrlvdtstleVEVLREQGIN 269
Cdd:PRK13652 237 LDL---PSLPKL--------------IRSLQAQGIA 255
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
1.59e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.79 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGGvQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLV--NKSSG-RVSVFGYD------LEK 71
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGsHIELLGRTvqregrLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 72 DVVNAKRQLGLVPQEFNF-NPFETVQQIVVNQAG----------YYGVERKEaidRSEKYLKQLDLWEKRNERARMLSGG 140
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLvNRLSVLENVLIGALGstpfwrtcfsWFTREQKQ---RALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 141 MKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-196 |
2.74e-27 |
|
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: 111.30 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLGLV 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFnpFETV--QQIVVNQAGYYGVERKEAIDRS--EKYLKQLD--LWEKRNERARMLSGGMKRRLMIARALMHEPKL 157
Cdd:TIGR02868 415 AQDAHL--FDTTvrENLRLARPDATDEELWAALERVglADWLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992389469 158 LILDEPTAGVDIELRRSMwgfLKDLND--KGTTIILTTHYL 196
Cdd:TIGR02868 493 LLLDEPTEHLDAETADEL---LEDLLAalSGRTVVLITHHL 530
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-212 |
4.06e-27 |
|
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: 105.88 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIalELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNaKRQL 80
Cdd:cd03296 1 MSI--EVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVnqagyYGVERKEAIDRSEKY-----------LKQLDLWEKR--NErarmLSGGMKRRLMI 147
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVA-----FGLRVKPRSERPPEAeirakvhellkLVQLDWLADRypAQ----LSGGQRQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 148 ARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHG 212
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-217 |
4.46e-27 |
|
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: 105.66 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKRQL 80
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQE---FN-FNPFETVQqivvnqagyYGVERKEAIDRS---EKYLKQLDLWEKRNERARM---LSGGMKRRLMIARA 150
Cdd:cd03261 80 GMLFQSgalFDsLTVFENVA---------FPLREHTRLSEEeirEIVLEKLEAVGLRGAEDLYpaeLSGGMKKRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 151 LMHEPKLLILDEPTAGVD-------IELrrsmwgfLKDLND-KGTTIILTTHYLEEAEMLCRNIGIIQHGELVEN 217
Cdd:cd03261 151 LALDPELLLYDEPTAGLDpiasgviDDL-------IRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
5.23e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 106.08 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKkTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KSSGRVSVFG---YDLEKD 72
Cdd:PRK14267 1 MKFAIETVNLR-VYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGrniYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 73 VVNAKRQLGLVPQEFNFNPFETVQQIVVNQAGYYGV--ERKEAIDRSEKYLKQLDLWE----KRNERARMLSGGMKRRLM 146
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 147 IARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKgTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-225 |
6.88e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 105.36 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGvQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVN--AKRQLGL 82
Cdd:PRK10895 4 LTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHarARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFN-------FNPFETVQQIVVNqagyygVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEP 155
Cdd:PRK10895 83 LPQEASifrrlsvYDNLMAVLQIRDD------LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 156 KLLILDEPTAGVD----IELRRsmwgFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK10895 157 KFILLDEPFAGVDpisvIDIKR----IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-230 |
9.85e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.38 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KSSGRVSVFGYDLEK-DVVNAKR 78
Cdd:PRK14247 4 IEIRDLKVSF-GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKmDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQEFNFNP----FETV------QQIVVNqagyygveRKEAIDRSEKYLKQLDLWEKRNER----ARMLSGGMKRR 144
Cdd:PRK14247 83 RVQMVFQIPNPIPnlsiFENValglklNRLVKS--------KKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 145 LMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLL 224
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
....*.
gi 992389469 225 SKLKSE 230
Cdd:PRK14247 234 TNPRHE 239
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-199 |
1.02e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 107.73 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEkDVVNAKRQLGLVP 84
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVVnqagyYG-----VERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLI 159
Cdd:PRK09452 93 QSYALFPHMTVFENVA-----FGlrmqkTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992389469 160 LDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEA 199
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEA 208
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-308 |
1.24e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 107.13 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTiGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGL- 82
Cdd:NF000106 13 AVEVRGLVKHF-GEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*h 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 ----VPQEFNFNPFETVQQIvvnqAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLL 158
Cdd:NF000106 91 rpvr*GRRESFSGRENLYMI----GR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 159 ILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETFILDLAA 238
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 239 KSPLPQ---------LEGYHYRLVD--TSTLEVEVLREQGINSVFSQLSAQGIQVLSMRNKANRLEELFVSLVHEKQGDR 307
Cdd:NF000106 247 AAELDRmvgaiaqagLDGIAGATADheDGVVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAITGQKTSEA 326
|
.
gi 992389469 308 A 308
Cdd:NF000106 327 A 327
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-212 |
2.06e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.23 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE-KDVVNAKRQLGLVPQE----FNFn 90
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDtslsFEF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 91 pfeTVQQIV-------------VNQAGYYGVERkeAIDRSEkylkqLDLWEKRNerARMLSGGMKRRLMIARALMHEPKL 157
Cdd:PRK09536 93 ---DVRQVVemgrtphrsrfdtWTETDRAAVER--AMERTG-----VAQFADRP--VTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 158 LILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHG 212
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-244 |
2.29e-26 |
|
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: 104.50 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAK---RQLGLVPQEF--NFNPF 92
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQRRafrRDVQLVFQDSpsAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 ETVQQIVVNQAGYYgvERKEAIDRSEKYLKQLDLWEKRNE----RARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:TIGR02769 105 MTVRQIIGEPLRHL--TSLDESEQKARIAELLDMVGLRSEdadkLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 169 IELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETFILDLAAKSPLPQ 244
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSAVLPEHPV 259
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-229 |
2.51e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 104.28 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKD---VVNAK 77
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrDKDgqlKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGL-------VPQEFNFNPFETVQQIVVNQ-AGYYGVERKEAIDRSEKYLKQLDLwekrNERARM-----LSGGMKRR 144
Cdd:PRK10619 85 NQLRLlrtrltmVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGI----DERAQGkypvhLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 145 LMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLL 224
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
....*
gi 992389469 225 SKLKS 229
Cdd:PRK10619 241 GNPQS 245
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-216 |
3.05e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.71 E-value: 3.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLGL 82
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLsEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQefnfNP---F--ETVQQIVV----NQagyyGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK13635 86 VFQ----NPdnqFvgATVQDDVAfgleNI----GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGT-TIILTTHYLEEAEMLCRNIgIIQHGELVE 216
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVI-VMNKGEILE 220
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-226 |
3.17e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.54 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE---KDVVNAKRQLG 81
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQE-----FNFNPFETVQQIVVNqagyYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:PRK13636 86 MVFQDpdnqlFSASVYQDVSFGAVN----LKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-215 |
3.88e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.36 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 20 ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAK---RQLGLVPQEFNFNPFE-TV 95
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirKKVGLVFQYPEYQLFEeTI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 96 QQIVVNQAGYYGVERKEAIDRSEKYLKQLDL-WEKRNERARM-LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR 173
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLdYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 992389469 174 SMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK13637 182 EILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-216 |
6.22e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 6.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEkDVVNAKRQL 80
Cdd:PRK11607 16 LTPLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-199 |
7.50e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 7.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVsvfgydlekdVVNAKRQLGLVPQEFNFN---PF 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------RRAGGARVAYVPQRSEVPdslPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 eTVQQIVV----NQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:NF040873 73 -TVRDLVAmgrwARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 992389469 169 IELRRSMWGFLKDLNDKGTTIILTTHYLEEA 199
Cdd:NF040873 152 AESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-230 |
8.22e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.20 E-value: 8.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN------KSSGRVSVFGYDLEK-DVVNAKRQLGLVPQEFNFNPFE 93
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 94 TVQQIVVNQAGYYGVERKEAIDR-SEKYLKQLDLWEKRNER----ARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 169 IELRRSMWGFLKDLNDKgTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSE 230
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-226 |
1.35e-25 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 101.92 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPG-GVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAKRQLGL 82
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQE-FNFNpfETVQQivvNQA-GYYGVERKEAIDRSE-----KYLKQLDLWEKRN--ERARMLSGGMKRRLMIARALMH 153
Cdd:cd03251 81 VSQDvFLFN--DTVAE---NIAyGRPGATREEVEEAARaanahEFIMELPEGYDTVigERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTII----LTThyLEEAEMLCrnigIIQHGELVENTSMKNLLSK 226
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFViahrLST--IENADRIV----VLEDGKIVERGTHEELLAQ 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-169 |
1.52e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE--KDVVNAKRqL 80
Cdd:PRK13548 1 AMLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELARR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFN-PFeTVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM------H 153
Cdd:PRK13548 79 AVLPQHSSLSfPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170
....*....|....*.
gi 992389469 154 EPKLLILDEPTAGVDI 169
Cdd:PRK13548 158 PPRWLLLDEPTSALDL 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-215 |
1.94e-25 |
|
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: 100.65 E-value: 1.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 25 DLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVnAKRQLGLVPQEFNFNPFETVQQIV---VN 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-ADRPVSMLFQENNLFAHLTVEQNVglgLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 102 QAGYYGVERKEAIdrsEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKD 181
Cdd:cd03298 97 PGLKLTAEDRQAI---EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*
gi 992389469 182 LN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:cd03298 174 LHaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
11-216 |
2.76e-25 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 100.68 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 11 KKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydlekDVVNakrqlglvPQEFN-- 88
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----RVSS--------LLGLGgg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 FNPFETVQQIVVNQAGYYGVERKEaIDRSEKYLKQL-DLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGV 167
Cdd:cd03220 95 FNPELTGRENIYLNGRLLGLSRKE-IDEKIDEIIEFsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992389469 168 DIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-194 |
4.63e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 100.04 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKS---SGRVSVFGYDLEKDVVnaKRQLGLVPQEFNFNPFET 94
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQF--QKCVAYVRQDDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 95 VQQIVvnqagYY------------GVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:cd03234 98 VRETL-----TYtailrlprkssdAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 992389469 163 PTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-194 |
4.84e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 104.86 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 13 TYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGLVPQE---FN 88
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDtflFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 fnpfETVQQivvNQAgyYGverKEAIDRSE--KYLKQLDLWE--KR---------NERARMLSGGMKRRLMIARALMHEP 155
Cdd:COG1132 428 ----GTIRE---NIR--YG---RPDATDEEveEAAKAAQAHEfiEAlpdgydtvvGERGVNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 992389469 156 KLLILDEPTAGVDIE----LRRSMWGFLkdlndKGTTIILTTH 194
Cdd:COG1132 496 PILILDEATSALDTEtealIQEALERLM-----KGRTTIVIAH 533
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-199 |
5.45e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGvQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAKRQLGLV 83
Cdd:PRK11248 1 MLQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG----KPVEGPGAERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEP 163
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 992389469 164 TAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEA 199
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-216 |
1.25e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.73 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKST---TIGIISSLV--NKSSGRVSVFG---YDLEKD 72
Cdd:COG1117 8 LEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIpgARVEGEILLDGediYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 73 VVNAKRQLGLVPQefNFNPF-----ETVQqivvnqAG--YYGVERKEAID-RSEKYLKQLDLWE----KRNERARMLSGG 140
Cdd:COG1117 87 VVELRRRVGMVFQ--KPNPFpksiyDNVA------YGlrLHGIKSKSELDeIVEESLRKAALWDevkdRLKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 141 MKRRLMIARALMHEPKLLILDEPTAGVD------IElrrsmwGFLKDLNDKgTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpistakIE------ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
..
gi 992389469 215 VE 216
Cdd:COG1117 232 VE 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-194 |
1.34e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 7 LQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVfgydlEKDVvnakrQLGLVPQE 86
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-----PKGL-----RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNFNPFETVQQIV----------------VNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARML------------- 137
Cdd:COG0488 70 PPLDDDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILsglgfpeedldrp 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 138 ----SGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRsmW--GFLKDLndKGtTIILTTH 194
Cdd:COG0488 150 vselSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNY--PG-TVLVVSH 207
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
16-215 |
2.01e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.03 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE--KDVVNAkRQLGLVPQ--EFNFnP 91
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawSPWELA-RRRAVLPQhsSLAF-P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 92 FeTVQQIVvnQAGYYGVERKEAIDRS--EKYLKQLDLWEKRNERARMLSGGMKRRLMIARAL-------MHEPKLLILDE 162
Cdd:COG4559 90 F-TVEEVV--ALGRAPHGSSAAQDRQivREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 163 PTAGVDI-------ELrrsmwgfLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG4559 167 PTSALDLahqhavlRL-------ARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-216 |
2.95e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.62 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYP---------------------GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSS 59
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 60 GRVSVFGydlekdvvnakRQLGLVpqEFN--FNPFETVQQIVVNQAGYYGVERKEaIDRSEKYLKQL-DLWEKRNERARM 136
Cdd:COG1134 81 GRVEVNG-----------RVSALL--ELGagFHPELTGRENIYLNGRLLGLSRKE-IDEKFDEIVEFaELGDFIDQPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 137 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELR-RSMwGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQkKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
.
