|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-233 |
2.80e-106 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 309.30 E-value: 2.80e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVP 84
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEESFI 233
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFL 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-301 |
1.07e-82 |
|
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: 251.93 E-value: 1.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 12 KTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVPQEFNFGQ 91
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 92 FEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 172 RRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDT--SMKSFLNQLSEESfifdlaEPIAPLQLN-I 247
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGrIIAEGTpeELKRRLGKDTLES------RPRDIQSLKvE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 248 IGVKFNLIDSSTLEVTM-------------DKAHTLNDLFQLLESQGIRVRSMRNKSNRLEELFVKM 301
Cdd:TIGR01188 234 VSMLIAELGETGLGLLAvtvdsdrikilvpDGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-218 |
1.49e-75 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 230.72 E-value: 1.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVP 84
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 165 AGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDT 218
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKeEFGMTILLTTHYMEEAEQLCDRVAIIDHGrIIAEGT 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-214 |
5.91e-74 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 224.97 E-value: 5.91e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVP 84
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILvtqagyygihrkiaekraehyleklglwekrniqarMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-215 |
4.72e-72 |
|
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: 221.61 E-value: 4.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNG-FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVV 83
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQefnfgqfekaFDILVT----------QAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMH 153
Cdd:cd03263 81 PQ----------FDALFDeltvrehlrfYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 154 EPKLLILDEPTAGVDIELRRSMWDFLTEMNENgTSIILTTHYLEEAEMLCRQIAIIDRGVIK 215
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKG-RSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-232 |
1.53e-71 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 221.27 E-value: 1.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVP 84
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEESF 232
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-307 |
3.76e-59 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 191.48 E-value: 3.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPslaKQQLGVV 83
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGL--WEKRNIQArmLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLgdRANKKVEE--LSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 162 EPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEESFIFDLAEPIA 241
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 242 PLQlNIIGVKFNLIDSSTLEVTMDKAHTLNDLFQLLESQGiRVRSMRNKSNRLEELFVKMVEKNLE 307
Cdd:COG4152 235 WLR-ALPGVTVVEEDGDGAELKLEDGADAQELLRALLARG-PVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-217 |
1.68e-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: 186.63 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGfQALKGINLTVPEGeFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVP 84
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENgTSIILTTHYLEEAEMLCRQIAIIDRGVIKED 217
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-277 |
5.57e-57 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 186.45 E-value: 5.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYR-----NGF---------------QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVE 63
Cdd:COG4586 1 IIEVENLSKTYRvyekePGLkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 64 IFGHNldthPS-----LAKqQLGVVpqefnFGQ---------FEKAFDILvtqAGYYGIHRKIAEKRAEHYLEKLGLWEK 129
Cdd:COG4586 81 VLGYV----PFkrrkeFAR-RIGVV-----FGQrsqlwwdlpAIDSFRLL---KAIYRIPDAEYKKRLDELVELLDLGEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 130 RNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAI 208
Cdd:COG4586 148 LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 209 IDRGVIKEDTSMKSFLNQLSEESFI-FDLAEPIAPLQLNiIGVKFNLIDSSTLEVTMDKAHTLNDLFQLL 277
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIvLELAEPVPPLELP-RGGEVIEREGNRVRLEVDPRESLAEVLARL 296
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
7.54e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 181.06 E-value: 7.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNldthPSLAKQQL 80
Cdd:COG1121 3 MMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEFNFgqfEKAFDILV---------TQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAM 151
Cdd:COG1121 78 GYVPQRAEV---DWDFPITVrdvvlmgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDT 218
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-226 |
2.51e-53 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 174.06 E-value: 2.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPSLAKQQLGVV 83
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQE-FNfgQF-------EKAFdilvtqaG--YYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMH 153
Cdd:COG1122 81 FQNpDD--QLfaptveeDVAF-------GpeNLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 154 EPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-214 |
1.64e-52 |
|
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: 171.52 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAK---- 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 --QQLGVVPQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEP 155
Cdd:cd03255 80 rrRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 156 KLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDrGVI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRD-GKI 218
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-217 |
2.06e-52 |
|
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: 172.09 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVV 83
Cdd:TIGR03864 1 ALEVAGLSFRY-GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 pqefnFGQFEKAFDILVTQ-----AGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:TIGR03864 80 -----FQQPTLDLDLSVRQnlryhAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 159 ILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMlCRQIAIIDRGVIKED 217
Cdd:TIGR03864 155 LLDEPTVGLDPASRAAITAHVRALaRDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLAD 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
9.51e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 169.84 E-value: 9.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--L 75
Cdd:COG1136 1 MSPLLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEreL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 AK---QQLGVVPQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:COG1136 81 ARlrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDrGVIKEDTS 219
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRLRD-GRIVSDER 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-214 |
1.20e-50 |
|
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: 166.77 E-value: 1.20e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRN---GFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLG 81
Cdd:cd03266 2 ITADALTKRFRDvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQefNFGQFEK--AFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03266 82 FVSD--STGLYDRltARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
6-212 |
2.65e-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: 2.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 6 VLRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAK-QQLGVV 83
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNfGQF-------EKAFDilvtqAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:cd03225 81 FQNPD-DQFfgptveeEVAFG-----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-214 |
2.94e-50 |
|
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: 165.53 E-value: 2.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDThpsLAKQQLGVVP 84
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
8.24e-49 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 163.34 E-value: 8.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTD---ALVLRDLSKTYR---NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPS 74
Cdd:COG1116 1 MSAaapALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-TGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 75 lakQQLGVVPQEFN------------FGqfekafdiLVTQagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMK 142
Cdd:COG1116 80 ---PDRGVVFQEPAllpwltvldnvaLG--------LELR----GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 143 RRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDR--GVIKED 217
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-214 |
1.14e-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: 161.55 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHnldtHPSLAKQQLGVVPQEFN 88
Cdd:cd03235 4 DLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 89 FgqfEKAFDILV---------TQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03235 79 I---DRDFPISVrdvvlmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-218 |
2.62e-48 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.99 E-value: 2.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAK--QQLGV 82
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreIPYlrRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFNFGQFEKAFD--ILVTQAGyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:COG2884 84 VFQDFRLLPDRTVYEnvALPLRVT--GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 161 DEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDT 218
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-209 |
3.52e-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: 160.72 E-value: 3.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSlakqQLG 81
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP----DRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFN------------FGqfekafdiLVTQagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIAR 149
Cdd:cd03293 77 YVFQQDAllpwltvldnvaLG--------LELQ----GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 150 AMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAII 209
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-212 |
8.97e-48 |
|
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: 157.41 E-value: 8.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS-LAKQQLGVVPQ 85
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 efnfgqfekafdilvtqagyygihrkiaekraehyleklglwekrniqarmLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1595846010 166 GVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-214 |
