|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-233 |
3.14e-107 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 311.61 E-value: 3.14e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSETFI 233
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFL 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-299 |
3.63e-76 |
|
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: 234.98 E-value: 3.63e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 12 KTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVPQEFNFNP 91
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL 171
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 172 RRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSETFILDLAAKSPL--------- 242
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQSLkvevsmlia 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 243 ---PKLDGYHS--RLTDTSTLEVEVMREQgLNGLFTQLSAQGVQVLSMRNKANRLEELFVTL 299
Cdd:TIGR01188 240 elgETGLGLLAvtVDSDRIKILVPDGDET-VPEIVEAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-214 |
3.98e-76 |
|
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: 230.36 E-value: 3.98e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVvnqagyygvtrreamaraekylnqldlwgkrnerarMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-232 |
1.80e-73 |
|
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: 225.89 E-value: 1.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSETF 232
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-215 |
8.30e-72 |
|
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: 221.09 E-value: 8.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 165 AGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-215 |
4.71e-69 |
|
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: 213.91 E-value: 4.71e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV 83
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 164 TAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-305 |
1.12e-61 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 197.64 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVnakRQLGLV 83
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR---RRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETVLQivvnQAGYY----GVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLI 159
Cdd:COG4152 77 PEERGLYPKMKVGE----QLVYLarlkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 160 LDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSETFILDL-AA 238
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEAdGD 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 239 KSPLPKLDGYHSRLTDTSTLEVEVMREQGLNGLFTQLSAQGvQVLSMRNKANRLEELFVTLVNGNGE 305
Cdd:COG4152 233 AGWLRALPGVTVVEEDGDGAELKLEDGADAQELLRALLARG-PVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-215 |
3.60e-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: 186.38 E-value: 3.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGLV 83
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQefnfNP-----FETVLQIV----VNQagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQ 154
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVafgpENL----GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 155 PKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-215 |
4.52e-58 |
|
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: 185.47 E-value: 4.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGvKALRGIDLSVEAGdFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 165 AGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03264 159 AGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-200 |
3.19e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 179.51 E-value: 3.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKdivnAKRQL 80
Cdd:COG1121 3 MMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR----ARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFN---PFeTVLQIV----VNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMH 153
Cdd:COG1121 78 GYVPQRAEVDwdfPI-TVRDVVlmgrYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAE 200
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVR 203
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-200 |
7.32e-55 |
|
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: 178.25 E-value: 7.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV 83
Cdd:TIGR03864 1 ALEVAGLSFRY-GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEP 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1398598869 164 TAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAE 200
Cdd:TIGR03864 160 TVGLDPASRAAITAHVRALARdQGLSVLWATHLVDEIE 197
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-215 |
1.27e-54 |
|
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: 176.79 E-value: 1.27e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTY---AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLG 81
Cdd:cd03266 2 ITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-214 |
1.47e-53 |
|
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: 174.22 E-value: 1.47e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAK---- 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 -RQLGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIgIIQNGEL 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRII-ELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
2.42e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 171.38 E-value: 2.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDI 73
Cdd:COG1136 1 MSPLLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 74 VNAKRQ-LGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALM 152
Cdd:COG1136 81 ARLRRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIgIIQNGELVENTS 219
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVI-RLRDGRIVSDER 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-203 |
3.66e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 171.81 E-value: 3.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYA---GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIVNAKRQL 80
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETVLQ---IVVNQAGyygVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:COG1116 83 GVVFQEPALLPWLTVLDnvaLGLELRG---VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEAEMLC 203
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLA 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-278 |
1.09e-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: 1.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV------------PQ 85
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVVfgqrsqlwwdlpAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 86 E-FNFNpfetvlqivvnqAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:COG4586 115 DsFRLL------------KAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSETFI-LDLAAKSPL 242
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIvLELAEPVPP 262
|
250 260 270
....*....|....*....|....*....|....*..
gi 1398598869 243 PKLD-GYHSRLTDTSTLEVEVMREQGLNGLFTQLSAQ 278
Cdd:COG4586 263 LELPrGGEVIEREGNRVRLEVDPRESLAEVLARLLAR 299
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-215 |
1.22e-51 |
|
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: 169.00 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDivnAKRQLGLVP 84
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-215 |
1.85e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 169.85 E-value: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID----KDIVNAKRQ 79
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTalrgRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQEFNFNPFETVLQIVVN-QAGYYGVTR-------REAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARAL 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAgRLGRTSTWRsllglfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 152 MHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLC-RNIGiIQNGELV 215
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYAdRIIG-LRDGRVV 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-216 |
2.77e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 168.31 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAKRQL 80
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNP----FETV---LQIVvnqagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMH 153
Cdd:COG2884 82 GVVFQDFRLLPdrtvYENValpLRVT-------GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-213 |
2.34e-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: 165.72 E-value: 2.34e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 6 ELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL-GLV 83
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFN---FNPfeTVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:cd03225 81 FQNPDdqfFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGE 213
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-198 |
2.49e-50 |
|
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: 166.80 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAG-SVRVFGYDIDK-DIVNAKRQLG 81
Cdd:COG1119 3 LLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGeDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEF--NFNPFETVLQIVVnqAGYYGVTRR------EAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMH 153
Cdd:COG1119 82 LVSPALqlRFPRDETVLDVVL--SGFFDSIGLyreptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQG-TTIILTTHYLEE 198
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-212 |
5.93e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 167.67 E-value: 5.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV 83
Cdd:PRK13537 7 PIDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 164 TAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNG 212
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-203 |
1.60e-48 |
|
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: 161.10 E-value: 1.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIVNAKRQLG 81
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1398598869 162 EPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEAEMLC 203
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLA 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-212 |
2.62e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 164.62 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 2 NYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLG 81
Cdd:PRK13536 39 TVAIDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNG 212
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-215 |
8.17e-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: 8.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 6 ELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDivnaKRQLGLVPQ 85
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 86 EFNFNP-FE-TVLQIV----VNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLI 159
Cdd:cd03235 76 RRSIDRdFPiSVRDVVlmglYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 160 LDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIgIIQNGELV 215
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVV 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-216 |
5.26e-47 |
|
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: 165.08 E-value: 5.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTY----AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL 80
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 ----GLVPQefN----FNPFETVLQIV---VNQAGyyGVTRREAMARAEKYLNQLDLWGK-RNERARMLSGGMKRRLMIA 148
Cdd:COG1123 341 rrrvQMVFQ--DpyssLNPRMTVGDIIaepLRLHG--LLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 149 RALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-194 |
6.31e-47 |
|
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: 157.60 E-value: 6.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV- 83
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 ----PQEF-NFNPFETVLQIVVNQAGYYGVT------RREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALM 152
Cdd:cd03219 80 tfqiPRLFpELTVLENVMVAAQARTGSGLLLararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH 201
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-213 |
1.31e-46 |
|
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: 154.32 E-value: 1.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 6 ELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGLVP 84
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QefnfnpfetvlqivvnqagyygvtrreamaraekylnqldlwgkrnerarmLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGE 213
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-216 |
3.43e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 154.98 E-value: 3.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIdKDIVNAKRQLGLVP 84
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 165 AGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03259 159 SALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-194 |
1.01e-45 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 155.20 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK----DIVna 76
Cdd:COG0411 1 SDPLLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphRIA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 krQLGLV-----PQEFnfnPFETVLQIVV----NQAGY-----------YGVTRREAMARAEKYLNQLDLWGKRNERARM 136
Cdd:COG0411 78 --RLGIArtfqnPRLF---PELTVLENVLvaahARLGRgllaallrlprARREEREARERAEELLERVGLADRADEPAGN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 137 LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTH 194
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEH 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-213 |
1.27e-45 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 152.34 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVN---AKRQLG 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQIVVnqagyYGvtrreamaraekylnqldlwgkrnerarmLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIA-----LG-----------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGE 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-217 |
3.64e-45 |
|
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: 152.37 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIvNAKRQLGLVP 84
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRReamaRAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 165 AGVD----IELRRsmwgFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVEN 217
Cdd:cd03268 155 NGLDpdgiKELRE----LILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-215 |
3.73e-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: 3.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAKRQL 80
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETVLQ-IVVNQAGYYGVTR-------REAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALM 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLEnVLSGRLGRRSTWRslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
4-215 |
7.01e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 155.64 E-value: 7.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDkDIVNAKRQLGLV 83
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-GLPPEKRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFN-FnPFETVLQIVvnqaGYY----GVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLL 158
Cdd:COG3842 83 FQDYAlF-PHLTVAENV----AFGlrmrGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 159 ILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-226 |
8.80e-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: 151.96 E-value: 8.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID----KDIVNAK 77
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 RQLGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAK 226
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-215 |
5.37e-44 |
|
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: 150.58 E-value: 5.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKdiVNAK---RQL 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS--LSRRelaRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETVLQIVV----NQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVAlgryPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
6.50e-44 |
|
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: 148.78 E-value: 6.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVtrREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAE 200
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-216 |
1.89e-43 |
|
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: 148.42 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAK 77
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 RQLGLVPQE--FNFNPFETVLQIVVNQAGYYGVTRREAmARAEKYLNQLDLWGKRNERARM----LSGGMKRRLMIARAL 151
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKE-ARKEAVLLLLVGVGLPEEVLNRypheLSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 152 MHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-261 |
7.41e-43 |
|
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: 153.91 E-value: 7.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGG-VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTA---GSVRVFGYDIDK-DIVN 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLElSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 76 AKRQLGLVPQEF--NFNPfETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMH 153
Cdd:COG1123 81 RGRRIGMVFQDPmtQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSetf 232
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA--- 236
|
250 260 270
....*....|....*....|....*....|.
gi 1398598869 233 ildLAAKSPLPKLDGYHSRLTDTST--LEVE 261
Cdd:COG1123 237 ---LAAVPRLGAARGRAAPAAAAAEplLEVR 264
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-215 |
9.13e-43 |
|
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: 147.09 E-value: 9.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYA-----GGVK---------------ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRV 64
Cdd:cd03267 1 IEVSNLSKSYRvyskePGLIgslkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 65 FGYDIDKDIVNAKRQLGLVPQE-----FNFNPFETVLQIvvnqAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSG 139
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVFGQktqlwWDLPVIDSFYLL----AAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 140 GMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-282 |
1.11e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.46 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAK 77
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 RQLGLVPQefNFNPFE--TV-------LQIVvnqagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIA 148
Cdd:COG1135 82 RKIGMIFQ--HFNLLSsrTVaenvalpLEIA-------GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 149 RALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHyleeaEM-----LCRNIGIIQNGELVENTSMKG 222
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH-----EMdvvrrICDRVAVLENGRIVEQGPVLD 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 223 LLAKLKSET---FI-LDLAAKSPLPKLDGYHSRLTDTSTLEVEVMREQGLNGLFTQLSAQ-GVQV 282
Cdd:COG1135 228 VFANPQSELtrrFLpTVLNDELPEELLARLREAAGGGRLVRLTFVGESADEPLLSELARRfGVDV 292
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
1.44e-42 |
|
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: 143.56 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNA-KRQLGLVPQEFNFNPFETVLQIV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 100 VNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM----LSGGMKRRLMIARALMHQPKLLILDEPTA 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-230 |
2.22e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 143.79 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTY---AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQ 79
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQ--EFNFNPFETVLQIV---VNQAGyygvtRREAMARAEKYLNQLDLWGK-RNERARMLSGGMKRRLMIARALMH 153
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILaepLRIHG-----LPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE 230
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-194 |
3.08e-41 |
|
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: 142.28 E-value: 3.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID---KDIVNAKRQLG 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQ-IVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:cd03262 80 MVFQQFNLFPHLTVLEnITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-223 |
2.12e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 147.09 E-value: 2.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-KDIVNAKRQ 79
Cdd:COG1129 1 AEPLLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 -LGLVPQEFNFNPFETVLQ-IVV-NQAGYYGVTRREAM-ARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQP 155
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAEnIFLgREPRRGGLIDWRAMrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 156 KLLILDEPTA---GVDIElrrSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGL 223
Cdd:COG1129 160 RVLILDEPTAsltEREVE---RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-201 |
2.74e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 140.51 E-value: 2.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID---KDIVNAKRQLG 81
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQ------IVVNqagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQP 155
Cdd:COG1126 81 MVFQQFNLFPHLTVLEnvtlapIKVK-----KMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHyleeaEM 201
Cdd:COG1126 156 KVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH-----EM 196
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-215 |
3.45e-40 |
|
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: 137.95 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLvp 84
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 qefnfnpfETVLQivvnqagyygvtrreamaraekylnqldlwgkrnerarmLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03216 78 --------AMVYQ---------------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 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 |
1.63e-39 |
|
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: 137.92 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAKRQL 80
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-225 |
6.04e-39 |
|
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: 136.41 E-value: 6.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK----DIVnaKRQL 80
Cdd:cd03224 1 LEVENLNAGY-GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlpphERA--RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETVLQivvN-QAGYYGVTRREAMARAEKYLNQL-DLWGKRNERARMLSGGMKRRLMIARALMHQPKLL 158
Cdd:cd03224 78 GYVPEGRRIFPELTVEE---NlLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 159 ILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLA 225
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-216 |
1.87e-37 |
|
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: 135.57 E-value: 1.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTY---AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLV---NKTAGSVRVFGydidKDIVNAK- 77
Cdd:COG0444 2 LEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDG----EDLLKLSe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 --------RQLGLVPQE-FN-FNPFETVLQIV-----VNQagyyGVTRREAMARAEKYLNQLDLwgkRNERARM------ 136
Cdd:COG0444 78 kelrkirgREIQMIFQDpMTsLNPVMTVGDQIaeplrIHG----GLSKAEARERAIELLERVGL---PDPERRLdryphe 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 137 LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
.
gi 1398598869 216 E 216
Cdd:COG0444 231 E 231
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-214 |
2.08e-37 |
|
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: 132.52 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-KDIVNAKRQLGLV 83
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrKDLHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETvLQIVVNQAGYygvtrreAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:TIGR03740 80 PLYENLTAREN-LKVHTTLLGL-------PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 164 TAGVDI----ELRRsmwgFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:TIGR03740 152 TNGLDPigiqELRE----LIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-216 |
2.20e-37 |
|
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: 132.69 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KTAGSVRVFG---YDIDKDIVNA 76
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdiYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KRQLGLVPQEFNfnPFE-TVLQIVVnqagyYGVT------RREAMARAEKYLNQLDLWG--KRNERARMLSGGMKRRLMI 147
Cdd:cd03260 80 RRRVGMVFQKPN--PFPgSIYDNVA-----YGLRlhgiklKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 148 ARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQgTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVE 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-216 |
3.82e-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: 132.36 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIVN---AKRQLG 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDITNlppHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQivvNQAgyYGVTRR-----EAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:cd03300 76 TVFQNYALFPHLTVFE---NIA--FGLRLKklpkaEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-218 |
5.65e-37 |
|
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: 131.79 E-value: 5.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI---DKDIVNA- 76
Cdd:COG4181 8 IIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfalDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 -KRQLGLVPQEFNFNPFETVLQIV---VNQAGyygvtRREAMARAEKYLNQLDLwGKR-NERARMLSGGMKRRLMIARAL 151
Cdd:COG4181 88 rARHVGFVFQSFQLLPTLTALENVmlpLELAG-----RRDARARARALLERVGL-GHRlDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 152 MHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMlCRNIGIIQNGELVENT 218
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-225 |
1.25e-36 |
|
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: 130.87 E-value: 1.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK----DIVnaKRQL 80
Cdd:COG0410 4 LEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRIA--RLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQE---FnfnPFETVLQivvN-QAGYYGVTRREAMARAEKYLNQL--DLWGKRNERARMLSGGMKRRLMIARALMHQ 154
Cdd:COG0410 81 GYVPEGrriF---PSLTVEE---NlLLGAYARRDRAEVRADLERVYELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 155 PKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLA 225
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-216 |
1.49e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 130.88 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGLV 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIrEQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDL--WGKRNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-215 |
1.82e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.31 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID----KDIVNA 76
Cdd:COG3845 2 MPPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirspRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KrqLGLVPQEFN-FNPFeTVLQIVV--NQAGYYGVTRREAMAR-----AEKYLNQLDLwgkrNERARMLSGGMKRRLMIA 148
Cdd:COG3845 81 G--IGMVHQHFMlVPNL-TVAENIVlgLEPTKGGRLDRKAARArirelSERYGLDVDP----DAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 149 RALMHQPKLLILDEPTAG-----VDiELrrsmWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG3845 154 KALYRGARILILDEPTAVltpqeAD-EL----FEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-214 |
4.60e-36 |
|
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: 137.84 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 17 GVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVPQEFNFNPFETVL 96
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 QIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMW 176
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190
....*....|....*....|....*....|....*...