gi 992389469 216 E 216
Cdd:COG1134 226 M 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-215 |
2.96e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 102.44 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL 80
Cdd:PRK15439 8 APPLLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 G--LVPQEFNFNPFETVQQIVVnqagyYGVERKE-AIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKL 157
Cdd:PRK15439 87 GiyLVPQEPLLFPNLSVKENIL-----FGLPKRQaSMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 158 LILDEPTAGVD-IELRRsMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK15439 162 LILDEPTASLTpAETER-LFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-228 |
3.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIalELQQLKKTYPGGV----QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-----EK 71
Cdd:PRK13646 1 MTI--RFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 72 DVVNAKRQLGLVPQEFNFNPFE-TVQQIVVNQAGYYGVERKEAIDRSEKYLkqLDLWEKRNERAR---MLSGGMKRRLMI 147
Cdd:PRK13646 79 YIRPVRKRIGMVFQFPESQLFEdTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSQspfQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 148 ARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
..
gi 992389469 227 LK 228
Cdd:PRK13646 237 KK 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-225 |
5.67e-24 |
|
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: 101.72 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPG-GVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGL 82
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQE---FNFNPFETVQQIVVNQAGYYGVER-------KEAIDRSEKYLKQldlweKRNERARMLSGGMKRRLMIARALM 152
Cdd:TIGR02203 411 VSQDvvlFNDTIANNIAYGRTEQADRAEIERalaaayaQDFVDKLPLGLDT-----PIGENGVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILtTHYLEEAEMLCRnIGIIQHGELVENTSMKNLLS 225
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVI-AHRLSTIEKADR-IVVMDDGRIVERGTHNELLA 556
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-203 |
6.12e-24 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 98.42 E-value: 6.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvvnAKRQ- 79
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 -LGLVPQ--EFNFNPFETVQQIVVnqAGYYG----VERKEAIDRS--EKYLKQLDLWEKRNERARMLSGGMKRRLMIARA 150
Cdd:PRK15056 79 lVAYVPQseEVDWSFPVLVEDVVM--MGRYGhmgwLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLC 203
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-194 |
9.83e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.77 E-value: 9.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQA---LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL- 80
Cdd:PRK10584 7 VEVHHLKKSVGQGEHElsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 ----GLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:PRK10584 87 akhvGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTH 194
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTH 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
5-215 |
1.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTY----PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSV-----FGYDLEKDVVN 75
Cdd:PRK13643 2 IKFEKVNYTYqpnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 76 AKRQLGLVpqeFNFNPFETVQQIVVNQAGY----YGVERKEAIDRSEKYLKQLDLWEKRNERARM-LSGGMKRRLMIARA 150
Cdd:PRK13643 82 VRKKVGVV---FQFPESQLFEETVLKDVAFgpqnFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-241 |
1.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 97.37 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVN-AKRQ 79
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLVPQefnfNPFETVQQIVVNQAGYYGVERKEaIDRSE------KYLKQLDLWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK13632 85 IGIIFQ----NPDNQFIGATVEDDIAFGLENKK-VPPKKmkdiidDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGT-TIILTTHYLEEAeMLCRNIGIIQHGELVENTSMKNLlskLKSETF 232
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI---LNNKEI 235
|
....*....
gi 992389469 233 ILDLAAKSP 241
Cdd:PRK13632 236 LEKAKIDSP 244
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-263 |
2.41e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEkdvvNAKRQLGL 82
Cdd:PRK11247 11 TPLLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA----EAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFNFNPFETVQQIVvnQAGYYGVERKEAidrsEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:PRK11247 86 MFQDARLLPWKKVIDNV--GLGLKGQWRDAA----LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 163 PTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVentsmknllsklksetfiLDLAAKSP 241
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIG------------------LDLTVDLP 221
|
250 260
....*....|....*....|..
gi 992389469 242 LPQLEGYHyRLvdtSTLEVEVL 263
Cdd:PRK11247 222 RPRRRGSA-RL---AELEAEVL 239
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
14-231 |
2.67e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 2.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 14 YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KSSGRVSVFGYDL---EKDVVNAKRQLGLVPQ 85
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 86 EFNFNPFeTVQQIVVNQAGYYGVERKEAIDRS-EKYLKQLDLWEKRNER----ARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK14239 94 QPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAvEKSLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKgTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL-LSKLKSET 231
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMfMNPKHKET 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-200 |
2.70e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.20 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 20 ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVPQEFNFNPFETVQQIV 99
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 100 VNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFL 179
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180
....*....|....*....|..
gi 992389469 180 KDLN-DKGTTIILTTHYLEEAE 200
Cdd:NF033858 441 IELSrEDGVTIFISTHFMNEAE 462
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-190 |
2.86e-23 |
|
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: 95.58 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYP----GGVQ--ALRGIDLQVEAGDFYALLGPNGAGKSTTIGII--SSLVnkSSGRVSVFGYDLEKD 72
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLP--DSGSILVRHDGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 73 VVNA---------KRQLGLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLD----LWEkrnerarmL-- 137
Cdd:COG4778 79 LAQAspreilalrRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNlperLWD--------Lpp 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 138 ---SGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTII 190
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-226 |
3.03e-23 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 95.63 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 15 PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGLVPQEFNFNPFE 93
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 94 TVQQIVVNQAGYyGVERKEAIDR---SEKYLKQLDLWEKR--NERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:cd03252 92 IRDNIALADPGM-SMERVIEAAKlagAHDFISELPEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 169 IELRRSMWGFLKDLNDkGTTIILTTHYLeEAEMLCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:cd03252 171 YESEHAIMRNMHDICA-GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-194 |
3.19e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 6 ELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAK-----RQL 80
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG----LDVATTPsrelaKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVV------NQaGYYGVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:COG4604 78 AILRQENHINSRLTVRELVAfgrfpySK-GRLTAEDREIIDEA---IAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTH 194
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH 194
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-202 |
3.46e-23 |
|
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: 93.82 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQA-LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQ-LGL 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFNFnpFE-TVQQIVvnqagyygverkeaidrsekylkqldlwekrnerarmLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03246 81 LPQDDEL--FSgSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH---YLEEAEML 202
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHrpeTLASADRI 165
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-226 |
3.77e-23 |
|
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: 95.37 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 14 YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNA-KRQLGLVPQE---FN- 88
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVVPQDtvlFNd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 --------FNPFETVQQIvvnqagyYGVERKEAIDRS-----EKYLKQLdlwekrNERARMLSGGMKRRLMIARALMHEP 155
Cdd:cd03253 90 tigyniryGRPDATDEEV-------IEAAKAAQIHDKimrfpDGYDTIV------GERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 156 KLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAeMLCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-226 |
5.90e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 98.88 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 14 YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLeKDVVNA--KRQLGLVPQE---FN 88
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI-RTVTRAslRRNIAVVFQDaglFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 FNPFETVQqivVNQAGYYGVERKEAIDRSEKylkqLDLWEKR--------NERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK13657 423 RSIEDNIR---VGRPDATDEEMRAAAERAQA----HDFIERKpdgydtvvGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKGTTII----LTThyLEEAEMlcrnIGIIQHGELVENTSMKNLLSK 226
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGRTTFIiahrLST--VRNADR----ILVFDNGRVVESGSFDELVAR 559
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
5-194 |
7.03e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.17 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK----DVVNAKRQL 80
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190
....*....|....*....|....*....|....
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-212 |
8.25e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 8.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIalELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvVNAK-RQ 79
Cdd:PRK10851 1 MSI--EIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARdRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLVPQEFNFNPFETVQQivvNQA-GYYGVERKE-----AIDRS-EKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFD---NIAfGLTVLPRRErpnaaAIKAKvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHG 212
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
11-194 |
1.49e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 92.61 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 11 KKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN--KSSGRVSVFGYDLEKDVVnaKRQLGLVPQEFN 88
Cdd:cd03213 15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF--RKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 FNPFETVQQIVVNQAgyygverkeaidrsekylkqldlwekrneRARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:cd03213 93 LHPTLTVRETLMFAA-----------------------------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180
....*....|....*....|....*.
gi 992389469 169 IELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-225 |
2.45e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAK---RQLGLVPQEF--NFNPF 92
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKafrRDIQMVFQDSisAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 ETVQQIVVNQAGYY-GVERKEAIDRSEKYLKQLDL-WEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 170
Cdd:PRK10419 106 KTVREIIREPLRHLlSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 171 LRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK10419 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
2.49e-22 |
|
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: 92.91 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAKRQLGLVPQEFNFNPFETVQQ--- 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG----KQITEPGPDRMVVFQNYSLLPWLTVREnia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 98 IVVNQAGYY--GVERKEAIdrsEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:TIGR01184 77 LAVDRVLPDlsKSERRAIV---EEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 992389469 176 W-GFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHG 212
Cdd:TIGR01184 154 QeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-199 |
3.15e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 93.93 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIalELQQLKKTY----PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVfGYDL------E 70
Cdd:PRK13634 1 MDI--TFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkkN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 71 KDVVNAKRQLGLVPQEFNFNPFE-TVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARM-LSGGMKRRLMIA 148
Cdd:PRK13634 78 KKLKPLRKKVGIVFQFPEHQLFEeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992389469 149 RALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEA 199
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDA 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-226 |
3.15e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.43 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVvnaKR 78
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIadysEAAL---RQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQE---FN---------FNPFETVQQI--VVNQAGYygverkeaidrsEKYLKQ---LDLWekRNERARMLSGGM 141
Cdd:PRK11160 415 AISVVSQRvhlFSatlrdnlllAAPNASDEALieVLQQVGL------------EKLLEDdkgLNAW--LGEGGRQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 142 KRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAEMLCRnIGIIQHGELVENTSMK 221
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFDR-ICVMDNGQIIEQGTHQ 558
|
....*
gi 992389469 222 NLLSK 226
Cdd:PRK11160 559 ELLAQ 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-226 |
3.71e-22 |
|
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: 92.60 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 6 ELQQLKKTYPG--GVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKR-QLGL 82
Cdd:cd03249 2 EFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRsQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEfnfnP--FETvqQIVVNQAgyYG------VERKEAIDRSEKYLKQLDLWEKRN----ERARMLSGGMKRRLMIARA 150
Cdd:cd03249 82 VSQE----PvlFDG--TIAENIR--YGkpdatdEEVEEAAKKANIHDFIMSLPDGYDtlvgERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 151 LMHEPKLLILDEPTAGVDIE--------LRRSMwgflkdlndKGTTIILTTHYL---EEAEmlcrNIGIIQHGELVENTS 219
Cdd:cd03249 154 LLRNPKILLLDEATSALDAEseklvqeaLDRAM---------KGRTTIVIAHRLstiRNAD----LIAVLQNGQVVEQGT 220
|
....*..
gi 992389469 220 MKNLLSK 226
Cdd:cd03249 221 HDELMAQ 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-200 |
4.19e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 96.73 E-value: 4.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvvnaKRQLGLV 83
Cdd:NF033858 1 VARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-----ARHRRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 -------PQEF--NFNP----FETVQqivvnqagYYG-------VERKEAIDRsekYLKQLDLWEKRNERARMLSGGMKR 143
Cdd:NF033858 75 cpriaymPQGLgkNLYPtlsvFENLD--------FFGrlfgqdaAERRRRIDE---LLRATGLAPFADRPAGKLSGGMKQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 144 RLMIARALMHEPKLLILDEPTAGVDIELRRSMWgflkDLNDK------GTTIILTTHYLEEAE 200
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFW----ELIDRiraerpGMSVLVATAYMEEAE 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
6.49e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.76 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTY----PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSV-------------- 64
Cdd:PRK13631 20 IILRVKNLYCVFdekqENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 65 FGYDLEKDVVNAKRQLGLVPQEFNFNPFE----TVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARM-LSG 139
Cdd:PRK13631 100 ITNPYSKKIKNFKELRRRVSMVFQFPEYQlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFgLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 140 GMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEA-----EMLCRNIG-IIQHGE 213
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVlevadEVIVMDKGkILKTGT 259
|
250 260 270
....*....|....*....|....*....|...
gi 992389469 214 LVENTSMKNLLSKLKSE-----TFILDLAAKSP 241
Cdd:PRK13631 260 PYEIFTDQHIINSTSIQvprviQVINDLIKKDP 292
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-226 |
7.64e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.94 E-value: 7.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGG-VQALRGIDLQVEAGDFYALLGPNGAGKSTtigiISSLVN-------KSSGRVSVFGYDL-EKDVV 74
Cdd:PRK13640 5 IVEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKST----ISKLINglllpddNPNSKITVDGITLtAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 75 NAKRQLGLVPQEFNfNPF--ETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALM 152
Cdd:PRK13640 81 DIREKVGIVFQNPD-NQFvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 153 HEPKLLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMlCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-236 |
9.71e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.49 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGGVQ--ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL-EKDVVNAK 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGLVPQEFNfNPF--ETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWE-KRNERARmLSGGMKRRLMIARALMHE 154
Cdd:PRK13650 81 HKIGMVFQNPD-NQFvgATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDfKEREPAR-LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIgIIQHGElVENTSMKNLLSKLKSETFI 233
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVL-VMKNGQ-VESTSTPRELFSRGNDLLQ 236
|
...