1.45e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 159.84 E-value: 1.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL--- 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 -GVVPQEFNfgqfekafdiLVTQ-----------AGYYGIHRKI------AEK-RAEHYLEKLGLWEKRNIQARMLSGGM 141
Cdd:COG3638 82 iGMIFQQFN----------LVPRlsvltnvlagrLGRTSTWRSLlglfppEDReRALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
14-198 |
1.93e-47 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 159.48 E-value: 1.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 14 YRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSG-TVEIFGHNLDTHpSLA--KQQLGVVPQEF--N 88
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGE-DVWelRKRIGLVSPALqlR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 89 FGQFEKAFDILVTqaGYY---GIHRKIAE---KRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:COG1119 91 FPRDETVLDVVLS--GFFdsiGLYREPTDeqrERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMNENG-TSIILTTHYLEE 198
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
2.20e-47 |
|
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: 159.82 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL 80
Cdd:COG0411 1 SDPLLEVRGLTKRFG-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVV-----PQEFN------------FGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKR 143
Cdd:COG0411 80 GIArtfqnPRLFPeltvlenvlvaaHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 144 RLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDT 218
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGrVIAEGT 236
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-214 |
4.78e-47 |
|
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: 157.38 E-value: 4.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNlDTHPSLAKQQLGVVP 84
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGIhrkiAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGI----RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
5.03e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 157.66 E-value: 5.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNGFqALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQefnFGQFEKAFDI---LVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK13537 83 GVVPQ---FDNLDPDFTVrenLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 158 LILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-218 |
2.27e-45 |
|
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: 153.75 E-value: 2.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVV- 83
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 ----PQEF-NF---------GQFEKAFDILVTQAGYygiHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIAR 149
Cdd:cd03219 80 tfqiPRLFpELtvlenvmvaAQARTGSGLLLARARR---EEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 150 AMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDT 218
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGrVIAEGT 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-213 |
6.26e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 155.76 E-value: 6.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFqALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVV 83
Cdd:PRK13536 41 AIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQefnFGQFEKAFDI---LVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13536 120 PQ---FDNLDLEFTVrenLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 161 DEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGV 213
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-214 |
7.09e-45 |
|
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: 152.89 E-value: 7.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKqQLG 81
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRreLAR-RIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFNFgqfekAFDILVTQA---------GYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:COG1120 79 YVPQEPPA-----PFGLTVRELvalgryphlGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
4.81e-43 |
|
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: 145.10 E-value: 4.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP-SLAKQQLGVVPQEFNFGQFEKAFDIL 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 100 VTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRN----IQARMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-226 |
6.09e-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: 154.29 E-value: 6.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTY----RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL 80
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 ----GVVPQefN-FGQF---EKAFDILVTQAGYYGIH-RKIAEKRAEHYLEKLGLWEK---RNIqaRMLSGGMKRRLMIA 148
Cdd:COG1123 341 rrrvQMVFQ--DpYSSLnprMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPDladRYP--HELSGGQRQRVAIA 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 149 RAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQrELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-212 |
3.34e-42 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 143.87 E-value: 3.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSL---AKQQLG 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFNfgqfekafdiLVTqagyygiHRKIAEKRAehylekLGLwekrniqarmlSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:cd03229 80 MVFQDFA----------LFP-------HLTVLENIA------LGL-----------SGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 162 EPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-217 |
6.74e-42 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 144.78 E-value: 6.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVpqe 86
Cdd:cd03267 23 LKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 fnFGQFEK-AFDILVTQAGY-----YGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:cd03267 100 --FGQKTQlWWDLPVIDSFYllaaiYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 161 DEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKED 217
Cdd:cd03267 178 DEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-214 |
2.14e-41 |
|
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: 143.48 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL---- 80
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEFNF-GQFEKAFDILVTQAGYYGIHRKI------AEK-RAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:cd03256 81 GMIFQQFNLiERLSVLENVLSGRLGRRSTWRSLfglfpkEEKqRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-217 |
3.88e-41 |
|
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: 142.64 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP----SLAK 77
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlrKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 QQLGVVPQE----FN-----FGQFEKAFDILVTQAGyygihRKIAEKRAEHYLEKLGLWEKR-NIQARMLSGGMKRRLMI 147
Cdd:cd03257 82 KEIQMVFQDpmssLNprmtiGEQIAEPLRIHGKLSK-----KEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKED 217
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-216 |
4.85e-41 |
|
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: 142.33 E-value: 4.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS----LAKQQ 79
Cdd:cd03258 4 LKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINrELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
5.02e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 148.90 E-value: 5.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNG-FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKT---SGTVEIFGHNLDTHP-SL 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSeAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 AKQQLGVVPQEFnFGQF-------EKAFDILVTqagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIA 148
Cdd:COG1123 81 RGRRIGMVFQDP-MTQLnpvtvgdQIAEALENL-----GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 149 RAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-208 |
1.14e-40 |
|
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: 140.69 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTyRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVP 84
Cdd:COG4133 3 LEAENLSCR-RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGihRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEmLCRQIAI 208
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA-AARVLDL 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-214 |
3.39e-40 |
|
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: 139.58 E-value: 3.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAKQQLGVVP 84
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFN------------FGqfekafdiLVTQagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:cd03259 79 QDYAlfphltvaeniaFG--------LKLR----GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-212 |
2.17e-39 |
|
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: 147.47 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYR-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVPQ 85
Cdd:TIGR01257 931 VKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 E-FNFGQFEKAFDILVtQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:TIGR01257 1011 HnILFHHLTVAEHILF-YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1595846010 165 AGVDIELRRSMWDFLTEMnENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-225 |
3.81e-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: 137.18 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGV-- 82
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFN-FGQFEKAFDILVtqAGYYGIHRKIAEKRAEHY--LEKLGlwEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03224 80 VPEGRRiFPELTVEENLLL--GAYARRRAKRKARLERVYelFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLN 225
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-214 |
5.39e-39 |
|
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: 136.51 E-value: 5.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD-THPSLAK--QQLGVV 83
Cdd:cd03262 3 IKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINElrQKVGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFGQFEKAFD-ILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03262 82 FQQFNLFPHLTVLEnITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-214 |
9.55e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 139.85 E-value: 9.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDA-LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSlAKQQ 79
Cdd:COG3842 1 MAMPaLELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEF----------NFGqfekafdilvtqagyYGI-HRKI----AEKRAEHYLEKLGL--WEKRNIqaRMLSGGMK 142
Cdd:COG3842 79 VGMVFQDYalfphltvaeNVA---------------FGLrMRGVpkaeIRARVAELLELVGLegLADRYP--HQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 143 RRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
2.19e-38 |
|
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: 135.88 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALV-LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQ 79
Cdd:COG1127 1 MSEPMIeVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 L----GVVPQE---FN---------FGQFEkafdilvtqagYYGIHRKIAEKRAEHYLEKLGLwekRNIQARM---LSGG 140
Cdd:COG1127 80 LrrriGMLFQGgalFDsltvfenvaFPLRE-----------HTDLSEAEIRELVLEKLELVGL---PGAADKMpseLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 141 MKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTS 219
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*.