gi 1398598869 177 GFLKELNAqGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:TIGR01257 1102 DLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-215 |
9.41e-36 |
|
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: 127.76 E-value: 9.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 10 LTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIVNAKRQ--LGLVPQEF 87
Cdd:cd03226 5 ISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRksIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 NFNPF-ETVLQIVVNQAGYYGvtrrEAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:cd03226 81 DYQLFtDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 167 VDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-215 |
1.22e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.78 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 6 ELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVP 84
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QefnfnpfetvlqivvnqagyygvtrreAMARaekylnqLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03214 80 Q---------------------------ALEL-------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
2.12e-35 |
|
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: 127.79 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNA 76
Cdd:COG1127 2 SEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KRQLGLVPQE---F-NFNPFETV---LQIvvnqagYYGVTRREAMARAEKYLNQLDLwgkRNERARM---LSGGMKRRLM 146
Cdd:COG1127 81 RRRIGMLFQGgalFdSLTVFENVafpLRE------HTDLSEAEIRELVLEKLELVGL---PGAADKMpseLSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 147 IARALMHQPKLLILDEPTAGVD-------IELrrsmwgfLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENT 218
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpitsaviDEL-------IRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
|
....*..
gi 1398598869 219 SMKGLLA 225
Cdd:COG1127 225 TPEELLA 231
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-194 |
5.06e-35 |
|
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: 125.23 E-value: 5.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 14 YAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID---KDIVNAKRQLGLVPQefnfN 90
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrKGLLERRQRVGLVFQ----D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFETVLQIVVNQAGYY-----GVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTA 165
Cdd:TIGR01166 77 PDDQLFAADVDQDVAFgplnlGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180
....*....|....*....|....*....
gi 1398598869 166 GVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-215 |
8.55e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.04 E-value: 8.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRvfgydIDKDIVN----AKRQ 79
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-----IGGRDVTdlppKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQEF-NFnPFETV-------LQIVvnqagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARAL 151
Cdd:COG3839 77 IAMVFQSYaLY-PHMTVyeniafpLKLR-------KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 152 MHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-230 |
1.02e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 126.40 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVkALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKD---------IV 74
Cdd:PRK11264 3 AIEVKNLVKKFHGQT-VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 75 NAKRQLGLVPQEFNFNPFETVLQ-IVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE 230
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-216 |
2.71e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.13 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-------KDIVNA 76
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpseKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KRQLGLVPQEFNFNPFETVLQ-IVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQP 155
Cdd:COG4161 81 RQKVGMVFQQYNLWPHLTVMEnLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-226 |
5.49e-34 |
|
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: 130.26 E-value: 5.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGL 82
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQefnfNPF---ETV---LQIVVNQAGyygvtrREAMARAekyLNQLDLW--------------GkrnERARMLSGGMK 142
Cdd:COG4988 416 VPQ----NPYlfaGTIrenLRLGRPDAS------DEELEAA---LEAAGLDefvaalpdgldtplG---EGGRGLSGGQA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 143 RRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEmLCRNIGIIQNGELVENTSMKG 222
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEE 557
|
....
gi 1398598869 223 LLAK 226
Cdd:COG4988 558 LLAK 561
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
8.52e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.46 E-value: 8.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKR-Q 79
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQE-----FNFNPFETVLQIVVNQagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQ 154
Cdd:PRK13647 81 VGLVFQDpddqvFSSTVWDDVAFGPVNM----GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 155 PKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL 217
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-216 |
1.33e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.20 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-------KDIVNA 76
Cdd:PRK11124 2 SIQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsktpsdKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KRQLGLVPQEFNFNPFETVLQIVVNQ-AGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQP 155
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-233 |
1.67e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 125.30 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 6 ELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAKR 78
Cdd:PRK11153 3 ELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 79 QLGLVPQEFNF----NPFETV---LQIVvnqagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARAL 151
Cdd:PRK11153 83 QIGMIFQHFNLlssrTVFDNValpLELA-------GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 152 MHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE 230
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHP 235
|
....*.
gi 1398598869 231 T---FI 233
Cdd:PRK11153 236 LtreFI 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-214 |
2.51e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.46 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLV 83
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEfnfnPF---ETVLQIVvnQAGYYGVTRREAMARAEKYLNQLDL----WGKRNERarmLSGGMKRRLMIARALMHQPK 156
Cdd:COG4619 80 PQE----PAlwgGTVRDNL--PFPFQLRERKFDRERALELLERLGLppdiLDKPVER---LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-219 |
2.74e-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: 2.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVN--AKRQLGL 82
Cdd:COG1137 4 LEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHkrARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQE---F-------NFnpfETVLQIVvnqagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALM 152
Cdd:COG1137 83 LPQEasiFrkltvedNI---LAVLELR-------KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 153 HQPKLLILDEPTAGVD----IELRRsMWGFLKElnaQGTTIILTTHYLEEAEMLCRNIGIIQNGE-LVENTS 219
Cdd:COG1137 153 TNPKFILLDEPFAGVDpiavADIQK-IIRHLKE---RGIGVLITDHNVRETLGICDRAYIISEGKvLAEGTP 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-213 |
3.22e-33 |
|
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: 120.18 E-value: 3.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG-VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKR-QLGL 82
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFN-FNpfETVlqivvnqagyygvtrREamaraekylnqldlwgkrNerarMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03228 81 VPQDPFlFS--GTI---------------RE------------------N----ILSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMlCRNIGIIQNGE 213
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-214 |
4.53e-33 |
|
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: 121.50 E-value: 4.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGL-- 82
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFnpFE--TVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:cd03218 80 LPQEASI--FRklTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 161 DEPTAGVD----IELRRsmwgFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:cd03218 158 DEPFAGVDpiavQDIQK----IIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-221 |
8.57e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.11 E-value: 8.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID---KDIVNAKRQLG 81
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LV---PQEFNFNPfeTVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLL 158
Cdd:PRK13639 82 IVfqnPDDQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 159 ILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMK 221
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
15-216 |
1.66e-32 |
|
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: 121.21 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 15 AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAKRQ-LGLVPQEFNF 89
Cdd:cd03294 34 TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRRKkISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 90 NPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDI 169
Cdd:cd03294 114 LPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1398598869 170 ELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03294 194 LIRREMQDELLRLQAeLQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-216 |
2.53e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.56 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQivvNQAgyYGVT-----RREAMARAEKYLN--QLDLWGKRneRARMLSGGMKRRLMIARALMHQPKL 157
Cdd:COG1118 82 QHYALFPHMTVAE---NIA--FGLRvrppsKAEIRARVEELLElvQLEGLADR--YPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-230 |
4.72e-32 |
|
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: 118.98 E-value: 4.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIVNA---KRQLGLVPQEFNFNPFETVLQ 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDITNLppeKRDISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 98 ivvNQAgyYGVTRREAM--ARAEKYLNQLDLWGKR---NERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELR 172
Cdd:cd03299 91 ---NIA--YGLKKRKVDkkEIERKVLEIAEMLGIDhllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 173 RSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE 230
Cdd:cd03299 166 EKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-230 |
4.94e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.04 E-value: 4.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID---KDIVNAKRQLG 81
Cdd:PRK09493 2 IEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFNPFETVLQIVVnqagyYGVTRREAMARAEKYLNQLDLWGKRNERARM------LSGGMKRRLMIARALMHQP 155
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVM-----FGPLRVRGASKEEAEKQARELLAKVGLAERAhhypseLSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE 230
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-216 |
6.32e-32 |
|
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: 118.13 E-value: 6.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDkDIVNAKRQLGLVP 84
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-226 |
8.65e-32 |
|
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: 124.11 E-value: 8.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 3 YALELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQL 80
Cdd:COG4987 332 PSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQE---FNfnpfETV---LQIVVNQAGyygvtrREAMARA------EKYLNQ----LDLW-GkrnERARMLSGGMKR 143
Cdd:COG4987 412 AVVPQRphlFD----TTLrenLRLARPDAT------DEELWAAlervglGDWLAAlpdgLDTWlG---EGGRRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 144 RLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRnIGIIQNGELVENTSMKGL 223
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDR-ILVLEDGRIVEQGTHEEL 556
|
...
gi 1398598869 224 LAK 226
Cdd:COG4987 557 LAQ 559
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-226 |
2.18e-31 |
|
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: 123.41 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAG-GVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLG 81
Cdd:COG2274 473 DIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQE---FN---------FNP---FETVLQiVVNQAGyygvTRREAMARAEKYLNQLdlwgkrNERARMLSGGMKRRLM 146
Cdd:COG2274 553 VVLQDvflFSgtirenitlGDPdatDEEIIE-AARLAG----LHDFIEALPMGYDTVV------GEGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 147 IARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEmLCRNIGIIQNGELVENTSMKGLLAK 226
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-215 |
2.27e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 118.31 E-value: 2.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGV----KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-----DKDIV 74
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 75 NAKRQLGLVPQEFNFNPF-ETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM-LSGGMKRRLMIARALM 152
Cdd:PRK13649 82 QIRKKVGLVFQFPESQLFeETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFeLSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-217 |
3.20e-30 |
|
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: 114.14 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL---- 80
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrm 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVpqeFNFNPFETVLQIVVNQA----GYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:cd03261 80 GML---FQSGALFDSLTVFENVAfplrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 157 LLILDEPTAGVD-------IELRRSmwgfLKElnAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVEN 217
Cdd:cd03261 157 LLLYDEPTAGLDpiasgviDDLIRS----LKK--ELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-217 |
3.48e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 119.83 E-value: 3.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI---DKDIV 74
Cdd:PRK10535 1 MTALLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatlDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 75 NAKRQ--LGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALM 152
Cdd:PRK10535 81 AQLRRehFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGiIQNGELVEN 217
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIE-IRDGEIVRN 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-215 |
8.89e-30 |
|
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: 112.39 E-value: 8.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 24 IDLSVEaGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFG---YDIDK--DIVNAKRQLGLVPQEFNFNPFETVLQI 98
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkiNLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 VVnqAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGF 178
Cdd:cd03297 96 LA--FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1398598869 179 LKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03297 174 LKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
10-216 |
1.33e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 112.75 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 10 LTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV--PQEF 87
Cdd:TIGR04406 7 LIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGylPQEA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 NF-------NPFETVLQIVVNqagyygVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:TIGR04406 86 SIfrkltveENIMAVLEIRKD------LDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 161 DEPTAGVD----IELRRSMwGFLKElnaQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:TIGR04406 160 DEPFAGVDpiavGDIKKII-KHLKE---RGIGVLITDHNVRETLDICDRAYIISDGKVLA 215
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-216 |
2.07e-29 |
|
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: 111.85 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVN--AKRQLGL 82
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHerARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFNPFETVLQivvN-QAGYYGVTRREAMARAEKY-----LNQLdlwgkRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:TIGR03410 80 VPQGREIFPRLTVEE---NlLTGLAALPRRSRKIPDEIYelfpvLKEM-----LGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 157 LLILDEPTAGV------DIElrrsmwGFLKELNAQGT-TIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:TIGR03410 152 LLLLDEPTEGIqpsiikDIG------RVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
16-212 |
3.57e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 114.94 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-KDIVNAKRQLGLVPQE----FNFn 90
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDtslsFEF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 pfeTVLQIV-------VNQAGYYGVTRREAMARAekyLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:PRK09536 93 ---DVRQVVemgrtphRSRFDTWTETDRAAVERA---MERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 164 TAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNG 212
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADG 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-199 |
3.57e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.02 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidkdivnaKRQLGLVPQEFNFNPfetV 95
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPD---S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 96 LQIVVNQA---------GYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:NF040873 70 LPLTVRDLvamgrwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 1398598869 167 VDIELRRSMWGFLKELNAQGTTIILTTHYLEEA 199
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
6.93e-29 |
|
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: 115.46 E-value: 6.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGL 82
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQefnfNPFETVLQIVVNQAGYYGVTRREAMARAekyLNQLDLWG-----------KRNERARMLSGGMKRRLMIARAL 151
Cdd:TIGR02857 401 VPQ----HPFLFAGTIAENIRLARPDASDAEIREA---LERAGLDEfvaalpqgldtPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 152 MHQPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAE 200
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAA 521
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-229 |
7.30e-29 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.21 E-value: 7.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKD---IVNAK 77
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrDKDgqlKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 RQLGL-------VPQEFNFNPFETVLQIVVNQ-AGYYGVTRREAMARAEKYLNQLDLwgkrNERARM-----LSGGMKRR 144
Cdd:PRK10619 85 NQLRLlrtrltmVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGI----DERAQGkypvhLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 145 LMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLL 224
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
....*
gi 1398598869 225 AKLKS 229
Cdd:PRK10619 241 GNPQS 245
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-226 |
8.15e-29 |
|
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: 110.40 E-value: 8.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAG-GVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGL 82
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQE-FNFNpfETVLQivvNQA-GYYGVTRREAM-----ARAEKYLNQLDLWGKRN--ERARMLSGGMKRRLMIARALMH 153
Cdd:cd03251 81 VSQDvFLFN--DTVAE---NIAyGRPGATREEVEeaaraANAHEFIMELPEGYDTVigERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTII----LTThyLEEAEMLCrnigIIQNGELVENTSMKGLLAK 226
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMKNRTTFViahrLST--IENADRIV----VLEDGKIVERGTHEELLAQ 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-298 |
1.41e-28 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 115.88 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV 83
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQefnfnpFETVLQIVVNQAGYY------GVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:TIGR01257 2018 PQ------FDAIDDLLTGREHLYlyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLkSETFILDLA 237
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKF-GDGYIVTMK 2170
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 238 AKSP----LPKLDGYHSRLtdTSTLEVEVMREQGLNGLFTQLSAQGV----QVLSMRNKANRLEELFVT 298
Cdd:TIGR01257 2171 IKSPkddlLPDLNPVEQFF--QGNFPGSVQRERHYNMLQFQVSSSSLarifQLLISHKDSLLIEEYSVT 2237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-232 |
2.24e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.07 E-value: 2.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYagGVKALRgIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVnAKRQLGLVP 84
Cdd:COG3840 2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIV---VNQAGYYGVTRREAMARAekyLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:COG3840 78 QENNLFPHLTVAQNIglgLRPGLKLTAEQRAQVEQA---LERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSETF 232
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-214 |
2.35e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 2.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGGvKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLV--NKTAGS-VRVFGYDID------K 71
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQH-QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQregrlaR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 72 DIVNAKRQLGLVPQEFNFNPFETVLQIVVnqAGYYGVT----------RREAMARAEKYLNQLDLWGKRNERARMLSGGM 141
Cdd:PRK09984 80 DIRKSRANTGYIFQQFNLVNRLSVLENVL--IGALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 142 KRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-199 |
2.50e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI--DKDIVNAKRQLGLVPQefnfNP-FETVL 96
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTsdEENLWDIRNKAGMVFQ----NPdNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 QIVVNQAGY----YGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELR 172
Cdd:PRK13633 101 TIVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180
....*....|....*....|....*...
gi 1398598869 173 RSMWGFLKELNAQ-GTTIILTTHYLEEA 199
Cdd:PRK13633 181 REVVNTIKELNKKyGITIILITHYMEEA 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-199 |
4.56e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.58 E-value: 4.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDkDIVNAKRQLGLVP 84
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVnqagyYG-----VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLI 159
Cdd:PRK09452 93 QSYALFPHMTVFENVA-----FGlrmqkTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1398598869 160 LDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEA 199
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEA 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-199 |
5.62e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.80 E-value: 5.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDivNAKRql 80
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP--GADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:COG4525 79 GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEA 199
Cdd:COG4525 159 DEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
5.79e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 109.79 E-value: 5.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG----VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKD-------- 72
Cdd:PRK13651 3 IKVKNIVKIFNKKlpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 73 --------------IVNAK---RQLGLVPQEFNFNPFE-TVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERA 134
Cdd:PRK13651 83 vleklviqktrfkkIKKIKeirRRVGVVFQFAEYQLFEqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 135 RM-LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEA-EMLCRNIgIIQNG 212
Cdd:PRK13651 163 PFeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVlEWTKRTI-FFKDG 241
|
...