gi 992389469 234 LDL 236
Cdd:PRK13650 237 LGL 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-223 |
9.76e-22 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 94.89 E-value: 9.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSS--GRVSVFGYDLEKDVVNAKRQLGL 82
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 V--PQEFNFNPFETVQQIVV--NQAGYYG--VERKEAIDRSEKYLKQLDLWEKRNERARM-LSGGMKRRLMIARALMHEP 155
Cdd:TIGR02633 81 ViiHQELTLVPELSVAENIFlgNEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 156 KLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-194 |
1.14e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVsVFGYDLekdvvnakrQLGLVP 84
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETV---------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEF-NFNPFETVQQIVvnQAGYYGVERKEAIDrsekYLKQLDLWEKR-NERARMLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:COG0488 385 QHQeELDPDKTVLDEL--RDGAPGGTEQEVRG----YLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190
....*....|....*....|....*....|..
gi 992389469 163 PTAGVDIELRRSMWGFLKDLndKGtTIILTTH 194
Cdd:COG0488 459 PTNHLDIETLEALEEALDDF--PG-TVLLVSH 487
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-236 |
1.65e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.59 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL--EKDVVNAKRQLGL 82
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQefnfNPFETVQQIVVNQAGYYG--------VERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:PRK13644 82 VFQ----NPETQFVGRTVEEDLAFGpenlclppIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIgIIQHGELVENTSMKNLLSKLKSETFIL 234
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII-VMDRGKIVLEGEPENVLSDVSLQTLGL 233
|
..
gi 992389469 235 DL 236
Cdd:PRK13644 234 TP 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-194 |
2.23e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.60 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydlekDVVN----AKRQ 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-----RVVNelepADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLVPQEFNFNPFETVQQivvNQAgyYGVE-R---KEAID-RSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRE---NMA--YGLKiRgmpKAEIEeRVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTH 194
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTH 193
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-206 |
2.29e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKKTYPGG---VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAK- 77
Cdd:PRK11629 3 KILLQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 ----RQLGLVPQEFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK11629 83 elrnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNI 206
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-226 |
3.09e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.93 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGG-VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGL 82
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEFN-FNpfETVqqivVNQAGYYGVER--KEAIDRSEKYLKQLDLWEKRN--------ERARMLSGGMKRRLMIARAL 151
Cdd:PRK11176 422 VSQNVHlFN--DTI----ANNIAYARTEQysREQIEEAARMAYAMDFINKMDngldtvigENGVLLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 152 MHEPKLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTHYL---EEAEMlcrnIGIIQHGELVENTSMKNLLSK 226
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLstiEKADE----ILVVEDGEIVERGTHAELLAQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-226 |
5.42e-21 |
|
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: 89.21 E-value: 5.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 14 YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKR-QLGLVPQE---FNF 89
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRsMIGVVLQDtflFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 90 NPFE-------TVQQIVVNQAGyygverKEA-----IDRSEK-YLKQLdlwekrNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:cd03254 92 TIMEnirlgrpNATDEEVIEAA------KEAgahdfIMKLPNgYDTVL------GENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLNDKGTTII----LTThyLEEAEMlcrnIGIIQHGELVENTSMKNLLSK 226
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIiahrLST--IKNADK----ILVLDDGKIIEEGTHDELLAK 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-226 |
7.50e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 92.86 E-value: 7.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPG--GVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLG 81
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEfnfnPFETVQQIVVNQAgyYGVERKE------------AIDRSEKYLKQLDlwEKRNERARMLSGGMKRRLMIAR 149
Cdd:TIGR00958 559 LVGQE----PVLFSGSVRENIA--YGLTDTPdeeimaaakaanAHDFIMEFPNGYD--TEVGEKGSQLSGGQKQRIAIAR 630
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 150 ALMHEPKLLILDEPTAGVDIELRRSmwgFLKDLNDKGTTIILTTHYLEEAEMlCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQL---LQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-225 |
1.08e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 90.93 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 24 IDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG---YDLEKDV-VNA-KRQLGLVPQE---FnfnPFETV 95
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIfLPPhRRRIGYVFQEarlF---PHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 96 QQivvNQAgyYGVERKEAIDRSEKY---LKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELR 172
Cdd:COG4148 95 RG---NLL--YGRKRAPRAERRISFdevVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 173 RSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:COG4148 170 AEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-228 |
1.14e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRV----------SVFGYdleKDVVNAKRQLGLVPQ 85
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRysgdvllggrSIFNY---RDVLEFRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 86 EFNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERAR----MLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:PRK14271 109 RPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDKgTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLK 228
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-194 |
1.33e-20 |
|
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: 88.03 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGG-VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLG 81
Cdd:cd03245 2 RIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQE---FN---------FNPFETVQQIVvNQAGYYGVErkeaiDRSEKYLKQLDLweKRNERARMLSGGMKRRLMIAR 149
Cdd:cd03245 82 YVPQDvtlFYgtlrdnitlGAPLADDERIL-RAAELAGVT-----DFVNKHPNGLDL--QIGERGRGLSGGQRQAVALAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 992389469 150 ALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTH 194
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITH 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
20-214 |
1.64e-20 |
|
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: 86.72 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 20 ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLG--LVPQEfnfnpfetvqq 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGiaYVPED----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 98 ivvnqagyygvERKEAIdrsekyLKQLDLWEkrNER-ARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMW 176
Cdd:cd03215 84 -----------RKREGL------VLDLSVAE--NIAlSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 992389469 177 GFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:cd03215 145 RLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-215 |
1.75e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvVNAK---RQLG 81
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM--LSSRqlaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFNFNPFETVQQIV-------VNQAGYYGVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVaygrspwLSLWGRLSAEDNARVNQA---MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-216 |
1.95e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 91.13 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGgVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG----YDLEKDVVNA 76
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 77 KrqLGLVPQEFNFNPFETVQQIVV-----NQAGYygVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARAL 151
Cdd:PRK11288 80 G--VAIIYQELHLVPEMTVAENLYlgqlpHKGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 152 MHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-246 |
2.20e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 89.79 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 24 IDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG---YDLEKDVVNA--KRQLGLVPQEFNFNPFETVQQI 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPpeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 99 VVnqagyYGVERKEAIDRS---EKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:TIGR02142 96 LR-----YGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 176 WGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGelventsmknllsKLKSETFILDLAAKSPLPQLE 246
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDG-------------RVAAAGPIAEVWASPDLPWLA 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-225 |
2.22e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG--YDLEKDVVNAKR 78
Cdd:PRK09700 2 ATPYISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQEFN-FNPFETVQQIVVNQ------AGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARAL 151
Cdd:PRK09700 81 GIGIIYQELSvIDELTVLENLYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 152 MHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGE-----LVENTSMKNLLS 225
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSNDDIVR 239
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-225 |
2.51e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 87.63 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVN----- 75
Cdd:PRK11614 2 EKVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDwqtak 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 76 -AKRQLGLVPQEFNFNPFETVQQIVVnqAGYYGVERKEAIDRSEKYLKQLD-LWEKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK11614 77 iMREAVAIVPEGRRVFSRMTVEENLA--MGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-195 |
3.06e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTyPGGVQALRGIDLQVEAGDFYALLGPNGAGKST---TI-GIISSLVnkSSGRVSVFGYDLEKDVVN--AKR 78
Cdd:COG0396 1 LEIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLmGHPKYEV--TSGSILLDGEDILELSPDerARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQefnfNPFE----TVQ---QIVVNQAGYYGVERKEAIDRSEKYLKQLDLWE---KR--NERarmLSGGMKRRLM 146
Cdd:COG0396 78 GIFLAFQ----YPVEipgvSVSnflRTALNARRGEELSAREFLKLLKEKMKELGLDEdflDRyvNEG---FSGGEKKRNE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992389469 147 IARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHY 195
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-223 |
3.94e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.37 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSL--VNKSSGRVSVFGYDLEKDVVNAKR 78
Cdd:PRK13549 2 MEYLLEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLV--PQEFNFnpfetVQQIVVNQAGYYGVE--RKEAID------RSEKYLKQLDLWEKRNERARMLSGGMKRRLMIA 148
Cdd:PRK13549 81 RAGIAiiHQELAL-----VKELSVLENIFLGNEitPGGIMDydamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 149 RALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-195 |
6.46e-20 |
|
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: 85.66 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKST---TI-GIISSLVnkSSGRVSVFGYDLEKDVVN--AKRQLGLVPQEfnf 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTImGHPKYEV--TEGEILFKGEDITDLPPEerARLGIFLAFQY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 90 nPFEtvqqivvnqagYYGVerkeaidRSEKYLKQLdlwekrNERarmLSGGMKRRLMIARALMHEPKLLILDEPTAGVDI 169
Cdd:cd03217 86 -PPE-----------IPGV-------KNADFLRYV------NEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180
....*....|....*....|....*.
gi 992389469 170 ELRRSMWGFLKDLNDKGTTIILTTHY 195
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHY 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-216 |
9.01e-20 |
|
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: 89.36 E-value: 9.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLK---KTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTT----IGIISSLVNKSSGRVSVFGYDLEKDVVNAK 77
Cdd:COG4172 7 LSVEDLSvafGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQL-----GLVPQE--FNFNPFETV-QQIVVNQAGYYGVERKEAIDRSEKYLKQLDLwekRNERARM------LSGGMKR 143
Cdd:COG4172 87 RRIrgnriAMIFQEpmTSLNPLHTIgKQIAEVLRLHRGLSGAAARARALELLERVGI---PDPERRLdayphqLSGGQRQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 144 RLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVE 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-194 |
1.68e-19 |
|
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: 82.88 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVqALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVfgydlekdvvNAKRQLGLVP 84
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------GSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QefnfnpfetvqqivvnqagyygverkeaidrsekylkqldlwekrnerarmLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 992389469 165 AGVDIELRRSMWGFLKDLNDkgtTIILTTH 194
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-225 |
1.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.30 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYP--GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE-KDVVNAK 77
Cdd:PRK13642 1 MNKILEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLGLVPQEFNfNPF--ETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEP 155
Cdd:PRK13642 81 RKIGMVFQNPD-NQFvgATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 156 KLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRnIGIIQHGELVENTSMKNLLS 225
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDR-ILVMKAGEIIKEAAPSELFA 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-194 |
2.22e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVpQEFN----FNP 91
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV-RTFQhvrlFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 92 FETVQQIVVNQ---------------AGYYGVERkEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPK 156
Cdd:PRK11300 95 MTVIENLLVAQhqqlktglfsgllktPAFRRAES-EALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTH 194
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEH 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-214 |
2.69e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.01 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 7 LQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVsVFGYDLEKDVVNAKRQLGLVPQE 86
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAG 166
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992389469 167 VDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-230 |
3.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 11 KKTyPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE------KDVVNAKRQLGLVP 84
Cdd:PRK13645 18 KKT-PFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkiKEVKRLRKEIGLVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPF-ETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARM-LSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:PRK13645 97 QFPEYQLFqETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 163 PTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELV------ENTSMKNLLSKLKSE 230
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIsigspfEIFSNQELLTKIEID 251
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-231 |
6.46e-19 |
|
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: 83.57 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 23 GIDLQVEAGDFYALLGPNGAGKSTT----IGIISSLVNKSSGRVSVFGYDLEKDVVNAkRQLGLVPQE--FNFNPF---- 92
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDGRPLLPLSIRG-RHIATIMQNprTAFNPLftmg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 ----ETVQQ--IVVNQAGYYGVERKEAI--DRSEKYLKQLdlwekrnerARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:TIGR02770 83 nhaiETLRSlgKLSKQARALILEALEAVglPDPEEVLKKY---------PFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 165 AGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSET 231
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELrQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHET 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-216 |
7.49e-19 |
|
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: 84.11 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVsvfGYDLEKD-------VVNAK 77
Cdd:TIGR02323 4 LQVSGLSKSY-GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTA---TYIMRSGaelelyqLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQLgLVPQEFNF---NPFETVQQIVVNQAG-----------YYGVERKEAIDrsekYLKQLDLWEKR-NERARMLSGGMK 142
Cdd:TIGR02323 80 RRR-LMRTEWGFvhqNPRDGLRMRVSAGANigerlmaigarHYGNIRATAQD----WLEEVEIDPTRiDDLPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 143 RRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-199 |
1.12e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKkTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KSSGRVSVFG---YDLEKDV 73
Cdd:PRK14243 8 ETVLRTENLN-VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGknlYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 74 VNAKRQLGLVPQEFNfnPFEtvQQIVVNQA------GYYGvERKEAIDRSekyLKQLDLWEKRNERARM----LSGGMKR 143
Cdd:PRK14243 87 VEVRRRIGMVFQKPN--PFP--KSIYDNIAygarinGYKG-DMDELVERS---LRQAALWDEVKDKLKQsglsLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 144 RLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKgTTIILTTHYLEEA 199
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQA 213
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-212 |
1.32e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 84.77 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNaKRQLGLVP 84
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFNPFETVQQIVvnqaGY----YGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PRK11432 85 QSYALFPHMSLGENV----GYglkmLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEA-----EMLCRNIG-IIQHG 212
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAfavsdTVIVMNKGkIMQIG 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-194 |
2.32e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKS---SGRVSVFGYDLEKDVVnaKRQLGLVPQEFNFNPFETVQQ 97
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 98 IVVNQA------GYYGVERKEAIDrseKYLKQLDLWEKRN------ERARMLSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:TIGR00955 119 HLMFQAhlrmprRVTKKEKRERVD---EVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180
....*....|....*....|....*....
gi 992389469 166 GVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
5-242 |
2.40e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE----KDVVnakRQL 80
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyasKEVA---RRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVNqaGYYGVE------RKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVAR--GRYPHQplftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSE--- 230
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIEriy 241
|
250
....*....|....*.