gi 1595846010 220 MKSFLN 225
Cdd:COG1127 226 PEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-214 |
3.02e-38 |
|
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: 133.33 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFqALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAK-QQLGVVPQ 85
Cdd:cd03214 2 VENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELaRKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 efnfgqfekafdilvtqagyygihrkiaekraehYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 166 GVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03214 127 HLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-214 |
6.04e-38 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 132.17 E-value: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVp 84
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 qefnfgqfekafdiLVTQagyygihrkiaekraehyleklglwekrniqarmLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03216 79 --------------MVYQ----------------------------------LSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-217 |
9.58e-38 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 133.85 E-value: 9.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKtYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSL-----TKKTSGTVEIFGHN---LDTHPSLAKQ 78
Cdd:cd03260 3 LRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDiydLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 79 QLGVVPQEFNFgqFEK-AFDILVTQAGYYGIH-RKIAEKRAEHYLEKLGLWE--KRNIQARMLSGGMKRRLMIARAMMHE 154
Cdd:cd03260 82 RVGMVFQKPNP--FPGsIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 155 PKLLILDEPTAGVDIELRRSMWDFLTEMNENgTSIILTTHYLEEAEMLCRQIAIIDRGVIKED 217
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-230 |
4.98e-37 |
|
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: 132.62 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA-KQQ 79
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEfnfgqfekafdilvtqagYYG-------IHRKIAE-----------KRAEHYLEKLGLWEK-RNIQARMLSGG 140
Cdd:COG1124 81 VQMVFQD------------------PYAslhprhtVDRILAEplrihglpdreERIAELLEQVGLPPSfLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 141 MKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTS 219
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
250
....*....|.
gi 1595846010 220 MKSFLNQLSEE 230
Cdd:COG1124 223 VADLLAGPKHP 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-226 |
5.64e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.04 E-value: 5.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS-LAK--QQLG 81
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdINKlrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFN-F-----------GQfekafdILVtqagyYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIAR 149
Cdd:COG1126 81 MVFQQFNlFphltvlenvtlAP------IKV-----KKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 150 AMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHyleeaEM-LCRQIA--II--DRGVIKEDTSMKSFL 224
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH-----EMgFAREVAdrVVfmDGGRIVEEGPPEEFF 224
|
..
gi 1595846010 225 NQ 226
Cdd:COG1126 225 EN 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-216 |
8.56e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.05 E-value: 8.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS----LAKQQ 79
Cdd:COG1135 4 LENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelrAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEFN-------FGQFEKAFDILvtqagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:COG1135 84 IGMIFQHFNllssrtvAENVALPLEIA-------GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHyleeaEM-----LCRQIAIIDRGVIKE 216
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH-----EMdvvrrICDRVAVLENGRIVE 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-214 |
9.04e-37 |
|
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: 130.99 E-value: 9.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA----KQQL 80
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEF----NFGQFEK-AFDILVTQAGyygihRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEP 155
Cdd:cd03292 81 GVVFQDFrllpDRNVYENvAFALEVTGVP-----PREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 156 KLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-212 |
1.19e-36 |
|
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: 129.04 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA-KQQLGV 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFNFgqfekaFDilvtqagyygihRKIAEkraehyleklglwekrNIqarmLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03228 81 VPQDPFL------FS------------GTIRE----------------NI----LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEMlCRQIAIIDRG 212
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKT-VIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-214 |
1.32e-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: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSkTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKQQLGV 82
Cdd:COG0410 4 LEVENLH-AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhrIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFN-FGQF---EkafDILVtqAGYYGIHRKIAEKRAEHYLE---KLGlwEKRNIQARMLSGGMKRRLMIARAMMHEP 155
Cdd:COG0410 83 VPEGRRiFPSLtveE---NLLL--GAYARRDRAEVRADLERVYElfpRLK--ERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 156 KLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-218 |
1.21e-35 |
|
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: 128.32 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-----DTHPSL 75
Cdd:COG4181 8 IIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 AKQQLGVVPQEFnfgqfekafdilvtQ-----------------AGyygihRKIAEKRAEHYLEKLGLWEKRNIQARMLS 138
Cdd:COG4181 88 RARHVGFVFQSF--------------QllptltalenvmlplelAG-----RRDARARARALLERVGLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 139 GGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMlCRQIAIIDRGVIKED 217
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
.
gi 1595846010 218 T 218
Cdd:COG4181 228 T 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-214 |
5.08e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 126.58 E-value: 5.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFG---HNLDTHpslaKQQLG 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdiTNLPPH----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEF----NFGQFEK-AFDILVTqagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:cd03300 76 TVFQNYalfpHLTVFENiAFGLRLK-----KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-215 |
1.02e-34 |
|
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: 125.59 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAKqqLGVVP 84
Cdd:TIGR03740 1 LETKNLSKRFGKQ-TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW-TRKDLHK--IGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILVTQAGYYGIhrkiAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGL----PDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 165 AGVDI----ELRrsmwDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIK 215
Cdd:TIGR03740 153 NGLDPigiqELR----ELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-209 |
3.58e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.14 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL 80
Cdd:COG1129 1 AEPLLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GV--VPQEFN------------FGQfekafdiLVTQAGYygIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLM 146
Cdd:COG1129 80 GIaiIHQELNlvpnlsvaenifLGR-------EPRRGGL--IDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 147 IARAMMHEPKLLILDEPTA---GVDIElrrSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAII 209
Cdd:COG1129 151 IARALSRDARVLILDEPTAsltEREVE---RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
9-215 |
3.59e-34 |
|
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: 123.91 E-value: 3.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfgHNLDTHPSLAKQQLGVVPQEFN 88
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL--NGKPIKAKERRKSIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 89 FGQFEK-AFDILvtqagYYGIHRKIAEK-RAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:cd03226 82 YQLFTDsVREEL-----LLGLKELDAGNeQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 167 VDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIK 215
Cdd:cd03226 157 LDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-218 |
3.91e-34 |
|
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: 124.54 E-value: 3.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDthpSLAKQQLGVVPQE 86
Cdd:cd03261 3 LRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS---GLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 FNFgQFEKA--FDIL-VTQAGYYGI--HRKIAE----KRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKL 157
Cdd:cd03261 79 MGM-LFQSGalFDSLtVFENVAFPLreHTRLSEeeirEIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 158 LILDEPTAGVD-------IELRRSMWDfltemnENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDT 218
Cdd:cd03261 158 LLYDEPTAGLDpiasgviDDLIRSLKK------ELGLTSIMVTHDLDTAFAIADRIAVLYDGkIVAEGT 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-214 |
4.13e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 124.19 E-value: 4.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGV-- 82
Cdd:cd03218 1 LRAENLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFN-FGQFEKAFDILVTqAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:cd03218 80 LPQEASiFRKLTVEENILAV-LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 162 EPTAGVD----IELRRsmwdFLTEMNENGTSIILTTHYLEEAemlcrqIAIIDRGVI 214
Cdd:cd03218 159 EPFAGVDpiavQDIQK----IIKILKDRGIGVLITDHNVRET------LSITDRAYI 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-214 |
8.60e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.41 E-value: 8.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVP 84
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEF----------NFgqfekAFDILVTQAGyygihRKIAEKRAEHYLEKLGLwekRNIQARM---LSGGMKRRLMIARAM 151
Cdd:COG1118 82 QHYalfphmtvaeNI-----AFGLRVRPPS-----KAEIRARVEELLELVQL---EGLADRYpsqLSGGQRQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-214 |
9.58e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 122.62 E-value: 9.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSktYRNGFQA-LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA-KQQLGV 82
Cdd:COG4619 1 LELEGLS--FRVGGKPiLSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFNFG------QFEKAFDILvtqagyygiHRKIAEKRAEHYLEKLGL----WEKrniQARMLSGGMKRRLMIARAMM 152
Cdd:COG4619 79 VPQEPALWggtvrdNLPFPFQLR---------ERKFDRERALELLERLGLppdiLDK---PVERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTE-MNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-212 |
1.88e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.52 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD-THPSLA-KQ 78
Cdd:COG3845 2 MPPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAiAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 79 QLGVVPQEFnfgqfeKAFDIL-VTQ--------AGYYGIHRKIAEKRAEHYLEKLGLweKRNIQARM--LSGGMKRRLMI 147