gi 1398598869 213 ELV 215
Cdd:PRK13651 242 KII 244
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-216 |
7.00e-28 |
|
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: 108.74 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG--------VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVN 75
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 76 AK---RQLGLVPQEF--NFNPFETVLQIVVNQAGYYgvTRREAMARAEKYLNQLDLWGKRNE----RARMLSGGMKRRLM 146
Cdd:TIGR02769 83 RRafrRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHL--TSLDESEQKARIAELLDMVGLRSEdadkLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 147 IARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
1.05e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.01 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLtKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KTAGSVRVFGYDI---DKD 72
Cdd:PRK14267 1 MKFAIETVNL-RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIyspDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 73 IVNAKRQLGLVPQEFNFNPFETVLQIVVNQAGYYGV--TRREAMARAEKYLNQLDLW----GKRNERARMLSGGMKRRLM 146
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWdevkDRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 147 IARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQgTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-228 |
3.16e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.56 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 9 QLTKTYAGGV----KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-----DKDIVNAKRQ 79
Cdd:PRK13646 7 NVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQEFNFNPFE-TVLQIVVNQAGYYGVTRREAMARAEKYLnqLDLWGKRNERAR---MLSGGMKRRLMIARALMHQP 155
Cdd:PRK13646 87 IGMVFQFPESQLFEdTVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSQspfQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLK 228
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-225 |
3.50e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.13 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 10 LTKTYAGGvKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVN--AKRQLGLVPQEF 87
Cdd:PRK10895 9 LAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHarARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 N-------FNPFETVLQIVVNqagyygVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:PRK10895 88 SifrrlsvYDNLMAVLQIRDD------LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 161 DEPTAGVD----IELRRsmwgFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLA 225
Cdd:PRK10895 162 DEPFAGVDpisvIDIKR----IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-230 |
4.04e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 4.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KTAGSVRVFGYDIDK-DIVNAKRQLGLVPQEFNF 89
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 90 NP----FETV-LQIVVNQAGYygvTRREAMARAEKYLNQLDLWGKRNER----ARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:PRK14247 94 IPnlsiFENVaLGLKLNRLVK---SKKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQgTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE 230
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-190 |
4.16e-27 |
|
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: 105.59 E-value: 4.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYA----GGVK--ALRGIDLSVEAGDFYALLGPNGAGKSTTIGII--SSLVnkTAGSVRVFGYDIDKD 72
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYLP--DSGSILVRHDGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 73 IVNA---------KRQLGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLD----LWGkrnerarmL-- 137
Cdd:COG4778 79 LAQAspreilalrRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNlperLWD--------Lpp 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 138 ---SGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTII 190
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-215 |
8.32e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 105.62 E-value: 8.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID--KDIVNAKRqLG 81
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwSPAELARR-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEFNFN-PFeTVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALM------HQ 154
Cdd:PRK13548 80 VLPQHSSLSfPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 155 PKLLILDEPTAGVDIE-----LRrsmwgFLKEL-NAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13548 159 PRWLLLDEPTSALDLAhqhhvLR-----LARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-225 |
1.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.68 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-----DKDIVNAKRQLGLVPQEFNFNPFE 93
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKKLRKKVSLVFQFPEAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 94 -TVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM-LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL 171
Cdd:PRK13641 101 nTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 172 RRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLA 225
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-194 |
2.05e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 108.71 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 13 TYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQE-FNFN 90
Cdd:COG1132 348 SYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDtFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 pfETVLQivvNQAgyYG---VTR---REA--MARAEKYLNQLD------LwgkrNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:COG1132 428 --GTIRE---NIR--YGrpdATDeevEEAakAAQAHEFIEALPdgydtvV----GERGVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1398598869 157 LLILDEPTAGVDIE----LRRSmwgfLKELnAQGTTIILTTH 194
Cdd:COG1132 497 ILILDEATSALDTEtealIQEA----LERL-MKGRTTIVIAH 533
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-307 |
2.16e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 106.74 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTtiGIISSLVNKTAGSVRVFGYDI-------DKDIVNA 76
Cdd:NF000106 13 AVEVRGLVKHF-GEVKAVDGVDLDVREGTVLGVLGP*GAA**R--GALPAHV*GPDAGRRPWRF*TwcanrraLRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KRQLGLVPQEfNFNPFETVLQIvvnqAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:NF000106 90 HRPVR*GRRE-SFSGRENLYMI----GR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSETFILDL 236
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 237 AAKSPLPK---------LDGYHSRLTD--TSTLEVEVMREQGLNGLFTQLSAQGVQVLSMRNKANRLEELFVTLVNGNGE 305
Cdd:NF000106 245 AHAAELDRmvgaiaqagLDGIAGATADheDGVVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAITGQKTS 324
|
..
gi 1398598869 306 KA 307
Cdd:NF000106 325 EA 326
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-245 |
3.84e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.50 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLV 83
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQefnfNPFETVLQIVVNQAGYYGVTR----REAMA-RAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLL 158
Cdd:PRK13652 84 FQ----NPDDQIFSPTVEQDIAFGPINlgldEETVAhRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 159 ILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV------ENTSMKGLLAKLKset 231
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVaygtveEIFLQPDLLARVH--- 236
|
250
....*....|....
gi 1398598869 232 fiLDLaakSPLPKL 245
Cdd:PRK13652 237 --LDL---PSLPKL 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-230 |
4.47e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 103.59 E-value: 4.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVN------KTAGSVRVFGYDIDK-DIVNAKRQLGLVPQEFNFNPFE 93
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 94 TVLQIVVNQAGYYGVT-RREAMARAEKYLNQLDLWGKRNER----ARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVD 168
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 169 IELRRSMWGFLKELNAQgTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE 230
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNE 246
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-223 |
4.91e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 107.32 E-value: 4.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLV--------------NKTAGSVRvfg 66
Cdd:PRK13549 2 MEYLLEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgtyegeiifegeELQASNIR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 67 yDID-KDIVNAKRQLGLVPQEfnfnpfeTVLQIVV--NQAGYYGVTRREAM-ARAEKYLNQLDLWGKRNERARMLSGGMK 142
Cdd:PRK13549 78 -DTErAGIAIIHQELALVKEL-------SVLENIFlgNEITPGGIMDYDAMyLRAQKLLAQLKLDINPATPVGNLGLGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 143 RRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKG 222
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAG 229
|
.
gi 1398598869 223 L 223
Cdd:PRK13549 230 M 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-194 |
6.35e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 7 LAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRvfgydIDKDIvnakrQLGLVPQE 86
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-----IPKGL-----RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 87 FNFNPFETVLQIVVNQAGYYGVTRRE------AM--------------------------ARAEKYLNQLDLwGKRNERA 134
Cdd:COG0488 70 PPLDDDLTVLDTVLDGDAELRALEAEleeleaKLaepdedlerlaelqeefealggweaeARAEEILSGLGF-PEEDLDR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 135 RM--LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRsmW--GFLKELNAqgtTIILTTH 194
Cdd:COG0488 149 PVseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPG---TVLVVSH 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-226 |
8.67e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.39 E-value: 8.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 2 NYALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID---KDIVNAKR 78
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 79 QLGLVPQEFNFNPFE-TVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:PRK13636 83 SVGMVFQDPDNQLFSaSVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAK 226
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-199 |
1.65e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.09 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDivNAKRqlGLV 83
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP--GAER--GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1398598869 164 TAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEA 199
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-215 |
2.02e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.50 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-----DKDIVNAKRQLGLVPQEFNFNPFE 93
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstskQKEIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 94 -TVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM-LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL 171
Cdd:PRK13643 100 eTVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1398598869 172 RRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13643 180 RIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-214 |
2.15e-25 |
|
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: 99.60 E-value: 2.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKA-LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQ-LGL 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFnpFE-TVLQIVvnqagyygvtrreamaraekylnqldlwgkrnerarmLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03246 81 LPQDDEL--FSgSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRnIGIIQNGEL 214
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADR-ILVLEDGRV 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-215 |
2.34e-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: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 25 DLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVnAKRQLGLVPQEFNFNPFETVLQIV---VN 101
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP-ADRPVSMLFQENNLFAHLTVEQNVglgLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 102 QAGYYGVTRREAMARAekyLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKE 181
Cdd:cd03298 97 PGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1398598869 182 LNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:cd03298 174 LHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-212 |
2.79e-25 |
|
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: 101.26 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 3 YALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNaKRQLGL 82
Cdd:cd03296 1 MSIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFNPFETVLQIVVnqagyYGVTRREAMARAEKY-----------LNQLDLWGKR--NErarmLSGGMKRRLMIAR 149
Cdd:cd03296 79 VFQHYALFRHMTVFDNVA-----FGLRVKPRSERPPEAeirakvhellkLVQLDWLADRypAQ----LSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 150 ALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNG 212
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-226 |
3.81e-25 |
|
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: 100.77 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 14 YAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQEfnfnpf 92
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQD------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 93 eTVL---QIVVNQAgyYG---VTRRE--AMARA-----------EKYLNQLdlwgkrNERARMLSGGMKRRLMIARALMH 153
Cdd:cd03253 84 -TVLfndTIGYNIR--YGrpdATDEEviEAAKAaqihdkimrfpDGYDTIV------GERGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAeMLCRNIGIIQNGELVENTSMKGLLAK 226
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
10-215 |
5.04e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 101.66 E-value: 5.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 10 LTKTYAGGV----KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAK---RQLGL 82
Cdd:PRK13637 8 LTHIYMEGTpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdirKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFNPFE-TVLQIVVNQAGYYGVTRREAMARAEKYLN--QLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLI 159
Cdd:PRK13637 88 VFQYPEYQLFEeTIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 160 LDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-261 |
5.41e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 104.36 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGgVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLG--L 82
Cdd:PRK15439 12 LCARSISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFNPFETVLQIVVnqagyYGVTRRE-AMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:PRK15439 91 VPQEPLLFPNLSVKENIL-----FGLPKRQaSMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 162 EPTAGVD-IELRRsMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVentsMKGLLAKLKSETFIldlAAKS 240
Cdd:PRK15439 166 EPTASLTpAETER-LFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA----LSGKTADLSTDDII---QAIT 237
|
250 260
....*....|....*....|.
gi 1398598869 241 PLPKLDGyhsrLTDTSTLEVE 261
Cdd:PRK15439 238 PAAREKS----LSASQKLWLE 254
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-225 |
1.10e-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: 103.64 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAG-GVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGL 82
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQE---FNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRN--ERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:TIGR02203 411 VSQDvvlFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPigENGVLLSGGQRQRLAIARALLKDAPI 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRnIGIIQNGELVENTSMKGLLA 225
Cdd:TIGR02203 491 LILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLSTIEKADR-IVVMDDGRIVERGTHNELLA 556
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-216 |
1.32e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 98.76 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 12 KTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVrvfgyDIDKDIVNakrqlglvPQEFN--F 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-----TVRGRVSS--------LLGLGggF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 90 NPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDI 169
Cdd:cd03220 96 NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 170 ELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-216 |
1.67e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.34 E-value: 1.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKST---TIGIISSLV--NKTAGSVRVFGYDI---DKD 72
Cdd:COG1117 8 LEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIpgARVEGEILLDGEDIydpDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 73 IVNAKRQLGLVPQefNFNPF-----ETVLqivvnqagyYGV------TRREAMARAEKYLNQLDLW----GKRNERARML 137
Cdd:COG1117 87 VVELRRRVGMVFQ--KPNPFpksiyDNVA---------YGLrlhgikSKSELDEIVEESLRKAALWdevkDRLKKSALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 138 SGGMKRRLMIARALMHQPKLLILDEPTAGVD------IElrrsmwGFLKELnAQGTTIILTTHYLEEAEMLCRNIGIIQN 211
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakIE------ELILEL-KKDYTIVIVTHNMQQAARVSDYTAFFYL 228
|
....*
gi 1398598869 212 GELVE 216
Cdd:COG1117 229 GELVE 233
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-216 |
2.38e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.45 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIdKDIVNAKRQLGLVP 84
Cdd:PRK11607 20 LEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:PRK11607 98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 165 AGVDIELRRSM-WGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK11607 178 GALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
2.76e-24 |
|
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: 98.31 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDivNAKRQLglVPQEFNFNPFETVLQ--- 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP--GPDRMV--VFQNYSLLPWLTVREnia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 98 IVVNQAgYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWG 177
Cdd:TIGR01184 77 LAVDRV-LPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1398598869 178 FLKEL-NAQGTTIILTTHYLEEAEMLCRNIGIIQNG 212
Cdd:TIGR01184 156 ELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-194 |
2.80e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 2.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfGYDIdkdivnakrQLGLVP 84
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEF-NFNPFETVLQIVvnQAGYYGVTRREAMAraekYLNQLDLWGKR-NERARMLSGGMKRRLMIARALMHQPKLLILDE 162
Cdd:COG0488 385 QHQeELDPDKTVLDEL--RDGAPGGTEQEVRG----YLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458
|
170 180 190
....*....|....*....|....*....|..
gi 1398598869 163 PTAGVDIELRRSMWGFLKELnaQGtTIILTTH 194
Cdd:COG0488 459 PTNHLDIETLEALEEALDDF--PG-TVLLVSH 487
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
3.26e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.92 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRV--------------FGYDIDKDIVNAKRQLGLV 83
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelITNPYSKKIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFE----TVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM-LSGGMKRRLMIARALMHQPKLL 158
Cdd:PRK13631 119 SMVFQFPEYQlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFgLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 159 ILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-195 |
7.17e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.45 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKST---TI-GIISSLVnkTAGSVRVFGYDIDKDIVN--AKRQLGLV---PQEFNFNP 91
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTlakVLmGHPKYEV--TSGSILLDGEDILELSPDerARAGIFLAfqyPVEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDL---WGKR--NERarmLSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:COG0396 94 VSNFLRTALNARRGEELSAREFLKLLKEKMKELGLdedFLDRyvNEG---FSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180
....*....|....*....|....*....
gi 1398598869 167 VDIELRRSMWGFLKELNAQGTTIILTTHY 195
Cdd:COG0396 171 LDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-215 |
7.40e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 97.49 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 15 AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDkDIVNAK--RQLGLVPQ--EFNFn 90
Cdd:COG4559 11 LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLA-AWSPWElaRRRAVLPQhsSLAF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFeTVLQIVvnQAGYY--GVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARAL-------MHQPKLLILD 161
Cdd:COG4559 89 PF-TVEEVV--ALGRAphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 162 EPTAGVDI-------ELrrsmwgfLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG4559 166 EPTSALDLahqhavlRL-------ARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-194 |
7.92e-24 |
|
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: 96.08 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVN--KTAGSVRVFGYDIDKDivNAKRQLGLVPQEFNFNPFETVlqi 98
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTLTV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 vvnqagyygvtrREAMARAEKYlnqldlwgkrneraRMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGF 178
Cdd:cd03213 100 ------------RETLMFAAKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170
....*....|....*.
gi 1398598869 179 LKELNAQGTTIILTTH 194
Cdd:cd03213 154 LRRLADTGRTIICSIH 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-199 |
9.08e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.39 E-value: 9.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKdiVNAK-RQLGL 82
Cdd:PRK10851 2 SIEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARdRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFNPFETVLQivvNQAgyYGVT---RREAMARAE------KYLNQLDLWGKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK10851 79 VFQHYALFRHMTVFD---NIA--FGLTvlpRRERPNAAAikakvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEA 199
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEA 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
7-216 |
9.66e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 97.07 E-value: 9.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 7 LAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidkdivnakRQLGLVpqE 86
Cdd:COG1134 28 LLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----------RVSALL--E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 87 FN--FNPFETVLQIVVNQAGYYGVTRREAMAR-------AE--KYLNQldlwgkrneRARMLSGGMKRRLMIARALMHQP 155
Cdd:COG1134 95 LGagFHPELTGRENIYLNGRLLGLSRKEIDEKfdeivefAElgDFIDQ---------PVKTYSSGMRARLAFAVATAVDP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 156 KLLILDEPTAGVDIELR-RSMwGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:COG1134 166 DILLVDEVLAVGDAAFQkKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-200 |
1.28e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.97 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-KDIvNAKRQLGLVPQEFNFNPFETVLQI 98
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDI-ATRRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 VVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGF 178
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180
....*....|....*....|...