gi 992389469 231 ----TFILDLAAKSPL 242
Cdd:PRK10253 242 glrcMIIDDPVAGTPL 257
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-224 |
2.91e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 85.18 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL-GLV 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFiNYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEfnfnPFETVQQIVVNQagYYGVERKEAIDrseKYLKQLDLWEKRNERARM--------------LSGGMKRRLMIAR 149
Cdd:TIGR01193 554 PQE----PYIFSGSILENL--LLGAKENVSQD---EIWAACEIAEIKDDIENMplgyqtelseegssISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 150 ALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKgtTIILTTHYLEEAEMlCRNIGIIQHGELVENTSMKNLL 224
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-223 |
3.52e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 3.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYPGgVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVV-NAKRQ 79
Cdd:PRK10762 1 MQALLQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG----KEVTfNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 -----LGLVPQEFNFNPFETVQQIV------VNQAGyyGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIA 148
Cdd:PRK10762 76 sqeagIGIIHQELNLIPQLTIAENIflgrefVNRFG--RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 149 RALMHEPKLLILDEPT-AGVDIElRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:PRK10762 154 KVLSFESKVIIMDEPTdALTDTE-TESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-196 |
4.35e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.24 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLK---KTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSsGRVSVFGYDLEKDVVN-AKRQL 80
Cdd:PRK09473 13 LDVKDLRvtfSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSATFNGREILNlPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQE-----F-----NFNPFETV-QQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRnERARM----LSGGMKRRL 145
Cdd:PRK09473 92 NKLRAEqismiFqdpmtSLNPYMRVgEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEAR-KRMKMypheFSGGMRQRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992389469 146 MIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYL 196
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDL 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-168 |
4.41e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 82.06 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKT-YPGGV---QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAK--- 77
Cdd:COG1101 2 LELKNLSKTfNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KDVTKLPeyk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 --RQLGLVPQefnfNPFE------TVQQivvNQAGYY----------GVERKEaIDRSEKYLKQLDL-WEKR-NERARML 137
Cdd:COG1101 78 raKYIGRVFQ----DPMMgtapsmTIEE---NLALAYrrgkrrglrrGLTKKR-RELFRELLATLGLgLENRlDTKVGLL 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 992389469 138 SGGmkRR-----LMiarALMHEPKLLILDEPTAGVD 168
Cdd:COG1101 150 SGG--QRqalslLM---ATLTKPKLLLLDEHTAALD 180
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-216 |
4.59e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 26 LQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdVVNA------KRQLGLVPQEFNFNPFETVQQIV 99
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK-ISDAelrevrRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 100 VNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFL 179
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 992389469 180 KDLNDKGT-TIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK10070 208 VKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
5-214 |
4.60e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 81.36 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPG--GVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLG 81
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEfnfnPFETVQQIVVNQAgyYGV------ERKEAIDRSEKY----LKQLDLWEKRNERARMLSGGMKRRLMIARAL 151
Cdd:cd03248 92 LVGQE----PVLFARSLQDNIA--YGLqscsfeCVKEAAQKAHAHsfisELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 152 MHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKgTTIILTTHYLEEAEMlCRNIGIIQHGEL 214
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-196 |
4.87e-18 |
|
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: 80.05 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLV 83
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEfnfnpfetvqqivvnqagyygverkeaidrseKYLKQLDLwekRNERARMLSGGMKRRLMIARALMHEPKLLILDEP 163
Cdd:cd03247 81 NQR--------------------------------PYLFDTTL---RNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190
....*....|....*....|....*....|....
gi 992389469 164 TAGVDIELRRSMWG-FLKDLNDKgtTIILTTHYL 196
Cdd:cd03247 126 TVGLDPITERQLLSlIFEVLKDK--TLIWITHHL 157
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-227 |
5.53e-18 |
|
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: 84.08 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTY----PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVN----- 75
Cdd:TIGR03269 280 IKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKpgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 76 ---AKRQLGLVPQEFNFNPFETV-------------QQIVVNQAGY----YGVERKEAIDRSEKYLKQldlwekrnerar 135
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPHRTVldnlteaiglelpDELARMKAVItlkmVGFDEEKAEEILDKYPDE------------ 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 136 mLSGGMKRRLMIARALMHEPKLLILDEPTAGVD-IELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:TIGR03269 428 -LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|...
gi 992389469 215 VENTSMKNLLSKL 227
Cdd:TIGR03269 507 VKIGDPEEIVEEL 519
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-202 |
6.26e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.62 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KSSGRVSVFGYDLEKDVVNA---KRQLGLVPQEFNFNPF 92
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRVNLnrlRRQVSMVHPKPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 ETVQQIVvnqagyYGVE------RKEAIDRSEKYLKQLDLWE----KRNERARMLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:PRK14258 103 SVYDNVA------YGVKivgwrpKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992389469 163 PTAGVDIELRRSMWGFLKDLNDKGT-TIILTTHYLEEAEML 202
Cdd:PRK14258 177 PCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRL 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
1.11e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 80.74 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSvfgYDLEKDVV-------NAK 77
Cdd:PRK11701 7 LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH---YRMRDGQLrdlyalsEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 78 RQL------GLVPQefnfNPFETVQQIVvnQAG-------------YYGVERKEAIDrsekYLKQLDLWEKR-NERARML 137
Cdd:PRK11701 83 RRRllrtewGFVHQ----HPRDGLRMQV--SAGgnigerlmavgarHYGDIRATAGD----WLERVEIDAARiDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 138 SGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-221 |
1.28e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.92 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGgVQALRGIDLQVEAGDFYALLGPNGAGKSTtigiissLVNKSSGrVSVFG-YDLE----------KDv 73
Cdd:NF040905 2 LEMRGITKTFPG-VKALDDVNLSVREGEIHALCGENGAGKST-------LMKVLSG-VYPHGsYEGEilfdgevcrfKD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 74 VNAKRQLGLV--PQEFNFNPFETVQQ--IVVNQAGYYGV-ERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIA 148
Cdd:NF040905 72 IRDSEALGIViiHQELALIPYLSIAEniFLGNERAKRGViDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 149 RALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMK 221
Cdd:NF040905 152 KALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCR 224
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-247 |
1.57e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.49 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQlkktypGGVQALRGIDLQVEAGDFYALLGPNGAGKS----TTIGIISSLVNKSSGRVSVFGYDLEKDVVNA 76
Cdd:COG4170 9 LTIEIDTPQ------GRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 77 KRQL-----GLVPQEFN--FNPFETV-QQIvvnqagyygverKEAIDRSEkyLKQlDLWEKRNERAR------------- 135
Cdd:COG4170 83 RRKIigreiAMIFQEPSscLDPSAKIgDQL------------IEAIPSWT--FKG-KWWQRFKWRKKraiellhrvgikd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 136 ----M------LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLND-KGTTIILTTHYLEEAEMLCR 204
Cdd:COG4170 148 hkdiMnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWAD 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 205 NIGIIQHGELVENTSMKNLLSK---------LKS-ETFILDLAAKSPLPQLEG 247
Cdd:COG4170 228 TITVLYCGQTVESGPTEQILKSphhpytkalLRSmPDFRQPLPHKSRLNTLPG 280
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
2.92e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.39 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVsvfgydlekdVVNAKRQL 80
Cdd:PRK09544 1 MTSLVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFE--TVQQIVVNQAGYygveRKEAIDRSEKYLKQLDLWEKRNERarmLSGGMKRRLMIARALMHEPKLL 158
Cdd:PRK09544 70 GYVPQKLYLDTTLplTVNRFLRLRPGT----KKEDILPALKRVQAGHLIDAPMQK---LSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 159 ILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYL-----EEAEMLCRN 205
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLhlvmaKTDEVLCLN 195
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-216 |
5.47e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.88 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYP----------GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVnKSSGRVSVFGYDL----E 70
Cdd:COG4172 276 LEARDLKVWFPikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLdglsR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 71 KDVVNAKRQLGLVPQE-FN-FNPFETVQQIV-----VNQAGYYGVERKEAIDRSekyLKQLDLweKRNERARM---LSGG 140
Cdd:COG4172 355 RALRPLRRRMQVVFQDpFGsLSPRMTVGQIIaeglrVHGPGLSAAERRARVAEA---LEEVGL--DPAARHRYpheFSGG 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 141 MKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-216 |
6.49e-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: 81.00 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSL--VNKSSGRV-------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 63 ---SVFGYDLEKDVV-----------NAKRQLGLVPQE-FNFNPFETVQQIVVN---QAGYYGverKEAIDRSEKYLKQL 124
Cdd:TIGR03269 80 epcPVCGGTLEPEEVdfwnlsdklrrRIRKRIAIMLQRtFALYGDDTVLDNVLEaleEIGYEG---KEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 125 DLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLC 203
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|...
gi 992389469 204 RNIGIIQHGELVE 216
Cdd:TIGR03269 237 DKAIWLENGEIKE 249
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-196 |
6.98e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 79.62 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKTYP---------GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK 71
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 72 ----DVVNAKRQLGLVPQefN----FNPFETVQQIVvnqagyygvERKEAI----DRSEKYLKQLDLWEK---RNERA-- 134
Cdd:PRK11308 82 adpeAQKLLRQKIQIVFQ--NpygsLNPRKKVGQIL---------EEPLLIntslSAAERREKALAMMAKvglRPEHYdr 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 135 --RMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYL 196
Cdd:PRK11308 151 ypHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDL 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-168 |
9.95e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 79.01 E-value: 9.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYP----------GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVV 74
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG----QDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 75 NAK--------RQLGLVPQefnfNPFE------TVQQIVVNQAGYYGVE-RKEAIDRSEKYLKQLDLwekRNERAR---- 135
Cdd:COG4608 84 GLSgrelrplrRRMQMVFQ----DPYAslnprmTVGDIIAEPLRIHGLAsKAERRERVAELLELVGL---RPEHADryph 156
|
170 180 190
....*....|....*....|....*....|...
gi 992389469 136 MLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-215 |
1.54e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.74 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE---KDVVNAKRQLGLVPQEFNFNPFET- 94
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskRGLLALRQQVATVFQDPEQQIFYTd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 95 VQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992389469 175 MWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-216 |
1.70e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.75 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYP----------GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNkSSGRVSVFGYDLE---- 70
Cdd:PRK15134 276 LDVEQLQVAFPirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHnlnr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 71 KDVVNAKRQLGLVPQEFN--FNPFETVQQIV-----VNQAGYYGVERKEaidRSEKYLKQLDL-WEKRNERARMLSGGMK 142
Cdd:PRK15134 355 RQLLPVRHRIQVVFQDPNssLNPRLNVLQIIeeglrVHQPTLSAAQREQ---QVIAVMEEVGLdPETRHRYPAEFSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 143 RRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-197 |
1.81e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 77.30 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGII----SSLVnkSSGRVSVFGYDLEKDVVNAKRQLGL---------VPQEF 87
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEV--TSGTILFKGQDLLELEPDERARAGLflafqypeeIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 NFNPFETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERA--RMLSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:TIGR01978 94 NLEFLRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSvnEGFSGGEKKRNEILQMALLEPKLAILDEIDS 173
|
170 180 190
....*....|....*....|....*....|..