Cdd:COG3845 81 GIGMVHQHF------MLVPNLtVAEnivlglepTKGGRLDRKAARARIRELSERYGL--DVDPDAKVedLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 148 ARAMMHEPKLLILDEPTAG-----VDiELrrsmWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:COG3845 153 LKALYRGARILILDEPTAVltpqeAD-EL----FEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-219 |
3.86e-32 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.83 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS----LAKQQ 79
Cdd:PRK11153 4 LKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTS 219
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINrELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-214 |
4.53e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.10 E-value: 4.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPslAKQQLGV 82
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPP--KDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEF----------N--FGqfekafdiLVTQagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARA 150
Cdd:COG3839 80 VFQSYalyphmtvyeNiaFP--------LKLR----KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-194 |
5.02e-32 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 117.52 E-value: 5.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 14 YRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD-THPSL--AKQQLGVVPQEFNfg 90
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDySRKGLleRRQRVGLVFQDPD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 91 qfEKAFDILVTQAGYY-----GIHRKIAEKRAEHYLEKLGL--WEKRNIQarMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:TIGR01166 79 --DQLFAADVDQDVAFgplnlGLSEAEVERRVREALTAVGAsgLRERPTH--CLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 1595846010 164 TAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-214 |
8.13e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 118.59 E-value: 8.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSL---AKQQLG 81
Cdd:COG1137 4 LEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THLPMhkrARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQE---F-------NFgqfeKAfdILVTQagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAM 151
Cdd:COG1137 82 YLPQEasiFrkltvedNI----LA--VLELR----KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 152 MHEPKLLILDEPTAGVD----IELRRsMWDFLTEMnenGTSIILTTHYLEEAemlcrqIAIIDRGVI 214
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiavADIQK-IIRHLKER---GIGVLITDHNVRET------LGICDRAYI 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-216 |
3.29e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.04 E-value: 3.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPS-----LAKQQ 79
Cdd:COG4161 5 LKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsQKPSekairLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEFNFGQFEKAFDILvTQA--GYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKL 157
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENL-IEApcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 158 LILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-233 |
3.37e-31 |
|
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: 117.02 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHN-LDTHPSLAKQQLGVV 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFN-FGQFEKAFDI-LVTQAGYYGIHRKiaEKRAEHYLEKLGLwEKRNIQARM---LSGGMKRRLMIARAMMHEPKLL 158
Cdd:cd03295 81 IQQIGlFPHMTVEENIaLVPKLLKWPKEKI--RERADELLALVGL-DPAEFADRYpheLSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 159 ILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDTSMKSFLNQLSE--ESFI 233
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGeIVQVGTPDEILRSPANDfvAEFV 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-215 |
3.76e-31 |
|
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: 123.59 E-value: 3.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 2 TDALVLRDLSKTYR-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL 80
Cdd:TIGR01257 1935 TDILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQefnfgqFEKAFDILVTQAGYY------GIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHE 154
Cdd:TIGR01257 2015 GYCPQ------FDAIDDLLTGREHLYlyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 155 PKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIK 215
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-217 |
4.43e-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: 122.64 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYR-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLG 81
Cdd:COG2274 473 DIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQE---FN--------FGQFEKAFDILVTQAGYYGIHRKIaEKRAEHYLEKLGlwEkrniQARMLSGGMKRRLMIARA 150
Cdd:COG2274 553 VVLQDvflFSgtirenitLGDPDATDEEIIEAARLAGLHDFI-EALPMGYDTVVG--E----GGSNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEmLCRQIAIIDRGVIKED 217
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLKGRT-VIIIAHRLSTIR-LADRIIVLDKGRIVED 690
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-216 |
5.30e-31 |
|
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: 121.79 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLGV 82
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE---FN--------FGQfEKAFDILVTQAgyygihrkIAEKRAEHYLEKL--GLWEKRNIQARMLSGGMKRRLMIAR 149
Cdd:COG4988 416 VPQNpylFAgtirenlrLGR-PDASDEELEAA--------LEAAGLDEFVAALpdGLDTPLGEGGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 150 AMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEmLCRQIAIIDRGVIKE 216
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT-VILITHRLALLA-QADRILVLDDGRIVE 551
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-225 |
5.45e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 5.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFG-HNLDTHPS--LAKQQLGVVPQEFN-FGQFEK 94
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDerLIRQEAGMVFQQFYlFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 95 AFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PRK09493 95 LENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 175 MWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLN 225
Cdd:PRK09493 175 VLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-230 |
8.63e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.19 E-value: 8.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPS-----LAKQQLGVVPQEFNF-- 89
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsKTPSdkairELRRNVGMVFQQYNLwp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 90 ------GQFEKAFDILvtqagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:PRK11124 96 hltvqqNLIEAPCRVL-------GLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 164 TAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEE 230
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQPQTEA 235
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-219 |
1.07e-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: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVV- 83
Cdd:TIGR04406 2 LVAENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 -PQEFN-FGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:TIGR04406 81 lPQEASiFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 162 EPTAGVD----IELRRsmwdFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDTS 219
Cdd:TIGR04406 161 EPFAGVDpiavGDIKK----IIKHLKERGIGVLITDHNVRETLDICDRAYIISDGkVLAEGTP 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-214 |
1.33e-29 |
|
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: 111.96 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPslAKQQLGVV 83
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPP--KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 164 TAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-230 |
1.66e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.92 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQ---- 79
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 -----LGVVPQEFNFGQFEKAFD-ILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMH 153
Cdd:PRK11264 82 qlrqhVGFVFQNFNLFPHRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 154 EPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEE 230
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQP 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-199 |
1.81e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.79 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 16 NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHnldTHPSLAKQQLGVVPqefnfgqfekA 95
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---ARVAYVPQRSEVPD----------S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 96 FDILVTQA---------GYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:NF040873 70 LPLTVRDLvamgrwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 1595846010 167 VDIELRRSMWDFLTEMNENGTSIILTTHYLEEA 199
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
8-223 |
2.64e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD-THPSL--AKQQLGVVP 84
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLleVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNfgqfEKAFDILVTQAGYYG-----IHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:PRK13639 85 QNPD----DQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDTSMKSF 223
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGkIIKEGTPKEVF 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-208 |
3.69e-29 |
|
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: 113.22 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTY--RNG-FQALKGINLTVPEGEFYALLGPNGAGKSTT----IGIISSlTKKTSGTVEIFGHNLDTHP---- 73
Cdd:COG0444 2 LEVRNLKVYFptRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPP-PGITSGEILFDGEDLLKLSekel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 74 -SLAKQQLGVVPQE----FN-----FGQFEKAFDIlvtqagYYGIHRKIAEKRAEHYLEKLGLWEKRNIQAR---MLSGG 140
Cdd:COG0444 81 rKIRGREIQMIFQDpmtsLNpvmtvGDQIAEPLRI------HGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 141 MKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAI 208
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQrELGLAILFITHDLGVVAEIADRVAV 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
1.07e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.37 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHnlDTHPSLAKQ-- 78
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR--EVNAENEKWvr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 79 -QLGVVPQEFNFGQFE-KAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13647 79 sKVGLVFQDPDDQVFSsTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-217 |
1.09e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNG---------------------FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTS 59
Cdd:COG1134 1 MSSMIEVENVSKSYRLYhepsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 60 GTVEIFGhnldTHPSLAKQQLGVVPQ-------EFNfgqfekafdilvtqAGYYGIHRKIAEKRAEHYLEKLGLWEKRNI 132
Cdd:COG1134 81 GRVEVNG----RVSALLELGAGFHPEltgreniYLN--------------GRLLGLSRKEIDEKFDEIVEFAELGDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 133 QARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELR-RSMwDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDR 211
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQkKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*.