gi 1398598869 179 LKELN-AQGTTIILTTHYLEEAE 200
Cdd:NF033858 440 LIELSrEDGVTIFISTHFMNEAE 462
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-203 |
1.33e-23 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 97.26 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIvnAKRQLGLV 83
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL--QKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFN-PFETVLQIVV--NQAGYYGVTRR---EAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:PRK15056 84 PQSEEVDwSFPVLVEDVVmmGRYGHMGWLRRakkRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLC 203
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
1.51e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.40 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfGydiDKDIVNAKRQLGLVPQE------FNFnP- 91
Cdd:PRK13634 21 RALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-G---ERVITAGKKNKKLKPLRkkvgivFQF-Pe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 ---FE-TVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM-LSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:PRK13634 96 hqlFEeTVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398598869 167 VDIELRRSMWGFLKELN-AQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-222 |
2.11e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.04 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAK---- 77
Cdd:PRK11629 6 LQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 -RQLGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:PRK11629 86 nQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGiIQNGELVENTSMKG 222
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTAELSLMG 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-223 |
2.16e-23 |
|
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: 99.90 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLV--NKTAGSVRVFGYDIDKDIVNAKRQLGL 82
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 V--PQEFNFNPFETVLQIV-----VNQAGyyGVTRREAMA-RAEKYLNQLDLWGKRNERARM-LSGGMKRRLMIARALMH 153
Cdd:TIGR02633 81 ViiHQELTLVPELSVAENIflgneITLPG--GRMAYNAMYlRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGL 223
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
9-194 |
2.25e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 95.71 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 9 QLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAKRQLGLVP 84
Cdd:PRK10908 6 HVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190
....*....|....*....|....*....|
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:PRK10908 166 GNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
2.35e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.62 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIV-NAKR 78
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 79 QLGLVPQefnfNP---F--ETVLQIVV----NQagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIAR 149
Cdd:PRK13635 82 QVGMVFQ----NPdnqFvgATVQDDVAfgleNI----GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 150 ALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGT-TIILTTHYLEEAEMLCRNIgIIQNGELVE 216
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVI-VMNKGEILE 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-226 |
2.70e-23 |
|
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: 95.68 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 17 GVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIdKDIVNA--KRQLGLVPQEfnfnP--F 92
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLNLRwlRSQIGLVSQE----PvlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 93 ETvlQIVVNQA-GYYGVTRREAMARAEKYL---------NQLD-LWGkrnERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03249 90 DG--TIAENIRyGKPDATDEEVEEAAKKANihdfimslpDGYDtLVG---ERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYL---EEAEmlcrNIGIIQNGELVENTSMKGLLAK 226
Cdd:cd03249 165 EATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLstiRNAD----LIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-226 |
3.64e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.51 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 2 NYALELAQLTKTYAGG-VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQ- 79
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQa 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQE---FN-----------FNPFETVLQIVVNQAGYygvtrreamaraEKYLNQ---LDLW-GkrnERARMLSGGM 141
Cdd:PRK11160 416 ISVVSQRvhlFSatlrdnlllaaPNASDEALIEVLQQVGL------------EKLLEDdkgLNAWlG---EGGRQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 142 KRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRnIGIIQNGELVENTSMK 221
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQFDR-ICVMDNGQIIEQGTHQ 558
|
....*
gi 1398598869 222 GLLAK 226
Cdd:PRK11160 559 ELLAQ 563
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-200 |
4.07e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.43 E-value: 4.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDivnAKRQLG- 81
Cdd:NF033858 1 VARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMaDAR---HRRAVCp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 ---LVPQEFNFNPFETvLQIVVNQ---AGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQP 155
Cdd:NF033858 77 riaYMPQGLGKNLYPT-LSVFENLdffGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNAQ--GTTIILTTHYLEEAE 200
Cdd:NF033858 156 DLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAE 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-263 |
4.56e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.51 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDkdivNAKRQLGLVP 84
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA----EAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVvnQAGYYGVTRreamARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:PRK11247 88 QDARLLPWKKVIDNV--GLGLKGQWR----DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELventsmkGllaklksetfiLDLAAKSPLP 243
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI-------G-----------LDLTVDLPRP 223
|
250 260
....*....|....*....|
gi 1398598869 244 KLDGYHsRLtdtSTLEVEVM 263
Cdd:PRK11247 224 RRRGSA-RL---AELEAEVL 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-194 |
6.71e-23 |
|
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: 94.26 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNK---TAGSVRVFGYDIDKDIVnaKRQLGLVPQEFNFNPF-- 92
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQF--QKCVAYVRQDDILLPGlt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 93 --ETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:cd03234 98 vrETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....
gi 1398598869 171 LRRSMWGFLKELNAQGTTIILTTH 194
Cdd:cd03234 178 TALNLVSTLSQLARRNRIVILTIH 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-196 |
8.59e-23 |
|
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: 98.20 E-value: 8.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGLV 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQE---FNfnpfETVLQIVVNQAGyyGVTRREAMARAEKYlnQLDLWGKR---------NERARMLSGGMKRRLMIARAL 151
Cdd:TIGR02868 415 AQDahlFD----TTVRENLRLARP--DATDEELWAALERV--GLADWLRAlpdgldtvlGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 152 MHQPKLLILDEPTAGVDIELRRSMwgfLKELNA--QGTTIILTTHYL 196
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADEL---LEDLLAalSGRTVVLITHHL 530
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-194 |
9.19e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.08 E-value: 9.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGG---VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL- 80
Cdd:PRK10584 7 VEVHHLKKSVGQGeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 ----GLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLwGKR-NERARMLSGGMKRRLMIARALMHQP 155
Cdd:PRK10584 87 akhvGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGL-GKRlDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTH 194
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTH 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-215 |
9.72e-23 |
|
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: 93.81 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQE---FN----- 88
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDvtlFYgtlrd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 89 ----FNPF---ETVLQiVVNQAGYYGVTRREAmaraekylNQLDLwgKRNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:cd03245 97 nitlGAPLaddERILR-AAELAGVTDFVNKHP--------NGLDL--QIGERGRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 162 EPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRNIgIIQNGELV 215
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRII-VMDSGRIV 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-226 |
1.75e-22 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 93.44 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 14 YAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKR-QLGLVPQE---FNF 89
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRsMIGVVLQDtflFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 90 NPFETVLqivvnqagyYG--VTRREAMARAEKYLNQLDLWGKR--------NERARMLSGGMKRRLMIARALMHQPKLLI 159
Cdd:cd03254 92 TIMENIR---------LGrpNATDEEVIEAAKEAGAHDFIMKLpngydtvlGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 160 LDEPTAGVDIELRRSMWGFLKELNAQGTTII----LTThyLEEAEMlcrnIGIIQNGELVENTSMKGLLAK 226
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIiahrLST--IKNADK----ILVLDDGKIIEEGTHDELLAK 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-225 |
1.99e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK----DIVNAKRQLGLVPQEF--NFNPFET 94
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIQMVFQDSisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 95 VLQIVVNQAGYY-GVTRREAMARAEKYLNQLDL-WGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELR 172
Cdd:PRK10419 108 VREIIREPLRHLlSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 173 RSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLA 225
Cdd:PRK10419 188 AGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-212 |
3.05e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 95.17 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNaKRQLGLVP 84
Cdd:PRK11432 7 VVLKNITKRF-GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETVLQIVvnqaGY----YGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:PRK11432 85 QSYALFPHMSLGENV----GYglkmLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEA-----EMLCRNIG-IIQNG 212
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAfavsdTVIVMNKGkIMQIG 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-239 |
5.05e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.13 E-value: 5.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVN-AKRQLG 81
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQefnfNPFETVLQIVVNQAGYYG-----VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:PRK13632 87 IIFQ----NPDNQFIGATVEDDIAFGlenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQGT-TIILTTHYLEEAeMLCRNIGIIQNGELVENTSMKGLL--------AKL 227
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILnnkeilekAKI 241
|
250
....*....|..
gi 1398598869 228 KSeTFILDLAAK 239
Cdd:PRK13632 242 DS-PFIYKLSKK 252
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-215 |
5.31e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.77 E-value: 5.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKdiVNAK---RQLG 81
Cdd:PRK11231 3 LRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM--LSSRqlaRRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQefnfnpfetvlQIVVNQagyyGVTRREAMARAEK-YLNqldLWGKRNERARM---------------------LSG 139
Cdd:PRK11231 80 LLPQ-----------HHLTPE----GITVRELVAYGRSpWLS---LWGRLSAEDNArvnqameqtrinhladrrltdLSG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 140 GMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK11231 142 GQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-224 |
9.72e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.85 E-value: 9.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK--DIVNAKRQLGL 82
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFNFNPFETVLQ-------IVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQP 155
Cdd:PRK09700 85 IYQELSVIDELTVLEnlyigrhLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGE-----LVENTSMKGLL 224
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSNDDIV 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
14-233 |
1.38e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 14 YAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KTAGSVRVFGYDI---DKDIVNAKRQLGLVPQ 85
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 86 EFNFNPFeTVLQIVVNQAGYYGVTRREAMARA-EKYLNQLDLWGKRNER----ARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:PRK14239 94 QPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAvEKSLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQgTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLL---AKLKSETFI 233
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFmnpKHKETEDYI 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-223 |
1.67e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.21 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGgVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFG----YDIDKDIVNAKrqL 80
Cdd:PRK11288 5 LSFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrFASTTAALAAG--V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETV-----LQIVVNQAGYygVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQP 155
Cdd:PRK11288 82 AIIYQELHLVPEMTVaenlyLGQLPHKGGI--VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVEN-TSMKGL 223
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-215 |
2.24e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 92.47 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 24 IDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFG---YDIDKDIVNA--KRQLGLVPQE---FnfnPFETV 95
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIFLPphRRRIGYVFQEarlF---PHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 96 LQivvNQAgyYGVTRREAMARAEKYLNQLDLWG-----KRneRARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:COG4148 95 RG---NLL--YGRKRAPRAERRISFDEVVELLGighllDR--RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1398598869 171 LRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG4148 168 RKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-216 |
2.35e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.17 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 26 LSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKdIVNA------KRQLGLVPQEFNFNPFETVLQIV 99
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK-ISDAelrevrRKKIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 100 VNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFL 179
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 1398598869 180 KELNAQGT-TIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK10070 208 VKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-226 |
3.18e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.87 E-value: 3.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 14 YAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIdKDIVNA--KRQLGLVPQE---FN 88
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI-RTVTRAslRRNIAVVFQDaglFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 89 FNPFEtvlQIVVNQAGYYGVTRREAMARAEKylnqLDLWGKR--------NERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:PRK13657 423 RSIED---NIRVGRPDATDEEMRAAAERAQA----HDFIERKpdgydtvvGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQGTTIILtTHYL---EEAEMlcrnIGIIQNGELVENTSMKGLLAK 226
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGRTTFII-AHRLstvRNADR----ILVFDNGRVVESGSFDELVAR 559
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-226 |
3.89e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.63 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQEfnfnPFETVL 96
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQE----PVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 QIVVNQAgyYGVTR--REAMARAEKYLNQLDLWGKR--------NERARMLSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:TIGR00958 570 SVRENIA--YGLTDtpDEEIMAAAKAANAHDFIMEFpngydtevGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 167 VDIELRRSmwgFLKELNAQGTTIILTTHYLEEAEMlCRNIGIIQNGELVENTSMKGLLAK 226
Cdd:TIGR00958 648 LDAECEQL---LQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-226 |
4.16e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 89.85 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 15 AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQE---FNFN 90
Cdd:cd03252 12 PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQEnvlFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFETVlqivvnQAGYYGVTRRE-----AMARAEKYLNQLDLWGKR--NERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:cd03252 92 IRDNI------ALADPGMSMERvieaaKLAGAHDFISELPEGYDTivGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 164 TAGVDIELRRSMWGFLKELNAqGTTIILTTHYLeEAEMLCRNIGIIQNGELVENTSMKGLLAK 226
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICA-GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-195 |
6.28e-21 |
|
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: 88.35 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKST---TI-GIISSLVnkTAGSVRVFGYDIDKDIVN--AKRQLGLVPQEfnf 89
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTImGHPKYEV--TEGEILFKGEDITDLPPEerARLGIFLAFQY--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 90 nPFEtvlqivvnqagYYGVTRREAMaraeKYLNQldlwGkrnerarmLSGGMKRRLMIARALMHQPKLLILDEPTAGVDI 169
Cdd:cd03217 86 -PPE-----------IPGVKNADFL----RYVNE----G--------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180
....*....|....*....|....*.
gi 1398598869 170 ELRRSMWGFLKELNAQGTTIILTTHY 195
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHY 163
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-225 |
6.39e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 6.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 23 GIDLSVEAGDFYALLGPNGAGKSTTIGII-----SSLVNKTAGSVRVFGYDI---DKDIVNAKR--QLGLVPQE--FNFN 90
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSIlrllpSPPVVYPSGDIRFHGESLlhaSEQTLRGVRgnKIAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFETVLQIVVNQAGYYGVTRREAmARAEkYLNQLDLWGKRNERARM------LSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:PRK15134 107 PLHTLEKQLYEVLSLHRGMRREA-ARGE-ILNCLDRVGIRQAAKRLtdyphqLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLA 225
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-216 |
1.08e-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: 92.05 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 12 KTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTT----IGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL-----GL 82
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnriAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQE--FNFNPFETV-LQIVVNQAGYYGVTRREAMARAEKYLNQLdlwGKRNERARM------LSGGMKRRLMIARALMH 153
Cdd:COG4172 97 IFQEpmTSLNPLHTIgKQIAEVLRLHRGLSGAAARARALELLERV---GIPDPERRLdayphqLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVE 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-225 |
1.13e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.78 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQ 79
Cdd:PRK11614 2 EKVMLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 -LGLVPQEFNFNPFETVLQIVVnqAGYYGVTRREAMARAEKYLNQLD-LWGKRNERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:PRK11614 81 aVAIVPEGRRVFSRMTVEENLA--MGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLA 225
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-222 |
3.24e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.62 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIIS----------SLVNKtaGSVRVFGyDI----D 70
Cdd:NF040905 2 LEMRGITKTF-PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgsyegEILFD--GEVCRFK-DIrdseA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 71 KDIVNAKRQLGLVPQefnfnpfetvLQI-----VVNQAGYYGV-TRREAMARAEKYLNQLDLwgkrNERARMLSGGM--- 141
Cdd:NF040905 78 LGIVIIHQELALIPY----------LSIaenifLGNERAKRGViDWNETNRRARELLAKVGL----DESPDTLVTDIgvg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 142 KRRLM-IARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSM 220
Cdd:NF040905 144 KQQLVeIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDC 223
|
..
gi 1398598869 221 KG 222
Cdd:NF040905 224 RA 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-194 |
3.48e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 6 ELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID--KDIVNAKRqLGLV 83
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAttPSRELAKR-LAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPFETVLQIVvnQAGYYGVTR-------REAMARAEKYLNQLDLWGKR-NErarmLSGGMKRRLMIARALMHQP 155
Cdd:COG4604 81 RQENHINSRLTVRELV--AFGRFPYSKgrltaedREIIDEAIAYLDLEDLADRYlDE----LSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1398598869 156 KLLILDEPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTH 194
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-215 |
6.57e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGgVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQ- 79
Cdd:PRK10762 1 MQALLQLKGIDKAFPG-VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 -LGLVPQEFNFNPFETVLQIV------VNQAGyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALM 152
Cdd:PRK10762 80 gIGIIHQELNLIPQLTIAENIflgrefVNRFG--RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 153 HQPKLLILDEPT-AGVDIElRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK10762 158 FESKVIIMDEPTdALTDTE-TESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-226 |
7.11e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 89.69 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGL 82
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFN-FNpfETVLQ-IVVNQAGYYgvTRRE-----AMARAEKYLNQLD--LWGKRNERARMLSGGMKRRLMIARALMH 153
Cdd:PRK11176 422 VSQNVHlFN--DTIANnIAYARTEQY--SREQieeaaRMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILtTHYL---EEAEMlcrnIGIIQNGELVENTSMKGLLAK 226
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLstiEKADE----ILVVEDGEIVERGTHAELLAQ 568
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-214 |
7.89e-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: 88.25 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 24 IDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFG---YDIDKDIVNA--KRQLGLVPQEFNFNPFETVLQI 98
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKGIFLPpeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 VVnqagyYGVTR---REAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSM 175
Cdd:TIGR02142 96 LR-----YGMKRarpSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1398598869 176 WGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:TIGR02142 171 LPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-194 |
1.31e-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: 83.27 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfgydidkdivNAKRQLGLVP 84
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------GSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QefnfnpfetvlqivvnqagyygvtrreamaraekylnqldlwgkrnerarmLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 1398598869 165 AGVDIELRRSMWGFLKELNAqgtTIILTTH 194
Cdd:cd03221 99 NHLDLESIEALEEALKEYPG---TVILVSH 125
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-214 |
1.97e-19 |
|
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: 83.64 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLG--LVPQEfnfnpfetvl 96
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGiaYVPED---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 qivvnqagyygvtRREA-----MARAEKYLNqldlwgkrnerARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL 171
Cdd:cd03215 84 -------------RKREglvldLSVAENIAL-----------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1398598869 172 RRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-228 |
1.97e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVkALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAG----------SVRVFGYdidKDI 73
Cdd:PRK14271 21 AMAAVNLTLGFAGKT-VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllgGRSIFNY---RDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 74 VNAKRQLGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERAR----MLSGGMKRRLMIAR 149
Cdd:PRK14271 97 LEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 150 ALMHQPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLK 228
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-194 |
2.87e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVrvfgyDIDKDIVN----AKRQ 79
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-----WIGGRVVNelepADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQEFNFNPFETVLQivvNQAgyYG-----VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQ 154
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRE---NMA--YGlkirgMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVRE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1398598869 155 PKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTH 194
Cdd:PRK11650 153 PAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTH 193
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-231 |
3.04e-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: 84.34 E-value: 3.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 23 GIDLSVEAGDFYALLGPNGAGKSTT----IGIISSLVNKTAGSVRVFGYDIDKDIVNAkRQLGLVPQE--FNFNPFETVL 96
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDGRPLLPLSIRG-RHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 QIVVNQAGYYGVTRREAMARAekyLNQLDLWGKRNER------ARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALI---LEALEAVGLPDPEevlkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 171 LRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSET 231
Cdd:TIGR02770 160 NQARVLKLLRELRQLfGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHET 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-225 |
4.41e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYA--GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-KDIVNAK 77
Cdd:PRK13642 1 MNKILEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 RQLGLVPQEFNfNPF--ETVLQIVVNQAGYYGVTRREAMARAEKYL---NQLDLwgKRNERARmLSGGMKRRLMIARALM 152
Cdd:PRK13642 81 RKIGMVFQNPD-NQFvgATVEDDVAFGMENQGIPREEMIKRVDEALlavNMLDF--KTREPAR-LSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRnIGIIQNGELVENTSMKGLLA 225
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAASSDR-ILVMKAGEIIKEAAPSELFA 229
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-194 |
4.55e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 84.66 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVPQEFNFNPFE-- 93
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFRem 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 94 TVLQ-IVVNQ---------AGY-----YGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLL 158
Cdd:PRK11300 96 TVIEnLLVAQhqqlktglfSGLlktpaFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1398598869 159 ILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTH 194
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEH 212
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-216 |
6.22e-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: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGvKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfgydIDKD--------IVNA 76
Cdd:TIGR02323 4 LQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATY----IMRSgaelelyqLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KRQLgLVPQEFNF---NPFETvLQIVVNQAG------------YYGVTRreamARAEKYLNQLDLWGKR-NERARMLSGG 140
Cdd:TIGR02323 79 ERRR-LMRTEWGFvhqNPRDG-LRMRVSAGAnigerlmaigarHYGNIR----ATAQDWLEEVEIDPTRiDDLPRAFSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 141 MKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-219 |
8.12e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.40 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIV-NAKRQLGLVPQEFNfNPF--ETVLQ 97
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKIGMVFQNPD-NQFvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 98 IVVNQAGYYGVTRREAMARAEKYLNQLDLWG-KRNERARmLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMW 176
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDfKEREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1398598869 177 GFLKELNAQ-GTTIILTTHYLEEAEMLCRNIgIIQNGElVENTS 219
Cdd:PRK13650 181 KTIKGIRDDyQMTVISITHDLDEVALSDRVL-VMKNGQ-VESTS 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-199 |
8.67e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 8.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 2 NYALELAQLTkTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLvNKTAGSVRVFG---------YDIDKD 72
Cdd:PRK14243 8 ETVLRTENLN-VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRL-NDLIPGFRVEGkvtfhgknlYAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 73 IVNAKRQLGLVPQEFNfnPFETvlQIVVNQA------GYYGvtrrEAMARAEKYLNQLDLWGKRNERARM----LSGGMK 142
Cdd:PRK14243 86 PVEVRRRIGMVFQKPN--PFPK--SIYDNIAygarinGYKG----DMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 143 RRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQgTTIILTTHYLEEA 199
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQA 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-215 |
1.09e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTyaggvKALRGIDLSVEAGD---FYALLGpngAGKSTTIGIISSLVNKTAGSVRVFGYDID-KDIVNAKRQ 79
Cdd:COG1129 256 VLEVEGLSVG-----GVVRDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 -LGLVPQE-------------FNfnpfeTVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLwgK---RNERARMLSGGMK 142
Cdd:COG1129 328 gIAYVPEDrkgeglvldlsirEN-----ITLASLDRLSRGGLLDRRRERALAEEYIKRLRI--KtpsPEQPVGNLSGGNQ 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 143 RRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-247 |
1.18e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.57 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 12 KTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKS----TTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL-----GL 82
Cdd:COG4170 14 DTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKIigreiAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEFN--FNPFETVL-QIVvnQA-------GYYGVTRREAMARAEKYLNQLdlwGKRNERARM------LSGGMKRRLM 146
Cdd:COG4170 94 IFQEPSscLDPSAKIGdQLI--EAipswtfkGKWWQRFKWRKKRAIELLHRV---GIKDHKDIMnsypheLTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 147 IARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLL- 224
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILk 248
|
250 260 270
....*....|....*....|....*....|..