gi 992389469 166 GVDIELRRSMWGFLKDLNDKGTTIILTTHYLE 197
Cdd:TIGR01978 174 GLDIDALKIVAEGINRLREPDRSFLIITHYQR 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-215 |
2.53e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLkkTYPGGVqalRGIDLQVEAGD---FYALLGpngAGKSTTIGIISSLVNKSSGRVSVFGYDLE-KDVVNAKR 78
Cdd:COG1129 255 VVLEVEGL--SVGGVV---RDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 Q-LGLVP---QEFNFNPFETVQQ-IVVNQAGYYG----VERKEAIDRSEKYLKQLDLweK---RNERARMLSGGMKRRLM 146
Cdd:COG1129 327 AgIAYVPedrKGEGLVLDLSIREnITLASLDRLSrgglLDRRRERALAEEYIKRLRI--KtpsPEQPVGNLSGGNQQKVV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 147 IARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG1129 405 LAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-225 |
3.09e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKSTTIGII-----SSLVNKSSGRVSVFGYDLEKDVVNAKR-----QLGLVPQE-- 86
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSIlrllpSPPVVYPSGDIRFHGESLLHASEQTLRgvrgnKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNFNPFETVQ-QIVVNQAGYYGVERKEAidRSEkYLKQLDLWEKRNERARM------LSGGMKRRLMIARALMHEPKLLI 159
Cdd:PRK15134 103 VSLNPLHTLEkQLYEVLSLHRGMRREAA--RGE-ILNCLDRVGIRQAAKRLtdyphqLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 160 LDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-202 |
3.96e-16 |
|
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: 75.20 E-value: 3.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 20 ALRGIDLQVEAGDFYALLGPNGAGKSTtigIISSL---VNKSSGRVSVFGydlekdvvnakrQLGLVPQEfnfnPF---E 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPG------------SIAYVSQE----PWiqnG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 94 TVQQ-IV----VNQAGYygverKEAIDRSEkyLKQ-LDLWEKRN-----ERARMLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:cd03250 81 TIREnILfgkpFDEERY-----EKVIKACA--LEPdLEILPDGDlteigEKGINLSGGQKQRISLARAVYSDADIYLLDD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 992389469 163 PTAGVDIELRRSMW-----GFLKDlndkGTTIILTTH---YLEEAEML 202
Cdd:cd03250 154 PLSAVDAHVGRHIFencilGLLLN----NKTRILVTHqlqLLPHADQI 197
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-234 |
4.89e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.77 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 25 DLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDlEKDVVNAKRQLGLVPQEFNFNPFETVQQIV---VN 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIglgLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 102 QAGYYGVERKEAIdrsEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKD 181
Cdd:PRK10771 98 PGLKLNAAQREKL---HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 182 L-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLKSETFIL 234
Cdd:PRK10771 175 VcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALL 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-232 |
9.08e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.09 E-value: 9.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 15 PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGLVPQ-------- 85
Cdd:PLN03232 1246 PGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQspvlfsgt 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 86 -EFNFNPFETVqqivvNQAGYY-GVER---KEAIDRSEkylkqLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:PLN03232 1326 vRFNIDPFSEH-----NDADLWeALERahiKDVIDRNP-----FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 161 DEPTAGVDIELRRSMWGFLKDlNDKGTTIILTTHYLEEAeMLCRNIGIIQHGELVENTSMKNLLSKLKSETF 232
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-214 |
9.38e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 9.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 22 RGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLV---------------PQE 86
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrqssglyldaPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNfnpfetVQQIVVNQAGYYGVERKEAiDRSEKYLKQLDL-WEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:PRK15439 360 WN------VCALTHNRRGFWIKPAREN-AVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992389469 166 GVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-216 |
9.81e-16 |
|
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: 74.45 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 15 PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGLVPQE------- 86
Cdd:cd03244 14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDpvlfsgt 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 --FNFNPFETVQQIVVNQAgyygVERKEAIDRSEKYLKQLDLweKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03244 94 irSNLDPFGEYSDEELWQA----LERVGLKEFVESLPGGLDT--VVEEGGENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 992389469 165 AGVDIELRRSMWGFLKDlNDKGTTIILTTHYLeEAEMLCRNIGIIQHGELVE 216
Cdd:cd03244 168 ASVDPETDALIQKTIRE-AFKDCTVLTIAHRL-DTIIDSDRILVLDKGRVVE 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-194 |
1.29e-15 |
|
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: 77.10 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQA-LRGIDLQVEAGDFYALLGPNGAGKST----TIGIISSlvnkSSGRVSVFGYDLEK-DVVNAKR 78
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWPP----TAGSVRLDGADLSQwDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 QLGLVPQEFNFnpFE-TVQQ-I----------VVNQAGYYGVerKEAIDRSEK-YLKQLDlwekrnERARMLSGGMKRRL 145
Cdd:COG4618 407 HIGYLPQDVEL--FDgTIAEnIarfgdadpekVVAAAKLAGV--HEMILRLPDgYDTRIG------EGGARLSGGQRQRI 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 992389469 146 MIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-225 |
2.37e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKT--YPGG------VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE-KDVVN 75
Cdd:PRK15112 5 LEVRNLSKTfrYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 76 AKRQLGLVPQE--FNFNPFETVQQIV-----VNqAGYYGVERKEAIDRSekyLKQLDLW-EKRNERARMLSGGMKRRLMI 147
Cdd:PRK15112 85 RSQRIRMIFQDpsTSLNPRQRISQILdfplrLN-TDLEPEQREKQIIET---LRQVGLLpDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 148 ARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
2.87e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGL 82
Cdd:COG3845 256 VVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 --VPQE-------------FNF-------NPFetVQQIVVNqagyygveRKEAIDRSEKYLKQLDLwekR----NERARM 136
Cdd:COG3845 336 ayIPEDrlgrglvpdmsvaENLilgryrrPPF--SRGGFLD--------RKAIRAFAEELIEEFDV---RtpgpDTPARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 137 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
12-223 |
6.50e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.77 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 12 KTYPGgVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYdlEKDVVNAKRQL----GLVPQEF 87
Cdd:PRK10982 6 KSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK--EIDFKSSKEALengiSMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 NFnpfetVQQIVVNQAGYYG--------VERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLI 159
Cdd:PRK10982 83 NL-----VLQRSVMDNMWLGryptkgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 160 LDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
14-168 |
7.32e-15 |
|
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: 74.86 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 14 YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLeKDVVNA--KRQLGLVPQE---FN 88
Cdd:COG5265 367 YDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQAslRAAIGIVPQDtvlFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 fnpfETvqqIVVNQAgyYG--------VErkEAIDRS--EKYLKQL-DLWEKR-NERARMLSGGMKRRLMIARALMHEPK 156
Cdd:COG5265 446 ----DT---IAYNIA--YGrpdaseeeVE--AAARAAqiHDFIESLpDGYDTRvGERGLKLSGGEKQRVAIARTLLKNPP 514
|
170
....*....|..
gi 992389469 157 LLILDEPTAGVD 168
Cdd:COG5265 515 ILIFDEATSALD 526
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-196 |
8.34e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 15 PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKRQLGLVPQE--FN 88
Cdd:PRK15079 31 PKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 FNPFETVQQIVVN--QAGYYGVERKEAIDRSEKYLKQLDLWEKR-NERARMLSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:PRK15079 111 LNPRMTIGEIIAEplRTYHPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190
....*....|....*....|....*....|..
gi 992389469 166 GVDIELRRSMWGFLKDLN-DKGTTIILTTHYL 196
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDL 222
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-216 |
8.93e-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: 71.67 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTY-PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGL 82
Cdd:cd03369 7 IEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQE---------FNFNPFETvqqivvnqagYYGVERKEAIDRSEKYLKqldlwekrnerarmLSGGMKRRLMIARALMH 153
Cdd:cd03369 87 IPQDptlfsgtirSNLDPFDE----------YSDEEIYGALRVSEGGLN--------------LSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDLNdKGTTIILTTHYLEEAeMLCRNIGIIQHGELVE 216
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-194 |
1.16e-14 |
|
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: 70.26 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVfgydlekdvvNAKRQLGLVP 84
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM----------PEGEDLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNFnPFETVQQIVVnqagyygverkeaidrsekYLkqldlWEkrneraRMLSGGMKRRLMIARALMHEPKLLILDEPT 164
Cdd:cd03223 71 QRPYL-PLGTLREQLI-------------------YP-----WD------DVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|
gi 992389469 165 AGVDIELRRSMwgfLKDLNDKGTTIILTTH 194
Cdd:cd03223 120 SALDEESEDRL---YQLLKELGITVISVGH 146
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-223 |
1.24e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.12 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK---DVVNAKRQ------------LGL 82
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRrsrQVIELSEQsaaqmrhvrgadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQE--FNFNPFETV-QQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERAR---MLSGGMKRRLMIARALMHEPK 156
Cdd:PRK10261 109 IFQEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNL 223
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
1.72e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.73 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSttigiisSLVN------KSSGRVSVFGYDL-EKDVV 74
Cdd:PRK11174 347 PVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKT-------SLLNallgflPYQGSLKINGIELrELDPE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 75 NAKRQLGLV---PQEF------NF---NPFETVQQIvvNQAgyygVERKEAIDRSEKYLKQLDLWEKrnERARMLSGGMK 142
Cdd:PRK11174 420 SWRKHLSWVgqnPQLPhgtlrdNVllgNPDASDEQL--QQA----LENAWVSEFLPLLPQGLDTPIG--DQAAGLSVGQA 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 143 RRLMIARALMHEPKLLILDEPTAGVDielRRSMWGFLKDLND--KGTTIILTTHYLEEAEMlCRNIGIIQHGELVE 216
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLD---AHSEQLVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ 563
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-202 |
1.82e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE-KDVVNAKRQLGlvPQEFnFNPFET 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG--HRNA-MKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 95 VQQIVVNQAGYYGvERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PRK13539 90 VAENLEFWAAFLG-GEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180 190
....*....|....*....|....*....|.
gi 992389469 175 MWGFLKDLNDKGTTIILTTHY---LEEAEML 202
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-194 |
2.75e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVPQEFNFNPFETVQQivv 100
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 101 nqAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLK 180
Cdd:PRK13540 94 --NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....
gi 992389469 181 DLNDKGTTIILTTH 194
Cdd:PRK13540 172 EHRAKGGAVLLTSH 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-194 |
3.19e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 25 DLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSvfgydLEKDVVNAKRQLGlVPQEFNFNPFETVQQIVVNQAG 104
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII-----YEQDLIVARLQQD-PPRNVEGTVYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 105 ----YYGVERKEAIDRSEKYLKQL----------DLW--EKR------------NERARMLSGGMKRRLMIARALMHEPK 156
Cdd:PRK11147 97 ylkrYHDISHLVETDPSEKNLNELaklqeqldhhNLWqlENRinevlaqlgldpDAALSSLSGGWLRKAALGRALVSNPD 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 992389469 157 LLILDEPTAGVDIELRRSMWGFLKDLndKGtTIILTTH 194
Cdd:PRK11147 177 VLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISH 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-194 |
4.21e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.28 E-value: 4.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 7 LQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVsvfgydlekdVVNAKRQLGLVPQE 86
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA----------RPQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNFNPFETVQQIVVNQAGyygvERKEAIDR----SEKY--------------------LKQLDLW--EKRNERA----RM 136
Cdd:TIGR03719 77 PQLDPTKTVRENVEEGVA----EIKDALDRfneiSAKYaepdadfdklaaeqaelqeiIDAADAWdlDSQLEIAmdalRC 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 137 ---------LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE----LRRsmwgFLKDLndKGtTIILTTH 194
Cdd:TIGR03719 153 ppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLER----HLQEY--PG-TVVAVTH 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-226 |
5.16e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 2 TIALELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISS--LVNKSSGRVSVFGYDLEKDVVNAKRQ 79
Cdd:CHL00131 5 KPILEIKNLHASV-NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLvpqefnFNPFETVQQIV-VNQAGY----YGVERKEaidRSEKYLKQLDLWEKRNERARML---------------SG 139
Cdd:CHL00131 84 LGI------FLAFQYPIEIPgVSNADFlrlaYNSKRKF---QGLPELDPLEFLEIINEKLKLVgmdpsflsrnvnegfSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 140 GMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRN-IGIIQHGELVE-- 216
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDyVHVMQNGKIIKtg 234
|
250
....*....|
gi 992389469 217 NTSMKNLLSK 226
Cdd:CHL00131 235 DAELAKELEK 244
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
16-206 |
5.40e-14 |
|
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: 69.44 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLGLVPQEfnfNPFETV 95
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHA---PGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 96 QQIVVNQAGYYGVERKEAIdrsEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:cd03231 88 LSVLENLRFWHADHSDEQV---EEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|..
gi 992389469 176 WGFLKDLNDKGTTIILTTHY-LEEAEMLCRNI 206
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTHQdLGLSEAGAREL 196
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-224 |
5.90e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.05 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 13 TYPGGVQ-ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKR-QLGLVPQE-FNF 89
Cdd:PRK10789 322 TYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRsRLAVVSQTpFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 90 -----------NPFETVQQIvvNQAGYYGVERKEAIDRSEKYLKQLdlwekrNERARMLSGGMKRRLMIARALMHEPKLL 158
Cdd:PRK10789 402 sdtvannialgRPDATQQEI--EHVARLASVHDDILRLPQGYDTEV------GERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992389469 159 ILDEPTAGVDielRRSMWGFLKDLND--KGTTIILTTHYLE---EAEmlcrNIGIIQHGELVENTSMKNLL 224
Cdd:PRK10789 474 ILDDALSAVD---GRTEHQILHNLRQwgEGRTVIISAHRLSaltEAS----EILVMQHGHIAQRGNHDQLA 537
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-225 |
6.75e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.58 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 25 DLQVEAGDFYALLGPNGAGKSttigiisSLVNKSSGRVSVFGYDLEKDVVNAKR----QL-GLVPQEFNFN------PFE 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKS-------ALARALAGELPLLSGERQSQFSHITRlsfeQLqKLVSDEWQRNntdmlsPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 94 -----TVQQIVVNQAgyygveRKEAidRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:PRK10938 96 ddtgrTTAEIIQDEV------KDPA--RCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 169 IELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-194 |
7.38e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSS--GRVSVFGYDLEKDVVnakRQLGLVPQEFNFNPFETVQQI 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL---KRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 99 VVNQAGYY---GVERKEAIDRSEKYLKQLDLWEKRN-----ERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 170
Cdd:PLN03211 161 LVFCSLLRlpkSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180
....*....|....*....|....
gi 992389469 171 LRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-200 |
8.59e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.05 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKST----TIGIISSLVNkSSGRVSVFGYDLekDVVNA-KRQ 79
Cdd:COG4136 2 LSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFS-ASGEVLLNGRRL--TALPAeQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LGLVPQEFNFNPFETVQQivvNQA-----GYYGVERKEAIdrsEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHE 154
Cdd:COG4136 78 IGILFQDDLLFPHLSVGE---NLAfalppTIGRAQRRARV---EQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 992389469 155 PKLLILDEPTAGVDIELRRSMWGFLKD-LNDKGTTIILTTHYLEEAE 200
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEEDAP 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-198 |
1.02e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 24 IDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFG---YDLEKDVVNA--KRQLGLVPQEFNFNPFETVQqi 98
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGICLPpeKRRIGYVFQDARLFPHYKVR-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 99 vvnqaG--YYGVERKEAiDRSEKYLKQLDLwEKRNER-ARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:PRK11144 95 -----GnlRYGMAKSMV-AQFDKIVALLGI-EPLLDRyPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167
|
170 180
....*....|....*....|....