gi 1595846010 212 GVIKED 217
Cdd:COG1134 222 GRLVMD 227
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-226 |
1.73e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 114.86 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRN-GFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP--SLAkQQL 80
Cdd:COG4987 333 SLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDedDLR-RRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEFNFgqfekaFD------ILVT--QAGyygihrkiaEKRAEHYLEKLGL--WEKRNIQ---------ARMLSGGM 141
Cdd:COG4987 412 AVVPQRPHL------FDttlrenLRLArpDAT---------DEELWAALERVGLgdWLAALPDgldtwlgegGRRLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEmLCRQIAIIDRGVIKEDTSMK 221
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT-VLLITHRLAGLE-RMDRILVLEDGRIVEQGTHE 554
|
....*
gi 1595846010 222 SFLNQ 226
Cdd:COG4987 555 ELLAQ 559
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-226 |
1.73e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.49 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTK--KTSGT-VEIFGHNLDTHPSLAK 77
Cdd:PRK09984 1 MQTIIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQREGRLAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 Q------QLGVVPQEFNF-GQFEKAFDILVTQAGYYGIHR-------KIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKR 143
Cdd:PRK09984 80 DirksraNTGYIFQQFNLvNRLSVLENVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 144 RLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKS 222
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
....
gi 1595846010 223 FLNQ 226
Cdd:PRK09984 240 FDNE 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-216 |
2.23e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 110.95 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNG----FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVE-IFGHNLDTHPSLAKQ--- 78
Cdd:PRK13651 5 VKNIVKIFNKKlpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwIFKDEKNKKKTKEKEkvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 79 ---------------------QLGVVPQEFNFGQFEKAF--DILVTqAGYYGIHRKIAEKRAEHYLEKLGLWE---KRNI 132
Cdd:PRK13651 85 eklviqktrfkkikkikeirrRVGVVFQFAEYQLFEQTIekDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDEsylQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 133 QArmLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEA-EMLCRQIAIIDR 211
Cdd:PRK13651 164 FE--LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKDG 241
|
....*
gi 1595846010 212 GVIKE 216
Cdd:PRK13651 242 KIIKD 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-217 |
4.57e-28 |
|
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: 108.00 E-value: 4.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 18 FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGhnldthpslakqqlGVVPQ-EFNFGqFEKAF 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------RVSSLlGLGGG-FNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 97 ---DILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRR 173
Cdd:cd03220 100 tgrENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1595846010 174 SMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKED 217
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-232 |
5.08e-28 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 109.20 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGhnLDTHPSLAKQQL 80
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG--QPTRQALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEfnfGQFEKAFDILVTQA---GYYG----IHRKIAEKRA--EHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAM 151
Cdd:PRK15056 81 AYVPQS---EEVDWSFPVLVEDVvmmGRYGhmgwLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEES 231
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELA 237
|
.
gi 1595846010 232 F 232
Cdd:PRK15056 238 F 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-214 |
5.09e-28 |
|
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: 108.58 E-value: 5.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNgFQaLKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSlAKQQLGVVP 84
Cdd:cd03299 1 LKVENLSKDWKE-FK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP-EKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEF----NFGQFEK-AFDILVTQAGYYGIHRKIAEkraehYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03299 78 QNYalfpHMTVYKNiAYGLKKRKVDKKEIERKVLE-----IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-216 |
7.52e-28 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 108.20 E-value: 7.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVeIFGHNLDTHPSLAKQQLGVV 83
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFGQ----FEK-AFDILVTQAGYYGIHRKIAEkRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:cd03296 80 FQHYALFRhmtvFDNvAFGLRVKPRSERPPEAEIRA-KVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 159 ILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-232 |
1.43e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.15 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLskTYRNGFQALKgINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPslAKQQLGVV 83
Cdd:COG3840 2 LRLDDL--TYRYGDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtALPP--AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFgqfekaFDIL-VTQAGYYGIH---RKIAEKRA--EHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKL 157
Cdd:COG3840 77 FQENNL------FPHLtVAQNIGLGLRpglKLTAEQRAqvEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 158 LILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEESF 232
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-214 |
2.98e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 104.61 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQA-LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLGV 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEfnfgqfekafDILVtqAGyygihrKIAEkraehyleklglwekrNIqarmLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03246 81 LPQD----------DELF--SG------SIAE----------------NI----LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMlCRQIAIIDRGVI 214
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
3.36e-27 |
|
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: 106.01 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAKQqlgVVPQEFNFGQFEKAFDILV 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 101 TQAGYYGIHRKIAEKRA--EHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDF 178
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1595846010 179 LTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:TIGR01184 157 LMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-194 |
3.53e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 106.61 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVp 84
Cdd:PRK11300 6 LSVSGLMMRF-GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFN----FGQFEKAFDILVTQ---------AGYY---GIHRKIAEK--RAEHYLEKLGLWEKRNIQARMLSGGMKRRLM 146
Cdd:PRK11300 84 RTFQhvrlFREMTVIENLLVAQhqqlktglfSGLLktpAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTH 194
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEH 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-199 |
3.67e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 106.87 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQ---ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSlAKQql 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPG-ADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEF----------N--FG-QFEkafdilvtqagyyGIHRKIAEKRAEHYLEKLGL--WEKRNIQArmLSGGMKRRL 145
Cdd:COG4525 79 GVVFQKDallpwlnvldNvaFGlRLR-------------GVPKAERRARAEELLALVGLadFARRRIWQ--LSGGMRQRV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEA 199
Cdd:COG4525 144 GIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEA 198
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-169 |
4.20e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.39 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTyRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKqQLG 81
Cdd:PRK13548 2 MLEARNLSVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPaeLAR-RRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFNFgqfekAFDILVTQ-----AGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM---- 152
Cdd:PRK13548 80 VLPQHSSL-----SFPFTVEEvvamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170
....*....|....*....