gi 1398598869 225 --------AKLKS-ETFILDLAAKSPLPKLDG 247
Cdd:COG4170 249 sphhpytkALLRSmPDFRQPLPHKSRLNTLPG 280
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
16-205 |
2.17e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfgydidkdivNAKRQLGLVPQEFNFNPFE-- 93
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR----------NGKLRIGYVPQKLYLDTTLpl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 94 TVLQIVVNQAGyygvTRREAMARAEKYLNQLDLWgkrNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRR 173
Cdd:PRK09544 85 TVNRFLRLRPG----TKKEDILPALKRVQAGHLI---DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1398598869 174 SMWGFLKEL-NAQGTTIILTTHYL-----EEAEMLCRN 205
Cdd:PRK09544 158 ALYDLIDQLrRELDCAVLMVSHDLhlvmaKTDEVLCLN 195
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
2.36e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.67 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYD-IDKDIV---NAKRQL 80
Cdd:PRK11701 7 LSVRGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYalsEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 ------GLVPQefnfNPFETvLQIVVNQAG------------YYGVTRREA---MARAEKYLNQLDlwgkrnERARMLSG 139
Cdd:PRK11701 86 llrtewGFVHQ----HPRDG-LRMQVSAGGnigerlmavgarHYGDIRATAgdwLERVEIDAARID------DLPTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 140 GMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-215 |
2.63e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID---KDIVNAKRQLGLVPQEFNFNPFETVLQ 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskRGLLALRQQVATVFQDPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 98 I-VVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMW 176
Cdd:PRK13638 97 SdIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1398598869 177 GFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK13638 177 AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIL 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-214 |
3.25e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 22 RGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV---------------PQE 86
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrqssglyldaPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 87 FNfnpfetVLQIVVNQAGYYGVTRREAmARAEKYLNQLDL-WGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTA 165
Cdd:PRK15439 360 WN------VCALTHNRRGFWIKPAREN-AVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 166 GVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-214 |
3.42e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.93 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 7 LAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDkDIVNAKRQLGLVPQE 86
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 87 FNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 167 VDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-172 |
3.89e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 83.09 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYA---------GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-- 69
Cdd:PRK11308 2 QQPLLQAIDLKKHYPvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 70 -DKDIVNAKRQ-LGLVPQefN----FNPFETVLQI-----VVNqagyygvTRREAMARAEKYLNQLDLWGKRNERA---- 134
Cdd:PRK11308 82 aDPEAQKLLRQkIQIVFQ--NpygsLNPRKKVGQIleeplLIN-------TSLSAAERREKALAMMAKVGLRPEHYdryp 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1398598869 135 RMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELR 172
Cdd:PRK11308 153 HMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-194 |
4.50e-18 |
|
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: 84.41 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKA-LRGIDLSVEAGDFYALLGPNGAGKST----TIGIISSlvnkTAGSVRVFGYDIDK-DIVNAKR 78
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTlarlLVGVWPP----TAGSVRLDGADLSQwDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 79 QLGLVPQEFNFnpFE-TVLQivvNQAGYYGVTRREAMARAEK-------------YLNQLDlwgkrnERARMLSGGMKRR 144
Cdd:COG4618 407 HIGYLPQDVEL--FDgTIAE---NIARFGDADPEKVVAAAKLagvhemilrlpdgYDTRIG------EGGARLSGGQRQR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398598869 145 LMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-194 |
4.89e-18 |
|
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: 80.61 E-value: 4.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTyAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVP 84
Cdd:cd03231 1 LEADELTCE-RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEfnfNPFETVLQIVVNQAGYYGVTRREAMARAekyLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03231 80 HA---PGIKTTLSVLENLRFWHADHSDEQVEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
170 180 190
....*....|....*....|....*....|
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:cd03231 154 TALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-227 |
6.38e-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: 83.70 E-value: 6.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYA----GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVN----- 75
Cdd:TIGR03269 280 IKVRNVSKRYIsvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKpgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 76 ---AKRQLGLVPQEFNFNPFETVLQivvNQAGYYGVTRREAMARaEKYLNQLDLWGKRNERAR--------MLSGGMKRR 144
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPHRTVLD---NLTEAIGLELPDELAR-MKAVITLKMVGFDEEKAEeildkypdELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 145 LMIARALMHQPKLLILDEPTAGVD-IELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGL 223
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
....
gi 1398598869 224 LAKL 227
Cdd:TIGR03269 516 VEEL 519
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-215 |
6.80e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.57 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQL-GL 82
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLvGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQefnfNPFETVLQIVVNQAGYYG-----VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKL 157
Cdd:PRK13644 82 VFQ----NPETQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 158 LILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIgIIQNGELV 215
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRII-VMDRGKIV 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-196 |
7.62e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 82.46 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 12 KTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNK---TAGSVRVFGydidKDIVN-AKRQLGLVPQE- 86
Cdd:PRK09473 23 STPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNG----REILNlPEKELNKLRAEq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 87 ----F-----NFNPFETV---LQIVVNQagYYGVTRREAMARAEKYLNQLDLWGKRnERARM----LSGGMKRRLMIARA 150
Cdd:PRK09473 99 ismiFqdpmtSLNPYMRVgeqLMEVLML--HKGMSKAEAFEESVRMLDAVKMPEAR-KRMKMypheFSGGMRQRVMIAMA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 151 LMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYL 196
Cdd:PRK09473 176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDL 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-214 |
8.12e-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: 80.59 E-value: 8.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGLVPQEfnfnPFETVLQIV 99
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIsQYEHKYLHSKVSLVGQE----PVLFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 100 VNQA-GYYGVTRREAMARAEKY-------LNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL 171
Cdd:cd03248 106 DNIAyGLQSCSFECVKEAAQKAhahsfisELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1398598869 172 RRSMWGFLKELNaQGTTIILTTHYLEEAEMlCRNIGIIQNGEL 214
Cdd:cd03248 186 EQQVQQALYDWP-ERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-168 |
1.18e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 81.70 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTY----------AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIV 74
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG----QDIT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 75 NAK--------RQLGLVPQefnfNPFE------TVLQIVVNQAGYYGV-TRREAMARAEKYLNQLDLwgkRNERAR---- 135
Cdd:COG4608 84 GLSgrelrplrRRMQMVFQ----DPYAslnprmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL---RPEHADryph 156
|
170 180 190
....*....|....*....|....*....|...
gi 1398598869 136 MLSGGMKRRLMIARALMHQPKLLILDEPTAGVD 168
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-200 |
2.58e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.68 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKST----TIGIISSLVNkTAGSVRVFGYDIDkDIVNAKRQL 80
Cdd:COG4136 2 LSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSPAFS-ASGEVLLNGRRLT-ALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEFNFNPFETVLQivvNQAgyYG----VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:COG4136 79 GILFQDDLLFPHLSVGE---NLA--FAlpptIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1398598869 157 LLILDEPTAGVDIELRRSM--WGFlKELNAQGTTIILTTHYLEEAE 200
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFreFVF-EQIRQRGIPALLVTHDEEDAP 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
29-194 |
2.86e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 29 EAGDFYALLGPNGAGKSTTIGIISSLVNK---TAGSVRVFGYDIDKDIVnaKRQLGLVPQEFNFNPFETVLQIVVNQAGY 105
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 106 Y---GVTRREAMARAEKYLNQLDLWGKRN------ERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMW 176
Cdd:TIGR00955 127 RmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170
....*....|....*...
gi 1398598869 177 GFLKELNAQGTTIILTTH 194
Cdd:TIGR00955 207 QVLKGLAQKGKTIICTIH 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-216 |
2.99e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 77.74 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLV 83
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFnpFETVLqivvnqagyygvtrreamaraekylnqldlwgkRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:cd03247 81 NQRPYL--FDTTL---------------------------------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 164 TAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAEMLCRnIGIIQNGELVE 216
Cdd:cd03247 126 TVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHMDK-ILFLENGKIIM 176
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-194 |
3.05e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAK-RQLGlvPQEFnFNPFET 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAcHYLG--HRNA-MKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 95 VLQIVVNQAGYYGvTRREAMARAekyLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRS 174
Cdd:PRK13539 90 VAENLEFWAAFLG-GEELDIAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 1398598869 175 MWGFLKELNAQGTTIILTTH 194
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATH 185
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
16-197 |
4.18e-17 |
|
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: 78.84 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGII----SSLVnkTAGSVRVFGYDIDKDIVNAKRQLGLvpqefnFNP 91
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSYEV--TSGTILFKGQDLLELEPDERARAGL------FLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FETVLQIVvnqagyyGVT-----------RREAMARAE-KYLNQLDLWGKRNERARM------------LSGGMKRRLMI 147
Cdd:TIGR01978 83 FQYPEEIP-------GVSnleflrsalnaRRSARGEEPlDLLDFEKLLKEKLALLDMdeeflnrsvnegFSGGEKKRNEI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398598869 148 ARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLE 197
Cdd:TIGR01978 156 LQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR 205
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-226 |
4.18e-17 |
|
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: 81.40 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIdKDIVNA--KRQLGLVPQefnfnpfETVL-- 96
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-RDVTQAslRAAIGIVPQ-------DTVLfn 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 -QIVVNQAgyYG---VTRREAMARAEkyLNQLD------------LWGkrnERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:COG5265 446 dTIAYNIA--YGrpdASEEEVEAAAR--AAQIHdfieslpdgydtRVG---ERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLE---EAEmlcrNIGIIQNGELVENTSMKGLLAK 226
Cdd:COG5265 519 DEATSALDSRTERAIQAALREV-ARGRTTLVIAHRLStivDAD----EILVLEAGRIVERGTHAELLAQ 582
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-219 |
6.16e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.07 E-value: 6.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 2 NYALELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTtigiISSLVN-------KTAGSVRVFGYDIDKDI 73
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKST----ISKLINglllpddNPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 74 V-NAKRQLGLVPQEFNfNPF--ETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARA 150
Cdd:PRK13640 79 VwDIREKVGIVFQNPD-NQFvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 151 LMHQPKLLILDEPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEAEMlCRNIGIIQNGELVENTS 219
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGS 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-216 |
7.32e-17 |
|
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: 77.45 E-value: 7.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGV-KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGL 82
Cdd:cd03369 7 IEVENLSVRYAPDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQE---------FNFNPFETvlqivvnqagYYGVTRREAMARAEKYLNqldlwgkrnerarmLSGGMKRRLMIARALMH 153
Cdd:cd03369 87 IPQDptlfsgtirSNLDPFDE----------YSDEEIYGALRVSEGGLN--------------LSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKELnAQGTTIILTTHYLEEAeMLCRNIGIIQNGELVE 216
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-216 |
7.70e-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: 80.62 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSL------------------------------ 54
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 55 --VNKTAGSVRVFGYDI----DKDIVNAKRQLGLVPQE-FNFNPFETVLQIVVN---QAGYYGvtrREAMARAEKYLNQL 124
Cdd:TIGR03269 80 epCPVCGGTLEPEEVDFwnlsDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEaleEIGYEG---KEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 125 DLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEAEMLC 203
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLS 236
|
250
....*....|...
gi 1398598869 204 RNIGIIQNGELVE 216
Cdd:TIGR03269 237 DKAIWLENGEIKE 249
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
16-194 |
8.89e-17 |
|
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: 77.01 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 16 GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVPQEFNFNPFETV 95
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 96 LQIVVNQAGYYGVTRREAmaraEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSM 175
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*....
gi 1398598869 176 WGFLKELNAQGTTIILTTH 194
Cdd:TIGR01189 167 AGLLRAHLARGGIVLLTTH 185
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-225 |
1.13e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 78.29 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKT--YAGG------VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID-K 71
Cdd:PRK15112 1 VETLLEVRNLSKTfrYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 72 DIVNAKRQLGLVPQE--FNFNPFETVLQIV-----VNqagyygvTRREAMARAEKYLNQLDLWGKRNERA----RMLSGG 140
Cdd:PRK15112 81 DYSYRSQRIRMIFQDpsTSLNPRQRISQILdfplrLN-------TDLEPEQREKQIIETLRQVGLLPDHAsyypHMLAPG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 141 MKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTS 219
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
....*.
gi 1398598869 220 MKGLLA 225
Cdd:PRK15112 234 TADVLA 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-242 |
1.14e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 9 QLTKTYaGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVnakRQLGLVP 84
Cdd:PRK10253 12 QLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqhyaSKEVA---RRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNfNPFETVLQIVVNQAGY-----YGVTRRE---AMARAEKYLNQLDLwgkRNERARMLSGGMKRRLMIARALMHQPK 156
Cdd:PRK10253 88 QNAT-TPGDITVQELVARGRYphqplFTRWRKEdeeAVTKAMQATGITHL---ADQSVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELN-AQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKSE----- 230
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIEriygl 243
|
250
....*....|....
gi 1398598869 231 --TFILDLAAKSPL 242
Cdd:PRK10253 244 rcMIIDDPVAGTPL 257
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-194 |
1.25e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.53 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVPQEFNFNPF----ETVL 96
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYltlrENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 QIVVNQAGYYGVTRREAMARAEKYLNQldlwgkrneRARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMW 176
Cdd:PRK13540 97 YDIHFSPGAVGITELCRLFSLEHLIDY---------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*...