gi 992389469 176 WGFLKDL-NDKGTTIILTTHYLEE 198
Cdd:PRK11144 168 LPYLERLaREINIPILYVSHSLDE 191
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-216 |
1.07e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNkSSGRVSV----F-GYDLEKDVVNAKRQL-----GLVPQE-- 86
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMAekleFnGQDLQRISEKERRNLvgaevAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNFNP-----FETVQQIVVNQAGYYGVERKEAIDrsekYLKQL---DLWEKRNERARMLSGGMKRRLMIARALMHEPKLL 158
Cdd:PRK11022 100 TSLNPcytvgFQIMEAIKVHQGGNKKTRRQRAID----LLNQVgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 159 ILDEPTAGVDIELRRSMWGFLKDLNDK-GTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-236 |
1.12e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.78 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 20 ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRV-----SVFGYDLEKdvvnAKRQLGLVPQEFNfNPF-- 92
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEK----LRKHIGIVFQNPD-NQFvg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 ETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELR 172
Cdd:PRK13648 99 SIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 173 RSMWGFLKDLN-DKGTTIILTTHYLEEAeMLCRNIGIIQHGELVENTSMKNLLSKLKSETFI-LDL 236
Cdd:PRK13648 179 QNLLDLVRKVKsEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEELTRIgLDL 243
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-194 |
1.26e-13 |
|
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: 68.15 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL-------GLVPQ--- 85
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpGLKPElsa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 86 ----EFnFNPFETVQQIVVNQAgyygverkeaidrsekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:TIGR01189 91 lenlHF-WAAIHGGAQRTIEDA-----------------LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 992389469 162 EPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-194 |
3.20e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.88 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKST---------TIGIIsslvnksSGRVSVFGYDLEKdvvNAKRQLGLVPQEFNF 89
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTlldvlagrkTAGVI-------TGEILINGRPLDK---NFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 90 NPFETVqqivvnqagyygverKEAIDRSEKYlkqldlwekrneraRMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDI 169
Cdd:cd03232 91 SPNLTV---------------REALRFSALL--------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*
gi 992389469 170 ELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
5-216 |
3.47e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 68.19 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVqaLRGIDLQVEAGDFYALLGPNGAGKSTT----IGIISSLVNKSSGRVSVFGYDLEKDVVNAkRQL 80
Cdd:PRK10418 5 IELRNIALQAAQPL--VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCALRG-RKI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQefN----FNPFETVQQIVVNQAGYYGVERKEAidRSEKYLKQLDLwekrNERARML-------SGGMKRRLMIAR 149
Cdd:PRK10418 82 ATIMQ--NprsaFNPLHTMHTHARETCLALGKPADDA--TLTAALEAVGL----ENAARVLklypfemSGGMLQRMMIAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 150 ALMHEPKLLILDEPTAGVDIELRRSMWGFLKDL-NDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-194 |
7.18e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVQALRGIDLQVEAGDfyALL--GPNGAGKSTTIGIISSLVNKSSGRVsvfgydlekdVVNAKRQLG 81
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI----------ARPAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEfNFNPFETVQQIVV--NQAGYYGVER-KEAIDRS--EKYLKQLDL---WEKRnerarmLSGGMKRRLMIARALMH 153
Cdd:COG4178 430 FLPQR-PYLPLGTLREALLypATAEAFSDAElREALEAVglGHLAERLDEeadWDQV------LSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 992389469 154 EPKLLILDEPTAGVDIELRRSMWGFLKDlNDKGTTIILTTH 194
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-194 |
1.65e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 7 LQQLKKTYPGGVQALRGIDLQveagdFY-----ALLGPNGAGKSTTIGIISSLVNKSSGRVSVF-GYdlekdvvnakrQL 80
Cdd:PRK11819 9 MNRVSKVVPPKKQILKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGI-----------KV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 81 GLVPQEFNFNPFETVQQIVVNqagyyGV-ERKEAIDR----SEKY--------------------LKQLDLW--EKRNER 133
Cdd:PRK11819 73 GYLPQEPQLDPEKTVRENVEE-----GVaEVKAALDRfneiYAAYaepdadfdalaaeqgelqeiIDAADAWdlDSQLEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 134 ArM--------------LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE----LRRsmwgFLKDLndKGtTIILTTH 194
Cdd:PRK11819 148 A-MdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLEQ----FLHDY--PG-TVVAVTH 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-196 |
5.30e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVnKSSGRVSVFGYDLEK-DVVNAKRQLGLVPQEFNFNPFETVQQIV 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 100 vnQAGYYGVERKEAIDRSEKYL-KQLDLWEKRNERARMLSGGMKRRLMIARALMH-------EPKLLILDEPTAGVDIEL 171
Cdd:COG4138 91 --ALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|....*
gi 992389469 172 RRSMWGFLKDLNDKGTTIILTTHYL 196
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDL 193
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-195 |
4.17e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.12 E-value: 4.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTtigIISSLVNK-----SSGRVSVFGYDLekdvvnakrqLGLVPQE--------- 86
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKST---LSATLAGRedyevTGGTVEFKGKDL----------LELSPEDragegifma 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNFnPFET-------VQQIVVNQAGYYgvERKEAIDR------SEKYLKQLDLWEKRNERARML--SGGMKRRLMIARAL 151
Cdd:PRK09580 84 FQY-PVEIpgvsnqfFLQTALNAVRSY--RGQEPLDRfdfqdlMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 992389469 152 MHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHY 195
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-216 |
6.53e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.88 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 22 RGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE--KDVVNAKRQLGLVPQ---EFNFNP-FETV 95
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITEsrrDNGFFPnFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 96 QQIVVNQ----AGYYGV--------ERKEAIDRSEKY-LKQLDLWEKRNErarmLSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:PRK09700 360 QNMAISRslkdGGYKGAmglfhevdEQRTAENQRELLaLKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 163 PTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-170 |
6.77e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 6.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 3 IALELQQLKKTYPGGvQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVfGYDLEKDVVNAKRQlgl 82
Cdd:PRK11147 318 IVFEMENVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRA--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 vpqefNFNPFETV--------QQIVVNqagyyGVERkeaidRSEKYLKQLDLWEKRnerARM----LSGGMKRRLMIARA 150
Cdd:PRK11147 393 -----ELDPEKTVmdnlaegkQEVMVN-----GRPR-----HVLGYLQDFLFHPKR---AMTpvkaLSGGERNRLLLARL 454
|
170 180
....*....|....*....|
gi 992389469 151 LMHEPKLLILDEPTAGVDIE 170
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVE 474
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-170 |
1.87e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVqALRGIDLQVEAGDFYALLGPNGAGKSTtigIISSLVNkssgrvsvfgyDLEKDVvnakrqlGLV 83
Cdd:PRK15064 319 ALEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTT---LLRTLVG-----------ELEPDS-------GTV 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPfetvqqivvnqaGYYgverkeAIDRSEKYLKQLDL--W------EKRNERA------RML------------ 137
Cdd:PRK15064 377 KWSENANI------------GYY------AQDHAYDFENDLTLfdWmsqwrqEGDDEQAvrgtlgRLLfsqddikksvkv 438
|
170 180 190
....*....|....*....|....*....|....
gi 992389469 138 -SGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 170
Cdd:PRK15064 439 lSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-229 |
2.09e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEK-DVVNAKRQLGLVPQ---------EFNFN 90
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQapvlfsgtvRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 91 PFETVqqivvNQAGYY-GVER---KEAIDRSEkylkqLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAG 166
Cdd:PLN03130 1335 PFNEH-----NDADLWeSLERahlKDVIRRNS-----LGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 167 VDIelrRSMWGFLKDLND--KGTTIILTTHYLEEAeMLCRNIGIIQHGELVENTSMKNLLSKLKS 229
Cdd:PLN03130 1405 VDV---RTDALIQKTIREefKSCTMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-215 |
3.24e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.42 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvVNAK---RQLGLVPQEFNFNPFETVQQ 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES--WSSKafaRKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 98 IVV-------NQAGYYGVERKEaidRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 170
Cdd:PRK10575 105 LVAigrypwhGALGRFGAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 992389469 171 LRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK10575 182 HQVDVLALVHRLSqERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-194 |
3.41e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 1 MTIALELQQLKKT--YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKR 78
Cdd:PRK10247 1 MQENSPLLQLQNVgyLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 79 Q----LGLVPQEFNfnpfETVQQivvNQAGYYGVeRKEAIDRsEKYLKQLDLWEKRNE----RARMLSGGMKRRLMIARA 150
Cdd:PRK10247 81 QqvsyCAQTPTLFG----DTVYD---NLIFPWQI-RNQQPDP-AIFLDDLERFALPDTiltkNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTH 194
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTH 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-194 |
5.41e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.43 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKST----TIGIISSLVNKSSGRVSVFGYDLEKDVVNAkrqlglVPQEFNFNpfETVQ 96
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTllrlLAGALKGTPVAGCVDVPDNQFGREASLIDA------IGRKGDFK--DAVE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 97 qiVVNQAGYygverkeaidrSEKYlkqldLWEKrneRARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL-RRSM 175
Cdd:COG2401 118 --LLNAVGL-----------SDAV-----LWLR---RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTaKRVA 176
|
170
....*....|....*....
gi 992389469 176 WGFLKDLNDKGTTIILTTH 194
Cdd:COG2401 177 RNLQKLARRAGITLVVATH 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-172 |
8.22e-10 |
|
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: 58.19 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 13 TYPGGVQALRGIDLQVEAGDFY-----ALLGPNGAGKSTTIGIISSLVNKSSGRVsvfgyDLEKDVVNAKrqlglvPQEF 87
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDTVSYK------PQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 NFNPFETVQQI---VVNQAG---YYGVErkeaidrsekYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03237 71 KADYEGTVRDLlssITKDFYthpYFKTE----------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170
....*....|.
gi 992389469 162 EPTAGVDIELR 172
Cdd:cd03237 141 EPSAYLDVEQR 151
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-197 |
1.94e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 56.57 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 13 TYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRV--SVFGYDLEKDVVNAKRQLGLV------P 84
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRYSVayaaqkP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEFNfnpfETVQQIVVNQAGYyGVERKEAIDRSEKYLKQLDLW-----EKRNERARMLSGGMKRRLMIARALMHEPKLLI 159
Cdd:cd03290 89 WLLN----ATVEENITFGSPF-NKQRYKAVTDACSLQPDIDLLpfgdqTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 992389469 160 LDEPTAGVDIELRRSMW--GFLKDLNDKGTTIILTTHYLE 197
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-225 |
1.97e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 12 KTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSlVNKSSGRVSV--FGY---DLEKDVVNAKRQL-----G 81
Cdd:PRK15093 14 KTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTAdrMRFddiDLLRLSPRERRKLvghnvS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 82 LVPQEFN--FNPFETV-QQIVVNQAG--YYGVERKEAIDRSEKYLKQLDLWEKRNERARM------LSGGMKRRLMIARA 150
Cdd:PRK15093 93 MIFQEPQscLDPSERVgRQLMQNIPGwtYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMrsfpyeLTEGECQKVMIAIA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 151 LMHEPKLLILDEPTAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVT 248
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-216 |
2.08e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.06 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQLglvp 84
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 qeFN--FNPFETVQQIVVNQagyyGVERKEAIdrSEKYLKQLDLWEK-RNERARM----LSGGMKRRLMIARALMHEPKL 157
Cdd:PRK10522 399 --FSavFTDFHLFDQLLGPE----GKPANPAL--VEKWLERLKMAHKlELEDGRIsnlkLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 158 LILDEPTAGVDIELRRSMWG-FLKDLNDKGTTIILTTH---YLEEAEMLCRnigiIQHGELVE 216
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHddhYFIHADRLLE----MRNGQLSE 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
52-194 |
2.18e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 52 SSLVNKSSGRVSVFGYDL-EKDVVNAKRQLGLVPQE---FNFNPFETVQqivvnqagyYGVE--RKEAIDRSEKYLKQLD 125
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEpmlFNMSIYENIK---------FGKEdaTREDVKRACKFAAIDE 1339
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 126 LWEKRNER--------ARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKG-TTIILTTH 194
Cdd:PTZ00265 1340 FIESLPNKydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAH 1417
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-194 |
2.27e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 15 PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVnkssgrvSVFGYDLEKDvvnAKRQLGLVPQEfnfnPFET 94
Cdd:TIGR00954 462 PNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-------PVYGGRLTKP---AKGKLFYVPQR----PYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 95 V----QQIVvnqagyYGVERKEAIDRS------EKYLKQLDL---------WEKRNERARMLSGGMKRRLMIARALMHEP 155
Cdd:TIGR00954 528 LgtlrDQII------YPDSSEDMKRRGlsdkdlEQILDNVQLthilereggWSAVQDWMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190
....*....|....*....|....*....|....*....