gi 1595846010 153 --HEPKLLILDEPTAGVDI 169
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDL 173
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-169 |
4.55e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 106.35 E-value: 4.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTyRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKqQLGV 82
Cdd:COG4559 2 LEAENLSVR-LGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPweLAR-RRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE----FNFGQFEkafdilVTQAGYY--GIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAM----- 151
Cdd:COG4559 80 LPQHsslaFPFTVEE------VVALGRAphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwe 153
|
170 180
....*....|....*....|
gi 1595846010 152 --MHEPKLLILDEPTAGVDI 169
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDL 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
6.01e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 110.58 E-value: 6.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNGFQA---LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--- 74
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 75 --LAKQQLGVVPQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:PRK10535 81 aqLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKS 222
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEK 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-216 |
6.32e-27 |
|
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: 105.30 E-value: 6.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKQQLGV 82
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPheRARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQ--EFnFGQFEKAFDILVTQAGYYGIHRKIAEkraehylEKLGLW----EKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:TIGR03410 80 VPQgrEI-FPRLTVEENLLTGLAALPRRSRKIPD-------EIYELFpvlkEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 157 LLILDEPTAGV------DIE--LRRsmwdfLTEmnENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:TIGR03410 152 LLLLDEPTEGIqpsiikDIGrvIRR-----LRA--EGGMAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-212 |
6.63e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD-THPSLAK--QQLG 81
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKlrESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFNfgqfEKAFDILVTQAGYYG-----IHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13636 86 MVFQDPD----NQLFSASVYQDVSFGavnlkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-215 |
7.61e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.64 E-value: 7.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNG--FQ--ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAK--- 77
Cdd:PRK13634 3 ITFQKVEHRYQYKtpFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 --QQLGVVpqeFNFGQ---FEKAF--DILVTQAGYyGIHRKIAEKRAEHYLEKLGLWEKrnIQARM---LSGGMKRRLMI 147
Cdd:PRK13634 83 lrKKVGIV---FQFPEhqlFEETVekDICFGPMNF-GVSEEDAKQKAREMIELVGLPEE--LLARSpfeLSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIK 215
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-216 |
2.69e-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: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP--SLaKQQLG 81
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTleSL-RRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQE---FN--------FGQfEKAFDILVTQAgyygihrkiAEK-RAEHYLEKL--GLwekrniQAR------MLSGGM 141
Cdd:COG1132 418 VVPQDtflFSgtirenirYGR-PDATDEEVEEA---------AKAaQAHEFIEALpdGY------DTVvgergvNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSII----LTThyLEEAEmlcrQIAIIDRGVIKE 216
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIViahrLST--IRNAD----RILVLDDGRIVE 554
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-214 |
2.71e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 2.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSL--AKQQLGVVPQ 85
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI-TKENIreVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 EFNfgqfEKAFDILVTQAGYYG-----IHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13652 86 NPD----DQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 161 DEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-216 |
1.20e-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: 101.92 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLaKQQLGV 82
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIRevTLDSL-RRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE---FN--------FGQfEKAFDILVTQAGYYG-IHRKIaEKRAEHYLEKLGlweKRNIqarMLSGGMKRRLMIARA 150
Cdd:cd03253 80 VPQDtvlFNdtigynirYGR-PDATDEEVIEAAKAAqIHDKI-MRFPDGYDTIVG---ERGL---KLSGGEKQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILtTHYLEEAeMLCRQIAIIDRGVIKE 216
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTI-VNADKIIVLKDGRIVE 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-212 |
1.32e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 102.28 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP--SLAKQQLGV 82
Cdd:PRK10895 4 LTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFNFGQFEKAFD-ILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK10895 83 LPQEASIFRRLSVYDnLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 162 EPTAGVD----IELRRsmwdFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK10895 163 EPFAGVDpisvIDIKR----IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-214 |
1.39e-25 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 102.72 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP-----SLAKQQLGVVPQefNFGQFEK 94
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkelrELRRKKISMVFQ--SFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 95 -------AFDILVTqagyyGIHRKIAEKRAEHYLEKLGL--WEKRNIQArmLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:cd03294 117 rtvlenvAFGLEVQ-----GVPRAEREERAAEALELVGLegWEHKYPDE--LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 166 GVDIELRRSMWD-FLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03294 190 ALDPLIRREMQDeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
2.05e-25 |
|
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: 99.81 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSktyrnGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVv 83
Cdd:cd03215 4 VLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 pqefnfgqfekafdilvtqaGYygihrkIAEKRAEHYLeKLGLWEKRNIQ-ARMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03215 78 --------------------AY------VPEDRKREGL-VLDLSVAENIAlSSLLSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-223 |
2.80e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.09 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfgHNLDT----HPSLAKQQLGVVPQEFNfGQFEKA 95
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTsdeeNLWDIRNKAGMVFQNPD-NQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 96 fdILVTQAGY----YGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:PRK13633 102 --IVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 172 RRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRqIAIIDRG-VIKEDTSMKSF 223
Cdd:PRK13633 180 RREVVNTIKELNKKyGITIILITHYMEEAVEADR-IIVMDSGkVVMEGTPKEIF 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-217 |
4.79e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-------------DT 71
Cdd:PRK10619 6 LNVIDLHKRY-GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 72 HP-SLAKQQLGVVPQEFNFGQFEKAFD-ILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARM-LSGGMKRRLMIA 148
Cdd:PRK10619 85 NQlRLLRTRLTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 149 RAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKED 217
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-220 |
5.97e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 100.28 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAK---- 77
Cdd:PRK11629 6 LQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 -QQLGVVPQeF-----NFGQFEK-AFDILVTqagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARA 150
Cdd:PRK11629 86 nQKLGFIYQ-FhhllpDFTALENvAMPLLIG-----KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSM 220
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-199 |
7.63e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.50 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKST---TIGIISSLTK--KTSGTVEIFGHNL---DTH 72
Cdd:COG1117 8 LEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgaRVEGEILLDGEDIydpDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 73 PSLAKQQLGVVPQEFN-----------FGqfekafdilvtqAGYYGIH-RKIAEKRAEHYLEKLGLWE----KRNIQARM 136
Cdd:COG1117 87 VVELRRRVGMVFQKPNpfpksiydnvaYG------------LRLHGIKsKSELDEIVEESLRKAALWDevkdRLKKSALG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVD------IElrrsmwDFLTEMNENGTsIILTTHYLEEA 199
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistakIE------ELILELKKDYT-IVIVTHNMQQA 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-215 |
8.61e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.99 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfghnldtHPSLakqQLGVVPQE 86
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-------PKGL---RIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 FNFGQFEKAFDILVtqAGYYGIHRKIAEKRA------------------EHYLEKLGLWEkrnIQARM------------ 136
Cdd:COG0488 70 PPLDDDLTVLDTVL--DGDAELRALEAELEEleaklaepdedlerlaelQEEFEALGGWE---AEARAeeilsglgfpee 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 137 --------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRsmW--DFLteMNENGTsIILTTH---YLEEaemLC 203
Cdd:COG0488 145 dldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFL--KNYPGT-VLVVSHdryFLDR---VA 216
|
250
....*....|..