gi 1398598869 177 GFLKELNAQGTTIILTTH 194
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-219 |
1.51e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.13 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID------KDIVNAKRQLGLVPQEFNFNPF 92
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkiKEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 93 -ETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM-LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:PRK13645 105 qETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398598869 171 LRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTS 219
Cdd:PRK13645 185 GEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-215 |
3.13e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 3.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGL- 82
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVa 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 -VPQE-------------FNFnpfetVLQIVvNQAGY--YGVTRREAM-ARAEKYLNQLDLwgkR----NERARMLSGGM 141
Cdd:COG3845 337 yIPEDrlgrglvpdmsvaENL-----ILGRY-RRPPFsrGGFLDRKAIrAFAEELIEEFDV---RtpgpDTPARSLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 142 KRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-225 |
4.34e-16 |
|
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: 78.63 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQ 79
Cdd:TIGR01193 470 LNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQF 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQEfnfnPF---ETVLQIVVNQAGYyGVTRRE-------AMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIAR 149
Cdd:TIGR01193 550 INYLPQE----PYifsGSILENLLLGAKE-NVSQDEiwaaceiAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 150 ALMHQPKLLILDEPTAGVDIELRRSMWGFLkeLNAQGTTIILTTHYLEEAEMlCRNIGIIQNGELVENTSMKGLLA 225
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-168 |
8.58e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.51 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKT-YAGGV---KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIVNAK--- 77
Cdd:COG1101 2 LELKNLSKTfNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KDVTKLPeyk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 78 --RQLGLVPQefnfNPFE------TVLQivvNQAGYY----------GVTRREaMARAEKYLNQLDLwG--KR-NERARM 136
Cdd:COG1101 78 raKYIGRVFQ----DPMMgtapsmTIEE---NLALAYrrgkrrglrrGLTKKR-RELFRELLATLGL-GleNRlDTKVGL 148
|
170 180 190
....*....|....*....|....*....|..
gi 1398598869 137 LSGGMKRRLMIARALMHQPKLLILDEPTAGVD 168
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-234 |
9.87e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.00 E-value: 9.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGgvKALRgIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDiDKDIVNAKRQLGLVP 84
Cdd:PRK10771 2 LKLTDITWLYHH--LPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 QEFNFNPFETV-----------LQIVVNQAGyygvtRREAMARA---EKYLNQLdlwgkrnerARMLSGGMKRRLMIARA 150
Cdd:PRK10771 78 QENNLFSHLTVaqniglglnpgLKLNAAQRE-----KLHAIARQmgiEDLLARL---------PGQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 151 LMHQPKLLILDEPTAGVDIELRRSMWGFLKEL-NAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLKS 229
Cdd:PRK10771 144 LVREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
....*
gi 1398598869 230 ETFIL 234
Cdd:PRK10771 224 ASALL 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-202 |
1.06e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVN-----KTAGSVRVFGYDIDKDIVNA---KRQLGLVPQEFNFN 90
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRVNLnrlRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PfetvLQIVVNQAgyYGVT------RREAMARAEKYLNQLDLW----GKRNERARMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:PRK14258 101 P----MSVYDNVA--YGVKivgwrpKLEIDDIVESALKDADLWdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQGT-TIILTTHYLEEAEML 202
Cdd:PRK14258 175 DEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
1.43e-15 |
|
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: 76.65 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 15 AGGVKALRGIDLSVEAGDFYALLGPNGAGKSTT----IGIISSlvnktAGSVRVFGYDID----KDIVNAKRQLGLVPQE 86
Cdd:COG4172 296 VGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDglsrRALRPLRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 87 -FN-FNPFETVLQIV-----VNQAGYYGVTRREAMARAekyLNQLDLwgKRNERARM---LSGGMKRRLMIARALMHQPK 156
Cdd:COG4172 371 pFGsLSPRMTVGQIIaeglrVHGPGLSAAERRARVAEA---LEEVGL--DPAARHRYpheFSGGQRQRIAIARALILEPK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:COG4172 446 LLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-253 |
2.47e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 76.21 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSttigiisSLVNKTAGSVRVFGYDIDKDIVNAKR----QL-GLVPQEFNFN--- 90
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKS-------ALARALAGELPLLSGERQSQFSHITRlsfeQLqKLVSDEWQRNntd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 ---PFE-----TVLQIVVNQAgyygvtrrEAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDE 162
Cdd:PRK10938 90 mlsPGEddtgrTTAEIIQDEV--------KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 163 PTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVEntsmKGLLAKLKSETFILDLA----- 237
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAE----TGEREEILQQALVAQLAhseql 237
|
250
....*....|....*.
gi 1398598869 238 AKSPLPKLDGYHSRLT 253
Cdd:PRK10938 238 EGVQLPEPDEPSARHA 253
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-223 |
3.14e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 75.54 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 17 GVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIdkDIVNAKRQL----GLVPQEFNFnpf 92
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFKSSKEALengiSMVHQELNL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 93 etVLQIVVNQAGYYG--------VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:PRK10982 85 --VLQRSVMDNMWLGryptkgmfVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 165 AGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGL 223
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-194 |
6.41e-15 |
|
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: 71.03 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLT-KTYAGGVKaLRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVrvfgydidkdIVNAKRQLGLV 83
Cdd:cd03223 1 IELENLSlATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEFNFNPfetvlqivvnqagyygVTRREAMARAekylnqldlWGkrneraRMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:cd03223 70 PQRPYLPL----------------GTLREQLIYP---------WD------DVLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|.
gi 1398598869 164 TAGVDIELRRSMWGFLKELnaqGTTIILTTH 194
Cdd:cd03223 119 TSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-194 |
8.49e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.59 E-value: 8.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 3 YALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIIsslvnktAGsvrvfgydIDKDIV-NAKRQ-- 79
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG--------VDKDFNgEARPQpg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 --LGLVPQEFNFNPFETVLQIVVN--------QAGYYGVTRR------------EAMARAEKYLNQLDLWG--KRNERA- 134
Cdd:TIGR03719 68 ikVGYLPQEPQLDPTKTVRENVEEgvaeikdaLDRFNEISAKyaepdadfdklaAEQAELQEIIDAADAWDldSQLEIAm 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 135 ---RM---------LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE----LRRsmwgFLKELnaQGtTIILTTH 194
Cdd:TIGR03719 148 dalRCppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLER----HLQEY--PG-TVVAVTH 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-194 |
8.85e-15 |
|
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: 71.51 E-value: 8.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSlvNKTAGSVR----VFGYDIDKDIvnaKRQLGLVPQEFNFNPFETVl 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLDKNF---QRSTGYVEQQDVHSPNLTV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 qivvnqagyygvtrREAMaRAEKYLnqldlwgkrneraRMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMW 176
Cdd:cd03232 97 --------------REAL-RFSALL-------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170
....*....|....*...
gi 1398598869 177 GFLKELNAQGTTIILTTH 194
Cdd:cd03232 149 RFLKKLADSGQAILCTIH 166
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-216 |
1.33e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNkTAGSVRVFGYDID----KDIVNAKRQLGLVPQEFN--FNPFE 93
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHnlnrRQLLPVRHRIQVVFQDPNssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 94 TVLQIV-----VNQAGYYGVTRREAMARAEKYLNqLDLwGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVD 168
Cdd:PRK15134 380 NVLQIIeeglrVHQPTLSAAQREQQVIAVMEEVG-LDP-ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1398598869 169 IELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK15134 458 KTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-216 |
1.57e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTT----IGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL-----GLVPQE--F 87
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSslaiMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLvgaevAMIFQDpmT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 NFNPFETV-LQIV----VNQAGyygvTRREAMARAEKYLNQLdlwGKRNERARM------LSGGMKRRLMIARALMHQPK 156
Cdd:PRK11022 101 SLNPCYTVgFQIMeaikVHQGG----NKKTRRQRAIDLLNQV---GIPDPASRLdvyphqLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-213 |
2.62e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 70.19 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTtigIISSL---VNKTAGSVRVFGydidkdivnakrQLGLVPQEfnfnPF---E 93
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPG------------SIAYVSQE----PWiqnG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 94 TVLQ-IV----VNQAGYYGVTRREAMARAEKYLNQLDLW--GkrnERARMLSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:cd03250 81 TIREnILfgkpFDEERYEKVIKACALEPDLEILPDGDLTeiG---EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 167 VDIELRRSMW-----GFLKElnaqGTTIILTTH---YLEEAEMlcrnIGIIQNGE 213
Cdd:cd03250 158 VDAHVGRHIFencilGLLLN----NKTRILVTHqlqLLPHADQ----IVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
20-216 |
2.95e-14 |
|
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: 70.60 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQE---------FNF 89
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDpvlfsgtirSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 90 NPFETvlqivvnqagYYGVTRREAMARA------EKYLNQLDLwgKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:cd03244 99 DPFGE----------YSDEELWQALERVglkefvESLPGGLDT--VVEEGGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 164 TAGVDIELRRSMWGFLKElNAQGTTIILTTHYLeEAEMLCRNIGIIQNGELVE 216
Cdd:cd03244 167 TASVDPETDALIQKTIRE-AFKDCTVLTIAHRL-DTIIDSDRILVLDKGRVVE 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-212 |
3.97e-14 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 24 IDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFG---YDIDKDIVNA--KRQLGLVPQEFNFNPFETV--- 95
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGICLPpeKRRIGYVFQDARLFPHYKVrgn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 96 LQivvnqagyYGVTRreamARAEKYLNQLDLWG-----KRNERArmLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:PRK11144 97 LR--------YGMAK----SMVAQFDKIVALLGiepllDRYPGS--LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1398598869 171 LRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNG 212
Cdd:PRK11144 163 RKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-216 |
4.02e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRG-IDLSVEAGDFYALLGPNGAGKSttigiisSLVN------KTAGSVRVFGYDI-DKDIVNAKRQLGLV---PQEF 87
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKT-------SLLNallgflPYQGSLKINGIELrELDPESWRKHLSWVgqnPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 -----------NFNPFETVLQIVVNQAGyygvtrreamarAEKYLNQLD--LWGKRNERARMLSGGMKRRLMIARALMHQ 154
Cdd:PRK11174 436 hgtlrdnvllgNPDASDEQLQQALENAW------------VSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQP 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 155 PKLLILDEPTAGVDielRRSMWGFLKELN--AQGTTIILTTHYLEEAEMlCRNIGIIQNGELVE 216
Cdd:PRK11174 504 CQLLLLDEPTASLD---AHSEQLVMQALNaaSRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQ 563
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-194 |
6.01e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.06 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 22 RGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQL-------GLVPQefnFNPFET 94
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIKTE---LTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 95 vLQIvvNQAGYyGVTRREAMARAekyLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP-----TAGVDI 169
Cdd:PRK13538 95 -LRF--YQRLH-GPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPftaidKQGVAR 167
|
170 180
....*....|....*....|....*
gi 1398598869 170 ELRRsmwgFLKELnAQGTTIILTTH 194
Cdd:PRK13538 168 LEAL----LAQHA-EQGGMVILTTH 187
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-221 |
7.21e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 7.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI---DKDIVNAKRQ------------LGL 82
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrSRQVIELSEQsaaqmrhvrgadMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQE--FNFNPFETV-LQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERAR---MLSGGMKRRLMIARALMHQPK 156
Cdd:PRK10261 109 IFQEpmTSLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 157 LLILDEPTAGVDIELRRSMWGFLKELNAQGTT-IILTTHYLEEAEMLCRNIGIIQNGELVENTSMK 221
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-216 |
8.46e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.67 E-value: 8.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLtKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISS--LVNKTAGSVRVFGYDIDKDIVNAKRQLGL 82
Cdd:CHL00131 8 LEIKNL-HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 vpqefnFNPFETVLQI--VVNQ----AGYYgvTRREAMARAE-------KYLNQ-LDLWGKR--------NERarmLSGG 140
Cdd:CHL00131 87 ------FLAFQYPIEIpgVSNAdflrLAYN--SKRKFQGLPEldpleflEIINEkLKLVGMDpsflsrnvNEG---FSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 141 MKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRN-IGIIQNGELVE 216
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDyVHVMQNGKIIK 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-232 |
1.12e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQ---------EFNFN 90
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQspvlfsgtvRFNID 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFETVlqivvNQAGYYGVTRREAMARAEKYlNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:PLN03232 1332 PFSEH-----NDADLWEALERAHIKDVIDR-NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 171 LRRSMWGFLKElNAQGTTIILTTHYLEEAeMLCRNIGIIQNGELVENTSMKGLLAKLKSETF 232
Cdd:PLN03232 1406 TDSLIQRTIRE-EFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-194 |
2.99e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLV--NKTAGSVRVFGYDIDKDIVnakRQLGLVPQEFNFNPFETVLQI 98
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTKQIL---KRTGFVTQDDILYPHLTVRET 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 VVNQAGYY---GVTRREAMARAEKYLNQLDLWGKRN-----ERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:PLN03211 161 LVFCSLLRlpkSLTKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180
....*....|....*....|....
gi 1398598869 171 LRRSMWGFLKELNAQGTTIILTTH 194
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-196 |
4.24e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 4.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVnKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQEFNFNPFETVLQIV 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 100 vnQAGYYGVTRREAMARAEKYL-NQLDLWGKRNERARMLSGGMKRRLMIARALMH-------QPKLLILDEPTAGVDIEL 171
Cdd:COG4138 91 --ALHQPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|....*
gi 1398598869 172 RRSMWGFLKELNAQGTTIILTTHYL 196
Cdd:COG4138 169 QAALDRLLRELCQQGITVVMSSHDL 193
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-196 |
4.33e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.58 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDI----DKDIVNAKRQLGLVPQE--FNFNPF 92
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 93 ETVLQIVVN--QAGYYGVTRREAMARAEKYLNQLDLWGKR-NERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDI 169
Cdd:PRK15079 115 MTIGEIIAEplRTYHPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180
....*....|....*....|....*...
gi 1398598869 170 ELRRSMWGFLKELNAQ-GTTIILTTHYL 196
Cdd:PRK15079 195 SIQAQVVNLLQQLQREmGLSLIFIAHDL 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-216 |
6.55e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGGVkaLRGIDLSVEAGDFYALLGPNGAGKSTT----IGIISSLVNKTAGSVRVFGYDIDKDIVNA 76
Cdd:PRK10418 1 MPQQIELRNIALQAAQPL--VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 kRQLGLVPQ--EFNFNPFETVLQIVVNQAGYYGVTRREAMARAEkyLNQLDLwgkrNERARML-------SGGMKRRLMI 147
Cdd:PRK10418 79 -RKIATIMQnpRSAFNPLHTMHTHARETCLALGKPADDATLTAA--LEAVGL----ENAARVLklypfemSGGMLQRMMI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 148 ARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK10418 152 ALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQkRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-194 |
6.65e-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: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDfyALL--GPNGAGKSTTIGIISSLVNKTAGSVRVfgydidkdivNAKRQLG 81
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIAR----------PAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEfNFNPFETVLQIVV--NQAGYYGVTR-REAMARA--EKYLNQLDL---WGKRnerarmLSGGMKRRLMIARALMH 153
Cdd:COG4178 430 FLPQR-PYLPLGTLREALLypATAEAFSDAElREALEAVglGHLAERLDEeadWDQV------LSLGEQQRLAFARLLLH 502
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMWGFLKElNAQGTTIILTTH 194
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-199 |
1.87e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 66.31 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQ-LGLVPQefnfNPFETVLQI 98
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKhIGIVFQ----NPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 VVNQAGYYG-----VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRR 173
Cdd:PRK13648 100 IVKYDVAFGlenhaVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180
....*....|....*....|....*..
gi 1398598869 174 SMWGFLKELNA-QGTTIILTTHYLEEA 199
Cdd:PRK13648 180 NLLDLVRKVKSeHNITIISITHDLSEA 206
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-225 |
5.77e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.21 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLT---KTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSlVNK-----TAGSVRVFGYDIDKDIVNA 76
Cdd:PRK15093 4 LDIRNLTiefKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKdnwrvTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 77 KRQL-----GLVPQEFN--FNPFETV-LQIVVNQAG--YYGVTRREAMARAEKYLNQLDLWGKRNERARM------LSGG 140
Cdd:PRK15093 83 RRKLvghnvSMIFQEPQscLDPSERVgRQLMQNIPGwtYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMrsfpyeLTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 141 MKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTS 219
Cdd:PRK15093 163 ECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAP 242
|
....*.