gi 992389469 156 KLLILDEPTAGVDIELRRSMWGFLKdlnDKGTTIILTTH 194
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYMYRLCR---EFGITLFSVSH 637
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-216 |
2.61e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.94 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLekDVVNA------KRQLGLVPQE--FNF 89
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI--DTLSPgklqalRRDIQFIFQDpyASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 90 NPFETVQQIVVNQAGYYGV-ERKEAIDRSEKYLKQLDL-----WEKRNErarmLSGGMKRRLMIARALMHEPKLLILDEP 163
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlpehaWRYPHE----FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 992389469 164 TAGVDIELRRSMWGFLKDLN-DKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-226 |
3.56e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 58.00 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTY-PGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNkSSGRVSVFGYDLEKDVVNAKRQ-LGL 82
Cdd:TIGR01271 1218 MDVQGLTAKYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKaFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 83 VPQEF---------NFNPFE--TVQQI--VVNQAGYYGVerkeaidrSEKYLKQLDLweKRNERARMLSGGMKRRLMIAR 149
Cdd:TIGR01271 1297 IPQKVfifsgtfrkNLDPYEqwSDEEIwkVAEEVGLKSV--------IEQFPDKLDF--VLVDGGYVLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 150 ALMHEPKLLILDEPTAGVDIE----LRRSMWGFLKDlndkgTTIILTTHYLeEAEMLCRNIGIIQHGELVENTSMKNLLS 225
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVtlqiIRKTLKQSFSN-----CTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
.
gi 992389469 226 K 226
Cdd:TIGR01271 1441 E 1441
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
130-191 |
5.34e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 5.34e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992389469 130 RNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIIL 191
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL 450
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
137-208 |
5.82e-09 |
|
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: 54.29 E-value: 5.82e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992389469 137 LSGGMKRRLMIARALMHEPK----LLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGI 208
Cdd:cd03227 78 LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-199 |
9.01e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKS-SGRVSVFG---------YDLekdvvnaKRQLGLVP----QE 86
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGySNDLTLFGrrrgsgetiWDI-------KKHIGYVSsslhLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 87 FNFNpfETVQQIVVnqAGYY---GVERKEAiDRSEKYLKQ-LDLWEKRNERA----RMLSGGMKRRLMIARALMHEPKLL 158
Cdd:PRK10938 349 YRVS--TSVRNVIL--SGFFdsiGIYQAVS-DRQQKLAQQwLDILGIDKRTAdapfHSLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 992389469 159 ILDEPTAGVDIELRRSMWGFLKDLNDKGTTIIL-TTHYLEEA 199
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDA 465
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-194 |
1.38e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 22 RGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQL---G--------LVPQE-FNF 89
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylGhqpgikteLTALEnLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 90 NpfetvQQIvvnqAGYYGVERKEAIdrsekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEP-----T 164
Cdd:PRK13538 98 Y-----QRL----HGPGDDEALWEA------LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPftaidK 162
|
170 180 190
....*....|....*....|....*....|
gi 992389469 165 AGVDIELRRsmwgFLKDLnDKGTTIILTTH 194
Cdd:PRK13538 163 QGVARLEAL----LAQHA-EQGGMVILTTH 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-194 |
1.81e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 19 QALRGIDLQVEAGDFYALLGPNGAGKSTtigiissLVNKSSGRVSVfGYDLEKDV-VNAK-------RQLGLVPQEFNFN 90
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTT-------LLNVLAERVTT-GVITGGDRlVNGRpldssfqRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 91 PFETVQQIVVNQAgyY-----GVERKEAIDRSEKYLKQLDLwEKRNERARMLSG-GM----KRRLMIARALMHEPKLLI- 159
Cdd:TIGR00956 849 PTSTVRESLRFSA--YlrqpkSVSKSEKMEYVEEVIKLLEM-ESYADAVVGVPGeGLnveqRKRLTIGVELVAKPKLLLf 925
|
170 180 190
....*....|....*....|....*....|....*
gi 992389469 160 LDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-226 |
2.29e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 4 ALELQQLKKTYPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQlGLV 83
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ-GVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 pqefnfnpfeTVQQIVVNQAGYYGVERKEAIDRSEKYL------KQLDLWEKR---------NERARMLSGGMKRRLMIA 148
Cdd:PRK10790 419 ----------MVQQDPVVLADTFLANVTLGRDISEEQVwqaletVQLAELARSlpdglytplGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 149 RALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKgTTIILTTHYLE---EAEmlcrNIGIIQHGELVENTSMKNLLS 225
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLStivEAD----TILVLHRGQAVEQGTHQQLLA 563
|
.
gi 992389469 226 K 226
Cdd:PRK10790 564 A 564
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-169 |
2.79e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.06 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKS--------SGRVSVFGYDLEK-DVVNAKRQLGLVPQE----F 87
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAiDAPRLARLRAVLPQAaqpaF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 NFnpfeTVQQIV-------VNQAGYYGVERKEAIDRSEKyLKQLDLWEKRNerARMLSGGMKRRLMIARAL--------- 151
Cdd:PRK13547 97 AF----SAREIVllgryphARRAGALTHRDGEIAWQALA-LAGATALVGRD--VTTLSGGELARVQFARVLaqlwpphda 169
|
170
....*....|....*...
gi 992389469 152 MHEPKLLILDEPTAGVDI 169
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDL 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
13-172 |
3.07e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 13 TYPGGVQALRGIDLQVEAGDFYA-----LLGPNGAGKSTTIGIISSLVNKSSGRVSVfgyDLEkdvVNAKrqlglvPQEF 87
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK---ISYK------PQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 NFNPFETVQQIVVNQAG-----YYGVE--RKEAIDR-SEKYLKQldlwekrnerarmLSGGMKRRLMIARALMHEPKLLI 159
Cdd:PRK13409 410 KPDYDGTVEDLLRSITDdlgssYYKSEiiKPLQLERlLDKNVKD-------------LSGGELQRVAIAACLSRDADLYL 476
|
170
....*....|...
gi 992389469 160 LDEPTAGVDIELR 172
Cdd:PRK13409 477 LDEPSAHLDVEQR 489
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-170 |
5.46e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 54.18 E-value: 5.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKST-TIGIISslVNKSS-GRVSVFGYDLEK-DVVNAKRQLGLVPQE---------FN 88
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSlTLGLFR--INESAeGEIIIDGLNIAKiGLHDLRFKITIIPQDpvlfsgslrMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 89 FNPFETVQQIVVnqagYYGVERKEAIDRSEKYLKQLDlwEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:TIGR00957 1380 LDPFSQYSDEEV----WWALELAHLKTFVSALPDKLD--HECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD 1453
|
..
gi 992389469 169 IE 170
Cdd:TIGR00957 1454 LE 1455
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-209 |
5.63e-08 |
|
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: 52.75 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 28 VEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGR----------VSVF-GYDLE---KDVVNAKRQLGLVPQefnfnpfe 93
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeiLDEFrGSELQnyfTKLLEGDVKVIVKPQ-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 94 TVQQIVVNQAGYYG--VERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 171
Cdd:cd03236 95 YVDLIPKAVKGKVGelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 992389469 172 RRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGII 209
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-168 |
5.98e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 5.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTtigIISSLVNKSSGRVSVFG------YDLEKDVVNAKRQLGLVPQEFNFNPFET 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCST---LLKALANRTEGNVSVEGdihyngIPYKEFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 95 VQQIvvnqagyygverkeaIDRSEKYlkqldlweKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:cd03233 100 VRET---------------LDFALRC--------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-194 |
7.00e-08 |
|
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: 50.83 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 31 GDFYALLGPNGAGKSTTIGIISSLVNKSSGRVsvfgydlekdvvnakrqlglvpqefnfnpfetvqqIVVNqagyygver 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------------IYID--------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 111 keaIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR------SMWGFLKDLND 184
Cdd:smart00382 38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAllllleELRLLLLLKSE 114
|
170
....*....|
gi 992389469 185 KGTTIILTTH 194
Cdd:smart00382 115 KNLTVILTTN 124
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-214 |
7.66e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 7.66e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 137 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-227 |
9.87e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTtigIISSLVNKSSgrvsvfgyDLEKDVVNAKRQLGLVPQ-EFNFNPfeTVQQIV 99
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTS---LISAMLGELS--------HAETSSVVIRGSVAYVPQvSWIFNA--TVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 100 VNQAGYYGVERKEAIDRSeKYLKQLDLWEKRN-----ERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PLN03232 700 LFGSDFESERYWRAIDVT-ALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 175 MWGFLKDLNDKGTTIILTT---HYLEEAE--MLCRNIGIIQHGELVENTSMKNLLSKL 227
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTnqlHFLPLMDriILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
137-214 |
1.21e-07 |
|
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: 52.90 E-value: 1.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 137 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-168 |
1.27e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVvNAK---RQLGLVPQ--------- 85
Cdd:PTZ00265 398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDI-NLKwwrSKIGVVSQdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 86 -------------------EFNFNPFETVQ--------------------------QIVVNQAGYYGVERKEAIDRSEKY 120
Cdd:PTZ00265 477 knnikyslyslkdlealsnYYNEDGNDSQEnknkrnscrakcagdlndmsnttdsnELIEMRKNYQTIKDSEVVDVSKKV 556
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 121 LKQ------LDLWEKR-NERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVD 168
Cdd:PTZ00265 557 LIHdfvsalPDKYETLvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-226 |
1.62e-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: 52.64 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVfgydlekdvvnaKRQLGLVPQEFNFNPFETVQQIV- 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVAYVPQQAWIQNDSLRENILf 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 100 ---VNQAGYYGVERKEAIDRSEKYLKQLDLWEKrNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMW 176
Cdd:TIGR00957 722 gkaLNEKYYQQVLEACALLPDLEILPSGDRTEI-GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 177 -------GFLkdlndKGTTIILTTH---YLEEAEMlcrnIGIIQHGELVENTSMKNLLSK 226
Cdd:TIGR00957 801 ehvigpeGVL-----KNKTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQELLQR 851
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-170 |
1.62e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 24 IDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGydleKDVVNAKRQ-----LGLVPQ-EFNFNPFETVQQ 97
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG----KTATRGDRSrfmayLGHLPGlKADLSTLENLHF 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 98 IvvnqAGYYGVERKEAIDRSekyLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIE 170
Cdd:PRK13543 106 L----CGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-246 |
1.65e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 20 ALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGyDLEKDVVNAkrqlGLVPQEFNFNPFETVQQIV 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISA----GLSGQLTGIENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 100 vnqagyyGVERKEAIDRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFL 179
Cdd:PRK13546 114 -------GFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 180 KDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVENTSMKNLLSKLksETFILDLAAKSPLPQLE 246
Cdd:PRK13546 187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY--EAFLNDFKKKSKAEQKE 251
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
16-226 |
2.66e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 51.01 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 16 GGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNkSSGRVSVFGYDLEKDVVNAKRQ-LGLVPQEF------- 87
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKaFGVIPQKVfifsgtf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 --NFNPFE--TVQQI--VVNQAGYYGVerkeaidrSEKYLKQLDLweKRNERARMLSGGMKRRLMIARALMHEPKLLILD 161
Cdd:cd03289 94 rkNLDPYGkwSDEEIwkVAEEVGLKSV--------IEQFPGQLDF--VLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992389469 162 EPTAGVDIELRRSMWGFLKDlNDKGTTIILTTHYLeEAEMLCRNIGIIQHGELVENTSMKNLLSK 226
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-172 |
3.19e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 10 LKKTYPGgvqalrgIDLQVEAGDFY-----ALLGPNGAGKSTTIGIISSLVNKSSGrvsvfgyDLEKDV-VNAKrqlglv 83
Cdd:COG1245 347 LTKSYGG-------FSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDLkISYK------ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 84 PQEFNFNPFETVQQIVVNQAgyygverKEAIDRS---EKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLIL 160
Cdd:COG1245 407 PQYISPDYDGTVEEFLRSAN-------TDDFGSSyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLL 479
|
170
....*....|..
gi 992389469 161 DEPTAGVDIELR 172
Cdd:COG1245 480 DEPSAHLDVEQR 491
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
130-194 |
4.33e-07 |
|
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: 50.47 E-value: 4.33e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 130 RNERARMLSGGMKR---RLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:pfam13304 230 GELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-215 |
5.04e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 24 IDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLE----KDVVNA--------KRQLGLVP----QEf 87
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirspRDAIRAgimlcpedRKAEGIIPvhsvAD- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 NFNpfetvqqIVV----NQAGYYGVERKEAiDRSEKYLKQLDLWEKRNERARM-LSGGMKRRLMIARALMHEPKLLILDE 162
Cdd:PRK11288 351 NIN-------ISArrhhLRAGCLINNRWEA-ENADRFIRSLNIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 992389469 163 PTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-196 |
6.26e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 27 QVEAGDFYALLGPNGAGKSTTIGIISSLVnKSSGRVSVFGYDLEKDVVN--AKRQLGLVPQE---FNFNPFetvQQIVVN 101
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelARHRAYLSQQQtppFAMPVF---QYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 102 QAGyygverKEAIDRSEKYL----KQLDLWEKRNERARMLSGGMKRR-------LMIARALMHEPKLLILDEPTAGVDIE 170
Cdd:PRK03695 94 QPD------KTRTEAVASALnevaEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*.