gi 1595846010 204 RQIAIIDRGVIK 215
Cdd:COG0488 217 TRILELDRGKLT 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-214 |
1.39e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 103.21 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAK-QQ 79
Cdd:PRK15439 8 APPLLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARLTPAKaHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGV--VPQE-FNFGQFEKAFDILVTQAGyygihRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK15439 86 LGIylVPQEpLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 157 LLILDEPTAGVD-IELRRsMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK15439 161 ILILDEPTASLTpAETER-LFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-170 |
2.22e-24 |
|
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: 98.77 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 6 VLRDLSKTY--RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPSLAKQQLGV 82
Cdd:cd03249 2 EFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE---FN--------FGQFEKAFDILVTQAGYYGIHRKIaEKRAEHYLEKLGlweKRNIQarmLSGGMKRRLMIARAM 151
Cdd:cd03249 82 VSQEpvlFDgtiaenirYGKPDATDEEVEEAAKKANIHDFI-MSLPDGYDTLVG---ERGSQ---LSGGQKQRIAIARAL 154
|
170
....*....|....*....
gi 1595846010 152 MHEPKLLILDEPTAGVDIE 170
Cdd:cd03249 155 LRNPKILLLDEATSALDAE 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-214 |
3.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfGHNLDTHPSLAKQ------QLGVVpqeFNFGQF 92
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEikpvrkKVGVV---FQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 93 EKAFDILVTQAGY----YGIHRKIAEKRAEHYLEKLGL----WEKRNIQarmLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:PRK13643 96 QLFEETVLKDVAFgpqnFGIPKEKAEKIAAEKLEMVGLadefWEKSPFE---LSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-216 |
3.20e-24 |
|
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: 98.07 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP-SLAKQQLGVVPQE 86
Cdd:cd03254 6 ENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 ---FNFGQFE--KAFDILVTQAgyyGIHRKIAEKRAEHYLEKL--GLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03254 86 tflFSGTIMEniRLGRPNATDE---EVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMNENGTSII----LTThyLEEAEmlcrQIAIIDRGVIKE 216
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIiahrLST--IKNAD----KILVLDDGKIIE 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-212 |
3.30e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.07 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKqql 80
Cdd:PRK11607 16 LTPLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 gvvPQEFNFGQFEKAFDILVTQAGYYGIHRKIAEK-----RAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEP 155
Cdd:PRK11607 92 ---PINMMFQSYALFPHMTVEQNIAFGLKQDKLPKaeiasRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 156 KLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-212 |
3.74e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 97.37 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 14 YRNGFQALKgINLTVPEgEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFG-------HNLDTHPSlaKQQLGVVPQE 86
Cdd:cd03297 8 KRLPDFTLK-IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQ--QRKIGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 FN-FGQFEKAFDILVtqaGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:cd03297 84 YAlFPHLNVRENLAF---GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1595846010 166 GVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-218 |
5.44e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.12 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKtyRNG-FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGV 82
Cdd:NF033858 266 AIEARGLTM--RFGdFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEF----------NfgqfekafdiLVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:NF033858 344 MSQAFslygeltvrqN----------LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEmLCRQIAIIDRG-VIKEDT 218
Cdd:NF033858 414 HKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAE-RCDRISLMHAGrVLASDT 480
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-217 |
5.90e-24 |
|
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: 95.84 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTY-RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVV 83
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFgqfekaFDILVtqagyygihrkiaekraehyLEKLGlwekrniqaRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:cd03247 81 NQRPYL------FDTTL--------------------RNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 164 TAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEMLcRQIAIIDRGVIKED 217
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKT-LIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-208 |
7.34e-24 |
|
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: 101.21 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPSLAKQQLGV 82
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE---------FN--FGQFEKAFDILVTQAGYYGIHRKIAEKRAehyleklGLWEKRNIQARMLSGGMKRRLMIARAM 151
Cdd:TIGR02857 401 VPQHpflfagtiaENirLARPDASDAEIREALERAGLDEFVAALPQ-------GLDTPIGEGGAGLSGGQAQRLALARAF 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEMLCRQIAI 208
Cdd:TIGR02857 474 LRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRT-VLLVTHRLALAALADRIVVL 529
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
108-310 |
9.64e-24 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 99.42 E-value: 9.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 108 IHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGT 187
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 188 SIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEESFIFDLAE---------PIAPLQLNIIGVKFNLIDSS 258
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAHaaeldrmvgAIAQAGLDGIAGATADHEDG 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 259 TLEVTMDKAHTLNDLFQLLESQGIRVRSMRNKSNRLEELFVKMVEKNLEGAA 310
Cdd:NF000106 276 VVNVPIVSDEQLSAVVGMLGERGFTISGHQHPSAQL*EVFLAITGQKTSEAA 327
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-226 |
1.37e-23 |
|
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: 96.53 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRN-GFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLaKQQLG 81
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRdyTLASL-RRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQE---FN--------FGQFEKAFDILVTQAGYYGIHRKIaEKRAEHYLEKLGlweKRNIQarmLSGGMKRRLMIARA 150
Cdd:cd03251 80 LVSQDvflFNdtvaeniaYGRPGATREEVEEAARAANAHEFI-MELPEGYDTVIG---ERGVK---LSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSII----LTThyLEEAEmlcrQIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFViahrLST--IENAD----RIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
1.72e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.83 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTK-----KTSGTVEIFGHNL---DTH 72
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIyspDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 73 PSLAKQQLGVVPQEFNFGQFEKAFDILVTQAGYYGIHRKIAE--KRAEHYLEKLGLWE----KRNIQARMLSGGMKRRLM 146
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT-IVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
9-255 |
2.21e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYRNG----FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-----DTHPSLAKQQ 79
Cdd:PRK13646 7 NVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRPVRKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEFNFGQFEKAF--DILVTQAGyYGIHRKIAEKRAEHYLEKLGLweKRNIQAR---MLSGGMKRRLMIARAMMHE 154
Cdd:PRK13646 87 IGMVFQFPESQLFEDTVerEIIFGPKN-FKMNLDEVKNYAHRLLMDLGF--SRDVMSQspfQMSGGQMRKIAIVSILAMN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 155 PKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSE-ESF 232
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKKKlADW 243
|
250 260
....*....|....*....|....*.