gi 1398598869 220 MKGLLA 225
Cdd:PRK15093 243 SKELVT 248
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-194 |
9.55e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 9.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 10 LTKTYAGGVKALRGIDLSveagdFY-----ALLGPNGAGKSTTIGIIsslvnktAGsvrvfgydIDKDIV-NAKRQ---- 79
Cdd:PRK11819 12 VSKVVPPKKQILKDISLS-----FFpgakiGVLGLNGAGKSTLLRIM-------AG--------VDKEFEgEARPApgik 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVPQEFNFNPFETVLQIV------VNQAgyygVTRREA------------------MARAEKYLNQLDLW--GKRNER 133
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVeegvaeVKAA----LDRFNEiyaayaepdadfdalaaeQGELQEIIDAADAWdlDSQLEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 134 ArM--------------LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE----LRRsmwgFLKELnaQGtTIILTTH 194
Cdd:PRK11819 148 A-MdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLEQ----FLHDY--PG-TVVAVTH 218
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-225 |
1.01e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.12 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKR-QLGLVPQefnfNPFETVLQI 98
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRsRLAVVSQ----TPFLFSDTV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 VVNQA-GYYGVTRR--EAMAR-----------AEKYLNQLdlwgkrNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:PRK10789 406 ANNIAlGRPDATQQeiEHVARlasvhddilrlPQGYDTEV------GERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 165 AGVDielRRSMWGFLKELN--AQGTTIILTTHYLE---EAEmlcrNIGIIQNGELVENTSMKGLLA 225
Cdd:PRK10789 480 SAVD---GRTEHQILHNLRqwGEGRTVIISAHRLSaltEAS----EILVMQHGHIAQRGNHDQLAQ 538
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-199 |
2.95e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIIS-----------SLVNKTAGSVRVFgYDIDKDIVNAKRQLGLvpqEFNF 89
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLFGRRRGSGETI-WDIKKHIGYVSSSLHL---DYRV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 90 NpfETVLQIVVnqAGYY---GVTRreAMARAEKYLNQ--LDLWGKRNERA----RMLSGGMKRRLMIARALMHQPKLLIL 160
Cdd:PRK10938 352 S--TSVRNVIL--SGFFdsiGIYQ--AVSDRQQKLAQqwLDILGIDKRTAdapfHSLSWGQQRLALIVRALVKHPTLLIL 425
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1398598869 161 DEPTAGVDIELRRSMWGFLKELNAQGTTIIL-TTHYLEEA 199
Cdd:PRK10938 426 DEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAEDA 465
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-170 |
4.08e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVkALRGIDLSVEAGDFYALLGPNGAGKSTtigIISSLVNK---TAGSVrvfgydidKDIVNAkrQL 80
Cdd:PRK15064 319 ALEVENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTT---LLRTLVGElepDSGTV--------KWSENA--NI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 81 GLVPQEfNFNPFETVLQIVVNQAGYYGVTRREAMARAekYLNQLdLWGKR--NERARMLSGGMKRRLMIARALMHQPKLL 158
Cdd:PRK15064 385 GYYAQD-HAYDFENDLTLFDWMSQWRQEGDDEQAVRG--TLGRL-LFSQDdiKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|..
gi 1398598869 159 ILDEPTAGVDIE 170
Cdd:PRK15064 461 VMDEPTNHMDME 472
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-224 |
4.74e-11 |
|
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: 63.78 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 10 LTKTYA-GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNkTAGSVRVFGYDIDKDIVNAKRQ-LGLVPQEF 87
Cdd:TIGR01271 1223 LTAKYTeAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKaFGVIPQKV 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 ---------NFNPFETV----LQIVVNQAGYYGVTrreamaraEKYLNQLDLwgKRNERARMLSGGMKRRLMIARALMHQ 154
Cdd:TIGR01271 1302 fifsgtfrkNLDPYEQWsdeeIWKVAEEVGLKSVI--------EQFPDKLDF--VLVDGGYVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 155 PKLLILDEPTAGVDIELRRSMWGFLKELNAQgTTIILTTHYLeEAEMLCRNIGIIQNGELVENTSMKGLL 224
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-216 |
7.70e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLglvp 84
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 85 qeF-----NFNPFETVLqivvNQAGYygvtrREAMARAEKYLNQLDLWGK-RNERARM----LSGGMKRRLMIARALMHQ 154
Cdd:PRK10522 399 --FsavftDFHLFDQLL----GPEGK-----PANPALVEKWLERLKMAHKlELEDGRIsnlkLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1398598869 155 PKLLILDEPTAGVDIELRRSMWG-FLKELNAQGTTIILTTH---YLEEAEMLCRnigiIQNGELVE 216
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHddhYFIHADRLLE----MRNGQLSE 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-216 |
8.94e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID----KDIVNAKRQLGLVPQE--FNFNP 91
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FETVLQIVVNQAGYYGVTRREAMARAEKYLnqLDLWGKRNERA----RMLSGGMKRRLMIARALMHQPKLLILDEPTAGV 167
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPGKAAAARVAWL--LERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398598869 168 DIELRRSMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-216 |
9.12e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 9.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 19 KALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID--KDIVNAKRQLGLVPQEFNFNPFETVL 96
Cdd:PRK09700 277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYITESRRDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 QIVVNQA--------GYYG----VTRREAMARAEKYLNQLDL-WGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:PRK09700 357 SIAQNMAisrslkdgGYKGamglFHEVDEQRTAENQRELLALkCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1398598869 164 TAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVE 216
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-194 |
1.23e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.36 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKST----TIGIISSLvnKTAGSVRVFGYDIDKD--IVNAkrqlglVPQEFNFNpfeT 94
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTllrlLAGALKGT--PVAGCVDVPDNQFGREasLIDA------IGRKGDFK---D 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 95 VLQiVVNQAGyygvtrreamaraekyLNQLDLWgKRneRARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL-RR 173
Cdd:COG2401 115 AVE-LLNAVG----------------LSDAVLW-LR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTaKR 174
|
170 180
....*....|....*....|.
gi 1398598869 174 SMWGFLKELNAQGTTIILTTH 194
Cdd:COG2401 175 VARNLQKLARRAGITLVVATH 195
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-194 |
1.87e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKT--YAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKR 78
Cdd:PRK10247 1 MQENSPLLQLQNVgyLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 79 Q----LGLVPQEFNfnpfETVLQivvNQAGYYGVtrREAMARAEKYLNQLDLWGKRNE----RARMLSGGMKRRLMIARA 150
Cdd:PRK10247 81 QqvsyCAQTPTLFG----DTVYD---NLIFPWQI--RNQQPDPAIFLDDLERFALPDTiltkNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1398598869 151 LMHQPKLLILDEPTAGVDIELRRSMWGFLKELNA-QGTTIILTTH 194
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVReQNIAVLWVTH 196
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-224 |
1.91e-10 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 60.25 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYA-GGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNkTAGSVRVFGYDIDKDIVNAKRQ-LGL 82
Cdd:cd03289 3 MTVKDLTAKYTeGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKaFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEF---------NFNPFET----VLQIVVNQAGYYGVTrreamaraEKYLNQLDLwgKRNERARMLSGGMKRRLMIAR 149
Cdd:cd03289 82 IPQKVfifsgtfrkNLDPYGKwsdeEIWKVAEEVGLKSVI--------EQFPGQLDF--VLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 150 ALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAqGTTIILTTHYLeEAEMLCRNIGIIQNGELVENTSMKGLL 224
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-175 |
2.03e-10 |
|
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: 61.10 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYagGVKAL-RGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfgydidKDIVnakrQLGLV 83
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETV----KLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 84 PQEF-NFNPFETVLQIVVNQAGYYGVTRREAMARAekYLNQLDLWGK-RNERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:TIGR03719 391 DQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGSdQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
170
....*....|....
gi 1398598869 162 EPTAGVDIELRRSM 175
Cdd:TIGR03719 469 EPTNDLDVETLRAL 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
130-191 |
2.43e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 2.43e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 130 RNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIIL 191
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL 450
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-194 |
2.61e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 25 DLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRvfgydIDKDIVNAKRQLGlVPQEFNFNPFETVLQIVVNQAG 104
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII-----YEQDLIVARLQQD-PPRNVEGTVYDFVAEGIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 105 ----YYGVTRREAMARAEKYLNQL----------DLW------------------GKRNErarmLSGGMKRRLMIARALM 152
Cdd:PRK11147 97 ylkrYHDISHLVETDPSEKNLNELaklqeqldhhNLWqlenrinevlaqlgldpdAALSS----LSGGWLRKAALGRALV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELnaQGtTIILTTH 194
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISH 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-215 |
6.44e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.65 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKdiVNAK---RQLGLVPQEFNFNPFETVLQ 97
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES--WSSKafaRKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 98 IV-VNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARM---LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRR 173
Cdd:PRK10575 105 LVaIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1398598869 174 SMWGFLKELNAQ-GTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK10575 185 DVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-195 |
6.92e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTtigIISSLVNK-----TAGSVRVFGYDIdkdivnakrqLGLVPQEFN----FNP 91
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKST---LSATLAGRedyevTGGTVEFKGKDL----------LELSPEDRAgegiFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FETVLQI--VVNQagYYGVTRREAMA--RAEKYLNQLDLWGKRNERARML---------------SGGMKRRLMIARALM 152
Cdd:PRK09580 84 FQYPVEIpgVSNQ--FFLQTALNAVRsyRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1398598869 153 HQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHY 195
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-169 |
7.72e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.75 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQ---------EFNFN 90
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQapvlfsgtvRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PF----ETVLQIVVNQAGYYGVTRReamaraekylNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAG 166
Cdd:PLN03130 1335 PFnehnDADLWESLERAHLKDVIRR----------NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
...
gi 1398598869 167 VDI 169
Cdd:PLN03130 1405 VDV 1407
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-172 |
1.14e-09 |
|
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: 57.80 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 13 TYAGGVKALRGIDLSVEAGDFY-----ALLGPNGAGKSTTIGIISSLVNKTAGSVrvfgyDIDKDIVNAKrqlglvPQEF 87
Cdd:cd03237 2 TYPTMKKTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI-----EIELDTVSYK------PQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 NFNPFETV---LQIVVNQAGYYGVTRREAMaraekylNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPT 164
Cdd:cd03237 71 KADYEGTVrdlLSSITKDFYTHPYFKTEIA-------KPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
....*...
gi 1398598869 165 AGVDIELR 172
Cdd:cd03237 144 AYLDVEQR 151
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
3-226 |
1.72e-09 |
|
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: 58.80 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 3 YALELAQLTKTYAGGVK-ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfgydidkdivnaKRQLG 81
Cdd:TIGR00957 635 NSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 LVPQEF---NFNPFETVLQIVVNQAGYYgvtrrEAMARAEKYLNQLDLW--GKRNE---RARMLSGGMKRRLMIARALMH 153
Cdd:TIGR00957 703 YVPQQAwiqNDSLRENILFGKALNEKYY-----QQVLEACALLPDLEILpsGDRTEigeKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 154 QPKLLILDEPTAGVDIELRRSMW-------GFLKelnaqGTTIILTTH---YLEEAEMlcrnIGIIQNGELVENTSMKGL 223
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHVGKHIFehvigpeGVLK-----NKTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQEL 848
|
...
gi 1398598869 224 LAK 226
Cdd:TIGR00957 849 LQR 851
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-208 |
2.69e-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: 55.06 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIgiisslvnktagsvrvfgydidkdivnakRQLGLVpqefnfnpfetVLQIVV 100
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTIL-----------------------------DAIGLA-----------LGGAQS 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 101 NQAGYYGVTRREAMARAEKYLNQLDLwgkrnerarMLSGGMKRRLMIARALMHQPK----LLILDEPTAGVDIELRRSMW 176
Cdd:cd03227 51 ATRRRSGVKAGCIVAAVSAELIFTRL---------QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|..
gi 1398598869 177 GFLKELNAQGTTIILTTHYLEEAEMLCRNIGI 208
Cdd:cd03227 122 EAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-226 |
2.93e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 4 ALELAQLTKTYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQ-LGL 82
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQgVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 83 VPQEfnfnpfetvlQIVVNQAGYYGVT-----RREAMARAEKYLnQLDLWGKR---------NERARMLSGGMKRRLMIA 148
Cdd:PRK10790 420 VQQD----------PVVLADTFLANVTlgrdiSEEQVWQALETV-QLAELARSlpdglytplGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 149 RALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQgTTIILTTHYLE---EAEmlcrNIGIIQNGELVENTSMKGLLA 225
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLStivEAD----TILVLHRGQAVEQGTHQQLLA 563
|
.
gi 1398598869 226 K 226
Cdd:PRK10790 564 A 564
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2-194 |
4.02e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 2 NYALELAQLTKTYAGgvkalrgidlSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVfGYDIDKDIVNAKRQlg 81
Cdd:PRK11147 326 NYQIDGKQLVKDFSA----------QVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRA-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 82 lvpqefNFNPFETVL--------QIVVNqagyyGVTRReamarAEKYLNQLDLWGKRnerARM----LSGGMKRRLMIAR 149
Cdd:PRK11147 393 ------ELDPEKTVMdnlaegkqEVMVN-----GRPRH-----VLGYLQDFLFHPKR---AMTpvkaLSGGERNRLLLAR 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1398598869 150 ALMHQPKLLILDEPTAGVDIELRRsmwgFLKEL--NAQGtTIILTTH 194
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLE----LLEELldSYQG-TVLLVSH 495
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-169 |
4.75e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGiisSLVNKTAGSVRVFGYDIDKDI-VNAK-----------RQLGLVPQE-- 86
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLK---ALAGDLTGGGAPRGARVTGDVtLNGEplaaidaprlaRLRAVLPQAaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 87 --FNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARAL---------MHQP 155
Cdd:PRK13547 94 paFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170
....*....|....
gi 1398598869 156 KLLILDEPTAGVDI 169
Cdd:PRK13547 174 RYLLLDEPTAALDL 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
18-215 |
4.97e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRG------IDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDID----KDIVNA--------KRQ 79
Cdd:PRK11288 260 LDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirspRDAIRAgimlcpedRKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LGLVP----QE-------FNFNPFETVLQivvnqagyygvTRREAmARAEKYLNQLDLWGKRNERARM-LSGGMKRRLMI 147
Cdd:PRK11288 340 EGIIPvhsvADninisarRHHLRAGCLIN-----------NRWEA-ENADRFIRSLNIKTPSREQLIMnLSGGNQQKAIL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 148 ARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-168 |
5.89e-09 |
|
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: 54.96 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTA---GSVRVFGYDIDKDIVNAKRQLGLVPQEFNFNPFETVLQ 97
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 98 IVvnqagyygvtrrEAMARAekylnqldlwgKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVD 168
Cdd:cd03233 103 TL------------DFALRC-----------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-214 |
9.81e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 9.81e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 137 LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-170 |
1.02e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.49 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKST-TIGIISslVNKTA-GSVRVFGYDIDK-DIVNAKRQLGLVPQEfnfnP--FETV 95
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSlTLGLFR--INESAeGEIIIDGLNIAKiGLHDLRFKITIIPQD----PvlFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 96 LQIVVNQAGYYG---VTRREAMARAEKYLNQL--DLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE 170
Cdd:TIGR00957 1376 LRMNLDPFSQYSdeeVWWALELAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
137-214 |
1.33e-08 |
|
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: 55.60 E-value: 1.33e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 137 LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGEL 214
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-194 |
1.41e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 24 IDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidKDIVNAKRQ-----LGLVPQefnfnpFETVLQI 98
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG----KTATRGDRSrfmayLGHLPG------LKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 VVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIE---LRRSM 175
Cdd:PRK13543 100 LENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEgitLVNRM 179
|
170
....*....|....*....
gi 1398598869 176 wgFLKELNAQGTTiILTTH 194
Cdd:PRK13543 180 --ISAHLRGGGAA-LVTTH 195
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-197 |
2.51e-08 |
|
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: 53.49 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 13 TYAGGVKALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQLGLVPQEFNFN-P 91
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQkP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FetVLQIVVNQAGYYGV----TRREAMARAEKYLNQLDL--WGKRN---ERARMLSGGMKRRLMIARALMHQPKLLILDE 162
Cdd:cd03290 89 W--LLNATVEENITFGSpfnkQRYKAVTDACSLQPDIDLlpFGDQTeigERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1398598869 163 PTAGVDIELRRSMW--GFLKELNAQGTTIILTTHYLE 197
Cdd:cd03290 167 PFSALDIHLSDHLMqeGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-175 |
3.17e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRV-----FGYdidkdivNAKRQLglvpqEFnFNPFETV 95
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLakgikLGY-------FAQHQL-----EF-LRADESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 96 LQIVVNQAgyygvtRREAMARAEKYLNQLDLWG-KRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRS 174
Cdd:PRK10636 395 LQHLARLA------PQELEQKLRDYLGGFGFQGdKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQA 468
|
.
gi 1398598869 175 M 175
Cdd:PRK10636 469 L 469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-240 |
4.74e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 20 ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGyDIDKDIVNAkrqlGLVPQEFNFNPFETVLQIV 99
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISA----GLSGQLTGIENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 100 vnqagyyGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFL 179
Cdd:PRK13546 114 -------GFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKI 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 180 KELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVENTSMKGLLAKLksETFILDLAAKS 240
Cdd:PRK13546 187 YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY--EAFLNDFKKKS 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
52-168 |
4.85e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.26 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 52 SSLVNKTAGSVRVFGYDI-DKDIVNAKRQLGLVPQE---FNFNPFETVlqivvnQAGYYGVTRrEAMARAEKYL------ 121
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEpmlFNMSIYENI------KFGKEDATR-EDVKRACKFAaidefi 1341
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1398598869 122 ----NQLDL----WGKRnerarmLSGGMKRRLMIARALMHQPKLLILDEPTAGVD 168
Cdd:PTZ00265 1342 eslpNKYDTnvgpYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-198 |
7.27e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.46 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 24 IDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK----DIVNAKRQLGLVPQE----FNFNPFETV 95
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRLYTVRKRMSMLFQSgalfTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 96 lqivvnqagyyGVTRREAMARAEKYLN-----QLDLWGKRNERARM---LSGGMKRRLMIARALMHQPKLLILDEPTAGV 167
Cdd:PRK11831 106 -----------AYPLREHTQLPAPLLHstvmmKLEAVGLRGAAKLMpseLSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190
....*....|....*....|....*....|..