gi 992389469 171 LRRSMWGFLKDLNDKGTTIILTTHYL 196
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-194 |
8.20e-07 |
|
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: 50.00 E-value: 8.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 22 RGI-DLQVE-AGDFYALLGPNGAGKSTTIGIISSLVNKSSGR--------------------VSVFGY------------ 67
Cdd:COG3593 12 RSIkDLSIElSDDLTVLVGENNSGKSSILEALRLLLGPSSSRkfdeedfylgddpdlpeieiELTFGSllsrllrlllke 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 68 ----DLEKDVVNAKRQLGLVPQEFNfnpfETVQQIVVNQAGYYGVERKEAIDRSEKYLKQLDLWEKRNERARM--LSGGM 141
Cdd:COG3593 92 edkeELEEALEELNEELKEALKALN----ELLSEYLKELLDGLDLELELSLDELEDLLKSLSLRIEDGKELPLdrLGSGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 142 KRRLMIA--RALMH-----EPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:COG3593 168 QRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-175 |
9.11e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.93 E-value: 9.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYpGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVfgydleKDVVnakrQLGLVP 84
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETV----KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 85 QEF-NFNPFETVQQIVVNQAGYYGVERKEAIDRSekYL-----KQLDlwekRNERARMLSGGMKRRLMIARALMHEPKLL 158
Cdd:TIGR03719 392 QSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVgrfnfKGSD----QQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170
....*....|....*..
gi 992389469 159 ILDEPTAGVDIELRRSM 175
Cdd:TIGR03719 466 LLDEPTNDLDVETLRAL 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-175 |
1.46e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSvfgydLEKDVvnakrQLGLVPQ---EF---------- 87
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG-----LAKGI-----KLGYFAQhqlEFlradesplqh 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 88 --NFNPFETVQQIVvNQAGYYGVERKEAIDRSEKYlkqldlwekrnerarmlSGGMKRRLMIARALMHEPKLLILDEPTA 165
Cdd:PRK10636 398 laRLAPQELEQKLR-DYLGGFGFQGDKVTEETRRF-----------------SGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
170
....*....|
gi 992389469 166 GVDIELRRSM 175
Cdd:PRK10636 460 HLDLDMRQAL 469
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-170 |
1.75e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 14 YPGGVQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSG--------RVSVF------GYDLEKDvvnakrq 79
Cdd:PLN03073 518 YPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGtvfrsakvRMAVFsqhhvdGLDLSSN------- 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 lglvPQEFNFNPFETV-QQIVVNQAGYYGVERKEAIdrsekylkqldlwekrnERARMLSGGMKRRLMIARALMHEPKLL 158
Cdd:PLN03073 591 ----PLLYMMRCFPGVpEQKLRAHLGSFGVTGNLAL-----------------QPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
170
....*....|..
gi 992389469 159 ILDEPTAGVDIE 170
Cdd:PLN03073 650 LLDEPSNHLDLD 661
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-239 |
1.87e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 137 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELVE 216
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 471
|
90 100
....*....|....*....|...
gi 992389469 217 NTSMKNllsklKSETFILDLAAK 239
Cdd:PRK10982 472 IVDTKT-----TTQNEILRLASL 489
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-198 |
2.14e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.22 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 24 IDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDL----EKDVVNAKRQLGLVPQE----FNFNPFETV 95
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSgalfTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 96 QQIVVNQAgyygvERKEAIDRSEKYLKqLDLWEKRNERARM---LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELR 172
Cdd:PRK11831 106 AYPLREHT-----QLPAPLLHSTVMMK-LEAVGLRGAAKLMpseLSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180
....*....|....*....|....*..
gi 992389469 173 RSMWGFLKDLNDK-GTTIILTTHYLEE 198
Cdd:PRK11831 180 GVLVKLISELNSAlGVTCVVVSHDVPE 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-214 |
2.63e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 31 GDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSvfgydLEKDVVNAK-RQlglvpQEFNFNPFETVQQIVVNQAGYYGV- 108
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVS-----LDPNERLGKlRQ-----DQFAFEEFTVLDTVIMGHTELWEVk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 109 ERKEAI----DRSEK-YLKQLDLWEKRNE--------RA-RMLSG-----------------GMKRRLMIARALMHEPKL 157
Cdd:PRK15064 97 QERDRIyalpEMSEEdGMKVADLEVKFAEmdgytaeaRAgELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 158 LILDEPTAGVDIELRRsmWgfLKD-LNDKGTTIILTTHYLEEAEMLCRNIGIIQHGEL 214
Cdd:PRK15064 177 LLLDEPTNNLDINTIR--W--LEDvLNERNSTMIIISHDRHFLNSVCTHMADLDYGEL 230
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-168 |
4.38e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKS----SGRVSVFGYDLEkDVVNAKRQLGLVPQEFNFN-PF 92
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPE-EIKKHYRGDVVYNAETDVHfPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 93 ETVQQIVVNQAG-------YYGVERKEAIDR-SEKYLKQLDLWEKR-----NERARMLSGGMKRRLMIARALMHEPKLLI 159
Cdd:TIGR00956 153 LTVGETLDFAARcktpqnrPDGVSREEYAKHiADVYMATYGLSHTRntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
....*....
gi 992389469 160 LDEPTAGVD 168
Cdd:TIGR00956 233 WDNATRGLD 241
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-213 |
7.33e-06 |
|
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: 47.09 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 35 ALLGPNGAGKSTTIGIISSLVNKSSGRvsvFGYDLEKD-VVNAKRQLGLvpqefnFNPFETVQQivvnqaGYYGVERK-E 112
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGD---YDEEPSWDeVLKRFRGTEL------QDYFKKLAN------GEIKVAHKpQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 113 AIDRSEKYLKQL--DLWEKRNERARM-------------------LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIEL 171
Cdd:COG1245 168 YVDLIPKVFKGTvrELLEKVDERGKLdelaeklglenildrdiseLSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 992389469 172 RRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIqHGE 213
Cdd:COG1245 248 RLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL-YGE 288
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
137-212 |
7.99e-06 |
|
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: 45.39 E-value: 7.99e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992389469 137 LSGGMKRRLMIARALMHEPK--LLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLeeaEMLCRNIGIIQHG 212
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL---DVLSSADWIIDFG 162
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-225 |
9.53e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 21 LRGIDLQVEAGDFYALLGPNGAGKSTTI-GIISSLVNKSSGRVSVFGydlekdvvnakrQLGLVPQ-EFNFNPfeTVQQI 98
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRG------------TVAYVPQvSWIFNA--TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 99 VV-----NQAGYYGVERKEAIDRSEKYLKQLDLWEKrNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRR 173
Cdd:PLN03130 699 ILfgspfDPERYERAIDVTALQHDLDLLPGGDLTEI-GERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGR 777
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 174 SMwgFLKDLND--KGTTIILTT---HYLEEAEmlcrNIGIIQHGELVENTSMKNLLS 225
Cdd:PLN03130 778 QV--FDKCIKDelRGKTRVLVTnqlHFLSQVD----RIILVHEGMIKEEGTYEELSN 828
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-194 |
2.96e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 38 GPNGAGKSTtigIISSLVNKSSGRVSVFGYDLEKD--VVNAKRQLGLVPQEFNfnpfetvqqivVNQAGYYGVERKEAID 115
Cdd:cd03240 29 GQNGAGKTT---IIEALKYALTGELPPNSKGGAHDpkLIREGEVRAQVKLAFE-----------NANGKKYTITRSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 116 RSEKYLKQLDL-WEKRNERARmLSGGMKR------RLMIARALMHEPKLLILDEPTAGVD-----------IELRRSMWG 177
Cdd:cd03240 95 ENVIFCHQGESnWPLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieeslaeiIEERKSQKN 173
|
170
....*....|....*..
gi 992389469 178 FLkdlndkgttIILTTH 194
Cdd:cd03240 174 FQ---------LIVITH 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-169 |
7.47e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 7.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 992389469 128 EKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDI 169
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-215 |
1.23e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992389469 137 LSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYLEEAEMLCRNIGIIQHGELV 215
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-209 |
1.23e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 36 LLGPNGAGKSTTIGIISSLVNKSSGRVS-------VFGY-------DLEKDVVNAKRQLGLVPQEFNFNP--FE-TVQQI 98
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDYEeepswdeVLKRfrgtelqNYFKKLYNGEIKVVHKPQYVDLIPkvFKgKVREL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 99 V--VNQAGyygverkeaidRSEKYLKQLDLWEKRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMW 176
Cdd:PRK13409 184 LkkVDERG-----------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVA 252
|
170 180 190
....*....|....*....|....*....|...
gi 992389469 177 GFLKDLNdKGTTIILTTHYLEEAEMLCRNIGII 209
Cdd:PRK13409 253 RLIRELA-EGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-174 |
2.73e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 38 GPNGAGKSTTIGIISSLVNKSSGRVSVfGydlekDVVnakrQLGLVPQEF-NFNPFETVQQIVVNQAGYYGVERKEAIDR 116
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKI-G-----ETV----KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSR 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 117 SekYL-----KQLDlwekRNERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PRK11819 427 A--YVgrfnfKGGD----QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA 483
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-194 |
4.57e-04 |
|
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: 41.71 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 5 LELQQLKKTYPGgVQALRG-----IDLQVEAGDFYALLGPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKDVVNAKRQ 79
Cdd:COG4615 328 LELRGVTYRYPG-EDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 80 LglvpqeF-----NFNPFETVqqivvnqagyYGVERKEAIDRSEKYLKQLDLWEK---RNER--ARMLSGGMKRRL-MIA 148
Cdd:COG4615 407 L------FsavfsDFHLFDRL----------LGLDGEADPARARELLERLELDHKvsvEDGRfsTTDLSQGQRKRLaLLV 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 992389469 149 rALMHEPKLLILDEPTAGVDIELRRSmwgF----LKDLNDKGTTIILTTH 194
Cdd:COG4615 471 -ALLEDRPILVFDEWAADQDPEFRRV---FytelLPELKARGKTVIAISH 516
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-194 |
5.21e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 38 GPNGAGKSTTIGIISSLVNKSSGRVSVFGYDLEKdvvNAKRQLGLVPQEFNFNPFETVQQIVVNQAGYYgvERKEAIDRS 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN---IAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY--NSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992389469 118 EKYLKQLDLWEkrnERARMLSGGMKRRLMIARALMHEPKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:PRK13541 108 IHYFKLHDLLD---EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-231 |
6.92e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 137 LSGGMKRRLMIARALMHEPK--LLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHyleEAEMLC---RNIGI--- 208
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH---DEQMISladRIIDIgpg 553
|
90 100
....*....|....*....|....*
gi 992389469 209 --IQHGELVENTSMKNLLSKLKSET 231
Cdd:PRK00635 554 agIFGGEVLFNGSPREFLAKSDSLT 578
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-194 |
7.72e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.37 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 18 VQALRGIDLQVEAGDFYALLGPNGAGKSTTIGIISSlvNKSSG------RVSVFgydlEKDVVNAKRQLGLVPQEFNFNP 91
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGyiegdiRISGF----PKKQETFARISGYCEQNDIHSP 966
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 92 FETVQQIVVnqagYYGVER--KEaIDRSEKYL---KQLDLWEKRNERARM--------LSGGMKRRLMIARALMHEPKLL 158
Cdd:PLN03140 967 QVTVRESLI----YSAFLRlpKE-VSKEEKMMfvdEVMELVELDNLKDAIvglpgvtgLSTEQRKRLTIAVELVANPSII 1041
|
170 180 190
....*....|....*....|....*....|....*.
gi 992389469 159 ILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTH 194
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
107-197 |
8.48e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.41 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 107 GVERKEAIDRSEKYLKQLDLWEKRNER-----ARMLSGGMKRRLMIARALM---HEPKLLILDEPTAGVDIELRRSMWGF 178
Cdd:COG1106 168 GIEDIEVEEEEIEDLVERKLIFKHKGGnvplpLSEESDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKL 247
|
90 100
....*....|....*....|
gi 992389469 179 LKDL-NDKGTTIILTTHYLE 197
Cdd:COG1106 248 FLDLaNKNNAQLIFTTHSTE 267
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
138-195 |
1.02e-03 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 39.54 E-value: 1.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 992389469 138 SGGMKRrlmIARALMH--EPKLLILDEPTAGVDIE----LRRSmwgFLKDLNDKGTTIILTTHY 195
Cdd:cd03280 93 SSHMKN---IARILQHadPDSLVLLDELGSGTDPVegaaLAIA---ILEELLERGALVIATTHY 150
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-182 |
1.89e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 35 ALLGPNGAGKST---------------TIGIISSLVNKSSGRVSV-FGYDLEKDVVNAKRQLGLVPQEFNFNPFEtVQQI 98
Cdd:COG0419 27 LIVGPNGAGKSTileairyalygkarsRSKLRSDLINVGSEEASVeLEFEHGGKRYRIERRQGEFAEFLEAKPSE-RKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992389469 99 VVNQAGYYGVER-----KEAIDRSEKYLKQLDLWEKRNER----------ARMLSGGMKRRLMIARALMhepklLILDep 163
Cdd:COG0419 106 LKRLLGLEIYEElkerlKELEEALESALEELAELQKLKQEilaqlsgldpIETLSGGERLRLALADLLS-----LILD-- 178
|
170
....*....|....*....
gi 992389469 164 TAGVDIELRRSMWGFLKDL 182
Cdd:COG0419 179 FGSLDEERLERLLDALEEL 197
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-196 |
7.31e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 7.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992389469 137 LSGGMKRRLMIARALMHE---PKLLILDEPTAGVDIELRRSMWGFLKDLNDKGTTIILTTHYL 196
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| |