gi 1398598869 168 DIELRRSMWGFLKELN-AQGTTIILTTHYLEE 198
Cdd:PRK11831 175 DPITMGVLVKLISELNsALGVTCVVVSHDVPE 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-239 |
1.72e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 137 LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELVe 216
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA- 470
|
90 100
....*....|....*....|....
gi 1398598869 217 ntsmkGLL-AKLKSETFILDLAAK 239
Cdd:PRK10982 471 -----GIVdTKTTTQNEILRLASL 489
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-172 |
1.80e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFYA-----LLGPNGAGKSTTIGIISSLVNKTAGSVrvfgydiDKDI-VNAKrqlglvPQEFNFNP 91
Cdd:PRK13409 347 TKKLGDFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEV-------DPELkISYK------PQYIKPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FETVLQIVVNQAGYYG-------VTRREAMARA-EKYLNQLdlwgkrnerarmlSGGMKRRLMIARALMHQPKLLILDEP 163
Cdd:PRK13409 414 DGTVEDLLRSITDDLGssyykseIIKPLQLERLlDKNVKDL-------------SGGELQRVAIAACLSRDADLYLLDEP 480
|
....*....
gi 1398598869 164 TAGVDIELR 172
Cdd:PRK13409 481 SAHLDVEQR 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-194 |
2.31e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 13 TYAGGVKA-----LRGIDLSVEAGDFYALLGPNGAGKST---------TIGIIsslvnkTAGSVRVFGYDIDKDIvnaKR 78
Cdd:TIGR00956 766 TYEVKIKKekrviLNNVDGWVKPGTLTALMGASGAGKTTllnvlaervTTGVI------TGGDRLVNGRPLDSSF---QR 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 79 QLGLVPQEFNFNPFETV---LQIVVNQAGYYGVTRREAMARAEKYLNQLDLwgkrNERARMLSG----GM----KRRLMI 147
Cdd:TIGR00956 837 SIGYVQQQDLHLPTSTVresLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEM----ESYADAVVGvpgeGLnveqRKRLTI 912
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1398598869 148 ARALMHQPKLLI-LDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:TIGR00956 913 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
128-194 |
4.71e-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: 4.71e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 128 GKRNERARMLSGGMKR---RLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:pfam13304 228 GGGELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-174 |
5.52e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 38 GPNGAGKSTTIGIISSLVNKTAGSVRVfGydidkDIVnakrQLGLVPQEF-NFNPFETVLQIVVNQAGYYGVTRREAMAR 116
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKI-G-----ETV----KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSR 426
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 117 AekYLNQLDLWG-KRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRS 174
Cdd:PRK11819 427 A--YVGRFNFKGgDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA 483
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-209 |
5.60e-07 |
|
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: 49.67 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 27 SVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSvrvFGYDID-KDIVNAKRQLGLvpQEFnfnpFETVL--------- 96
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDPPDwDEILDEFRGSEL--QNY----FTKLLegdvkvivk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 -----QIVVNQAGYYG--VTRREAMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDI 169
Cdd:cd03236 93 pqyvdLIPKAVKGKVGelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1398598869 170 ELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGII 209
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-194 |
6.73e-07 |
|
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: 48.14 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 31 GDFYALLGPNGAGKSTTIGIISSLVNKTAGSVrvfgydidkdivnakrqlglvpqefnfnpfetvlqIVVNqagyygvtr 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV-----------------------------------IYID--------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 111 reaMARAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRR------SMWGFLKELNA 184
Cdd:smart00382 38 ---GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAllllleELRLLLLLKSE 114
|
170
....*....|
gi 1398598869 185 QGTTIILTTH 194
Cdd:smart00382 115 KNLTVILTTN 124
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-196 |
7.99e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.16 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 27 SVEAGDFYALLGPNGAGKSTTIGIISSLVnKTAGSVRVFGYDIDKDIVN--AKRQLGLVPQEfnfNPfetVLQIVVNQ-- 102
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelARHRAYLSQQQ---TP---PFAMPVFQyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 103 AGYYGVTRREAMARAEKYL--NQLDLWGKRNERARMLSGGMKRR-------LMIARALMHQPKLLILDEPTAGVDIELRR 173
Cdd:PRK03695 91 TLHQPDKTRTEAVASALNEvaEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDVAQQA 170
|
170 180
....*....|....*....|...
gi 1398598869 174 SMWGFLKELNAQGTTIILTTHYL 196
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
134-168 |
1.68e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 1.68e-06
10 20 30
....*....|....*....|....*....|....*
gi 1398598869 134 ARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVD 168
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-194 |
2.13e-06 |
|
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: 47.60 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 38 GPNGAGKSTtigIISSLVNKTAGSVRVF--GYDIDKDIVNAKRQLGLVPQEFNfnpfetvlqivVNQAGYYGVTRREAMA 115
Cdd:cd03240 29 GQNGAGKTT---IIEALKYALTGELPPNskGGAHDPKLIREGEVRAQVKLAFE-----------NANGKKYTITRSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 116 RAEKYLNQLDL-WGKRNERARmLSGGMKR------RLMIARALMHQPKLLILDEPTAGVD-----------IELRRSMWG 177
Cdd:cd03240 95 ENVIFCHQGESnWPLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieeslaeiIEERKSQKN 173
|
170
....*....|....*..
gi 1398598869 178 FLkelnaqgttIILTTH 194
Cdd:cd03240 174 FQ---------LIVITH 181
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-194 |
2.14e-06 |
|
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: 49.03 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 5 LELAQLTKTYAGgVKALRG-----IDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKDIVNAKRQ 79
Cdd:COG4615 328 LELRGVTYRYPG-EDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 80 LglvpqeF-----NFNPFETVlqivvnqagyYGVTRREAMARAEKYLNQLDLWGK---RNER--ARMLSGGMKRRL-MIA 148
Cdd:COG4615 407 L------FsavfsDFHLFDRL----------LGLDGEADPARARELLERLELDHKvsvEDGRfsTTDLSQGQRKRLaLLV 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1398598869 149 rALMHQPKLLILDEPTAGVDIELRRSmwgF----LKELNAQGTTIILTTH 194
Cdd:COG4615 471 -ALLEDRPILVFDEWAADQDPEFRRV---FytelLPELKARGKTVIAISH 516
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
28-194 |
3.12e-06 |
|
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: 48.59 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 28 VEAGDFYALLGPNGAGKSTTIGIISSLVNktagsvrVFGYDIDKDivnAKRQLGLVPQEfnfnPFETVL----QIVVNQA 103
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELWP-------VYGGRLTKP---AKGKLFYVPQR----PYMTLGtlrdQIIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 104 GYYGVTRREAMARAEKYLNQLDL---------WGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRS 174
Cdd:TIGR00954 541 SEDMKRRGLSDKDLEQILDNVQLthilereggWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGY 620
|
170 180
....*....|....*....|
gi 1398598869 175 MWGFLKELnaqGTTIILTTH 194
Cdd:TIGR00954 621 MYRLCREF---GITLFSVSH 637
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-227 |
5.58e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTI-GIISSLVNKTAGSVRVFGydidkdivnakrQLGLVPQE---FNFNPFETVL 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVIRG------------SVAYVPQVswiFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 97 QIVVNQAGYYGvtrREAMARAEKYlnQLDLWGKRN-----ERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL 171
Cdd:PLN03232 701 FGSDFESERYW---RAIDVTALQH--DLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 172 RRSMWGFLKELNAQGTTIILTT---HYLEEAE--MLCRNIGIIQNGELVENTSMKGLLAKL 227
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTnqlHFLPLMDriILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1-203 |
8.44e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 1 MNYALELAQLTKTYAGGVK-------------------ALRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGS 61
Cdd:PRK13545 1 MNYKVKFEHVTKKYKMYNKpfdklkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 62 VrvfgydidkDIvnaKRQLGLVPQEFNFNPFETVLQIVVNQAGYYGVTRREAMARAEKYLNQLDLWGKRNERARMLSGGM 141
Cdd:PRK13545 81 V---------DI---KGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1398598869 142 KRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLC 203
Cdd:PRK13545 149 KSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFC 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-172 |
8.93e-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: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGIDLSVEAGDFY-----ALLGPNGAGKSTTIGIISSLVNKTAGSVrvfgydiDKDI-VNAKrqlglvPQEFNFNP 91
Cdd:COG1245 348 TKSYGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEV-------DEDLkISYK------PQYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 92 FETVLQIVvnqAGYYGVTRREAMARAEkYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIEL 171
Cdd:COG1245 415 DGTVEEFL---RSANTDDFGSSYYKTE-IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
.
gi 1398598869 172 R 172
Cdd:COG1245 491 R 491
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-215 |
1.15e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 1.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1398598869 137 LSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-194 |
3.47e-05 |
|
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: 44.99 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 18 VKALRGI-DLSVE-AGDFYALLGPNGAGKSTTIGIISsLVNKTAGSVRVFGYDI-------------------------- 69
Cdd:COG3593 8 IKNFRSIkDLSIElSDDLTVLVGENNSGKSSILEALR-LLLGPSSSRKFDEEDFylgddpdlpeieieltfgsllsrllr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 70 ----DKDIVNAKRQLGLVPQEFN--FNPFETVLQIVVNQA-GYYGVTRREAMARAEKYLNQLDLWGKRNERARM--LSGG 140
Cdd:COG3593 87 lllkEEDKEELEEALEELNEELKeaLKALNELLSEYLKELlDGLDLELELSLDELEDLLKSLSLRIEDGKELPLdrLGSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 141 MKRRLMIA--RALMH-----QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:COG3593 167 FQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-215 |
6.44e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 113 AMARAEKYLNQLDLWGKRNERA-RMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDieLRRSMWgFLKELNAQGTTIIL 191
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKAtKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLW-LETYLLKWPKTFIV 396
|
90 100
....*....|....*....|....
gi 1398598869 192 TTHYLEEAEMLCRNIGIIQNGELV 215
Cdd:PLN03073 397 VSHAREFLNTVVTDILHLHGQKLV 420
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-168 |
9.07e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.94 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISS-----LVNKTaGSVRVFGYDIDkDIVNAKRQLGL--------VPQEF 87
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgfHIGVE-GVITYDGITPE-EIKKHYRGDVVynaetdvhFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 88 NFNPFETVLQIVVNQAGYYGVTRRE-AMARAEKYLNQLDLWGKR-----NERARMLSGGMKRRLMIARALMHQPKLLILD 161
Cdd:TIGR00956 155 VGETLDFAARCKTPQNRPDGVSREEyAKHIADVYMATYGLSHTRntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQCWD 234
|
....*..
gi 1398598869 162 EPTAGVD 168
Cdd:TIGR00956 235 NATRGLD 241
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-173 |
9.24e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 9.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 21 LRGIDLSVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDK-DIVNAKRQLGLVPQE---------FNFN 90
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAyGLRELRRQFSMIPQDpvlfdgtvrQNVD 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFetvLQivvnqagyygvtrreamARAEKYLNQLDLWGKRnER---------ARMLSGGM-----KRRLM-IARALMHQP 155
Cdd:PTZ00243 1406 PF---LE-----------------ASSAEVWAALELVGLR-ERvasesegidSRVLEGGSnysvgQRQLMcMARALLKKG 1464
|
170
....*....|....*....
gi 1398598869 156 KLLIL-DEPTAGVDIELRR 173
Cdd:PTZ00243 1465 SGFILmDEATANIDPALDR 1483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
137-212 |
1.13e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.92 E-value: 1.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 137 LSGGMKRRLMIARALMHQPK--LLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHYLeeaEMLCRNIGIIQNG 212
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL---DVLSSADWIIDFG 162
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-194 |
1.48e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 31 GDFYALLGPNGAGKSTTIGIISSLVNKTAGSV------RV-------FGYD----IDKDIVnAKRQLGLVPQEFN---FN 90
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsldpneRLgklrqdqFAFEeftvLDTVIM-GHTELWEVKQERDriyAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFET------VLQIVVNQAGYYGVTrreAMARAEKYLNQLDL-----WGKRNERARmlsgGMKRRLMIARALMHQPKLLI 159
Cdd:PRK15064 106 PEMSeedgmkVADLEVKFAEMDGYT---AEARAGELLLGVGIpeeqhYGLMSEVAP----GWKLRVLLAQALFSNPDILL 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1398598869 160 LDEPTAGVDIELRRsmWgFLKELNAQGTTIILTTH 194
Cdd:PRK15064 179 LDEPTNNLDINTIR--W-LEDVLNERNSTMIIISH 210
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-194 |
3.11e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 38 GPNGAGKSTTIGIISSLVNKTAGSVRVFGYDIDKdivNAKRQLGLVPQEFNFNPFETVLQIVVNQAGYYGVTrrEAMARA 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN---IAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSA--ETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1398598869 118 EKYLNQLDLWgkrNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:PRK13541 108 IHYFKLHDLL---DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-209 |
3.98e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.72 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 36 LLGPNGAGKSTTIGIISSL-------VNKTAGSVRVFGY-------DIDKDIVNAKRQLGLVPQEFNFNP--FE-TVLQI 98
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGElipnlgdYEEEPSWDEVLKRfrgtelqNYFKKLYNGEIKVVHKPQYVDLIPkvFKgKVREL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 99 V--VNQAGyygvtrreamaRAEKYLNQLDLWGKRNERARMLSGGMKRRLMIARALMHQPKLLILDEPTAGVDIELRRSMW 176
Cdd:PRK13409 184 LkkVDERG-----------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVA 252
|
170 180 190
....*....|....*....|....*....|...
gi 1398598869 177 GFLKELnAQGTTIILTTHYLEEAEMLCRNIGII 209
Cdd:PRK13409 253 RLIREL-AEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
35-182 |
1.45e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.22 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 35 ALLGPNGAGKST---------------TIGIISSLVNKTAGSVRV-FGYDIDKDIVNAKRQLGLVPQEFNFNP------F 92
Cdd:COG0419 27 LIVGPNGAGKSTileairyalygkarsRSKLRSDLINVGSEEASVeLEFEHGGKRYRIERRQGEFAEFLEAKPserkeaL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 93 ETVLQIVVNQAGYYGVTRREAMARAEkyLNQLDLWGKRNER----------ARMLSGGMKRRLMIARALMhqpklLILDe 162
Cdd:COG0419 107 KRLLGLEIYEELKERLKELEEALESA--LEELAELQKLKQEilaqlsgldpIETLSGGERLRLALADLLS-----LILD- 178
|
170 180
....*....|....*....|
gi 1398598869 163 pTAGVDIELRRSMWGFLKEL 182
Cdd:COG0419 179 -FGSLDEERLERLLDALEEL 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-194 |
1.65e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 27 SVEAGDFYALLGPNGAGKSTTIGIISSLVNKTAGSVRVFGydidkdivnaKRQLGLVPQEF----------------NFN 90
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----------NWQLAWVNQETpalpqpaleyvidgdrEYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 91 PFETVLQIVVNQagyygvTRREAMARAEKYLNQLDLWGKRNERARML-----------------SGGMKRRLMIARALMH 153
Cdd:PRK10636 93 QLEAQLHDANER------NDGHAIATIHGKLDAIDAWTIRSRAASLLhglgfsneqlerpvsdfSGGWRMRLNLAQALIC 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1398598869 154 QPKLLILDEPTAGVDieLRRSMWgFLKELNAQGTTIILTTH 194
Cdd:PRK10636 167 RSDLLLLDEPTNHLD--LDAVIW-LEKWLKSYQGTLILISH 204
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
132-231 |
1.83e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1398598869 132 ERA-RMLSGGMKRRLMIARALMHQPK--LLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTHyleEAEMLC---RN 205
Cdd:PRK00635 471 ERAlATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH---DEQMISladRI 547
|
90 100 110
....*....|....*....|....*....|.
gi 1398598869 206 IGI-----IQNGELVENTSMKGLLAKLKSET 231
Cdd:PRK00635 548 IDIgpgagIFGGEVLFNGSPREFLAKSDSLT 578
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
127-181 |
2.81e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.44 E-value: 2.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1398598869 127 WGKRNERARMLSGGMKRRLM---IARALMHQ----------PKLLILDEPTAGVDIELRRSMWGFLKE 181
Cdd:pfam13558 23 EVETYRRSGGLSGGEKQLLAylpLAAALAAQygsaegrppaPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
138-195 |
3.76e-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: 38.00 E-value: 3.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1398598869 138 SGGMKRrlmIARALMHQPK--LLILDEPTAGVDIE----LRRSmwgFLKELNAQGTTIILTTHY 195
Cdd:cd03280 93 SSHMKN---IARILQHADPdsLVLLDELGSGTDPVegaaLAIA---ILEELLERGALVIATTHY 150
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-194 |
5.47e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 5.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1398598869 137 LSGGMKRRLMIARALMH---QPKLLILDEPTAGVDIELRRSMWGFLKELNAQGTTIILTTH 194
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| |