gi 1595846010 233 IFDLAEpIAPLQLNI---IGVKFNLI 255
Cdd:PRK13646 244 HIGLPE-IVQLQYDFeqkYQTKLKDI 268
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-219 |
2.34e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.48 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAKQQLGVVPQE 86
Cdd:PRK09452 17 LRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 F----NFGQFEK-AFDILVTQAGYYGIHRKIAEKRAEHYLEKLGlweKRNIQarMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK09452 95 YalfpHMTVFENvAFGLRMQKTPAAEITPRVMEALRMVQLEEFA---QRKPH--QLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 162 EPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTS 219
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
3.06e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 3 DALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfGHNLdthpslakqQLGV 82
Cdd:COG0488 314 KVLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE---FNFGQfeKAFDILVtqagyyGIHRKIAEKRAEHYLEKLGL----WEKRniqARMLSGGMKRRLMIARAMMHEP 155
Cdd:COG0488 383 FDQHqeeLDPDK--TVLDELR------DGAPGGTEQEVRGYLGRFLFsgddAFKP---VGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 156 KLLILDEPTAGVDIELRRSMWDFLTEMneNGTsIILTTH--YLeeAEMLCRQIAIIDRGVIKE 216
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDF--PGT-VLLVSHdrYF--LDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
7-214 |
4.46e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.35 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNG--FQ--ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFG-------HNLDTHPsl 75
Cdd:PRK13649 5 LQNVSYTYQAGtpFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstsKNKDIKQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 AKQQLGVVpqeFNFGQfEKAFDILVTQ-----AGYYGIHRKIAEKRAEHYLEKLGLWEK-RNIQARMLSGGMKRRLMIAR 149
Cdd:PRK13649 83 IRKKVGLV---FQFPE-SQLFEETVLKdvafgPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 150 AMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-214 |
4.86e-23 |
|
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: 94.85 E-value: 4.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTYRN--GFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGH--NLDTHPSLaKQQLGVV 83
Cdd:cd03248 15 QNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpiSQYEHKYL-HSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQE-----------FNFGQFEKAFDILVTQAGYYGIHRKIAEkraehyLEKlGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:cd03248 94 GQEpvlfarslqdnIAYGLQSCSFECVKEAAQKAHAHSFISE------LAS-GYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMNENgTSIILTTHYLEEAEMlCRQIAIIDRGVI 214
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-214 |
6.94e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 94.10 E-value: 6.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 26 LTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAKQQLGVVPQEFN-FGQFEKAFDILVTQAG 104
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNlFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 105 yyGIH-RKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN 183
Cdd:cd03298 98 --GLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|..
gi 1595846010 184 -ENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:cd03298 176 aETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-252 |
9.36e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.28 E-value: 9.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA-----KQQLGVVPQeFNFGQ-F 92
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklRKKVSLVFQ-FPEAQlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 93 EKAF--DILVTQAGYyGIHRKIAEKRAEHYLEKLGLWEK-RNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK13641 100 ENTVlkDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 170 ELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDTSMKSFLNQLSEESfiFDLAEPIAPL---QL 245
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGkLIKHASPKEIFSDKEWLKK--HYLDEPATSRfasKL 256
|
....*..
gi 1595846010 246 NIIGVKF 252
Cdd:PRK13641 257 EKGGFKF 263
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
1.30e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.69 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 16 NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVPQEF-NFGQFEK 94
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIkNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 95 AFDIlVTQAGYY------------------GIHRKIAEKRAEHYLEKLGLWE---KRNiqARMLSGGMKRRLMIARAMMH 153
Cdd:PRK13631 117 RVSM-VFQFPEYqlfkdtiekdimfgpvalGVKKSEAKKLAKFYLNKMGLDDsylERS--PFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 154 EPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDTSMKSFLNQ 226
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGkILKTGTPYEIFTDQ 267
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-214 |
1.35e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTyRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFG---HNLDThpSLAKQQLG 81
Cdd:PRK09536 4 IDVSDLSVE-FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvEALSA--RAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFNFgqfekAFDILVTQA---------GYYGIHRKIAEKRAEHYLEKLGL--WEKRNIQArmLSGGMKRRLMIARA 150
Cdd:PRK09536 81 SVPQDTSL-----SFEFDVRQVvemgrtphrSRFDTWTETDRAAVERAMERTGVaqFADRPVTS--LSGGERQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-218 |
1.61e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.30 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-----DTHPSLAKQQLGVVPQEFNFGQFEKA 95
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeEARAKLRAKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 96 FDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1595846010 176 WDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDrGVIKEDT 218
Cdd:PRK10584 186 ADLLFSLNrEHGTTLILVTHDLQLAARCDRRLRLVN-GQLQEEA 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-194 |
2.08e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 92.23 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDL-----SKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTK--KTSGTVEIFGHNLdtHPSLAK 77
Cdd:cd03213 4 LSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPL--DKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 QQLGVVPQEfnfgqfekafDILvtqagyygihrkiaekraehyLEKLGLWEKRNIQARM--LSGGMKRRLMIARAMMHEP 155
Cdd:cd03213 82 KIIGYVPQD----------DIL---------------------HPTLTVRETLMFAAKLrgLSGGERKRVSIALELVSNP 130
|
170 180 190
....*....|....*....|....*....|....*....
gi 1595846010 156 KLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-190 |
2.60e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 92.88 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTY----RNG--FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIF--GHNLDth 72
Cdd:COG4778 1 MTTLLEVENLSKTFtlhlQGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 73 psLA-----------KQQLGVVpqefnfGQFEK------AFDIlVTQAGY-YGIHRKIAEKRAEHYLEKLG----LWEkr 130
Cdd:COG4778 79 --LAqaspreilalrRRTIGYV------SQFLRviprvsALDV-VAEPLLeRGVDREEARARARELLARLNlperLWD-- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 131 nIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSII 190
Cdd:COG4778 148 -LPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-200 |
3.63e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 96.73 E-value: 3.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLAKQQLG 81
Cdd:NF033858 1 VARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdaRHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQ----------------EFnFGQFekafdilvtqagyYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRL 145
Cdd:NF033858 80 YMPQglgknlyptlsvfenlDF-FGRL-------------FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN--GTSIILTTHYLEEAE 200
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAE 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-216 |
4.35e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.05 E-value: 4.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTK-----KTSGTVEIFGHNLDTHP--SLAK 77
Cdd:PRK14247 4 IEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDviELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 --QQLGVVPQEF-NFGQFEKAfdILVTQAGYYGIHRKIAEKRAEHYLEKLGLWE----KRNIQARMLSGGMKRRLMIARA 150
Cdd:PRK14247 83 rvQMVFQIPNPIpNLSIFENV--ALGLKLNRLVKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMT-IVLVTHFPQQAARISDYVAFLYKGQIVE 225
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-194 |
5.11e-22 |
|
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: 91.95 E-value: 5.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSL---TKKTSGTVEIFGHNLdtHPSLAKQQLGVVPQefnfgqfeka 95
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR--KPDQFQKCVAYVRQ---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 96 FDIL-----VTQAGYYGIH--------RKIAEKRAEHYLEK-LGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:cd03234 89 DDILlpgltVRETLTYTAIlrlprkssDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190
....*....|....*....|....*....|...
gi 1595846010 162 EPTAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-217 |
6.72e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.43 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGtvEIFGHNldTHPSLAKQQLGVVP 84
Cdd:PRK11247 13 LLLNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGT--APLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDILvtQAGYYGIHRKiaekRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:PRK11247 88 QDARLLPWKKVIDNV--GLGLKGQWRD----AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 165 AGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAemlcrqIAIIDRGVIKED 217
Cdd:PRK11247 162 GALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEA------VAMADRVLLIEE 209
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-233 |
7.97e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.42 E-value: 7.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 14 YRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTK------KTSGTVEIFGHNLDTHPSLA-KQQLGVVPQE 86
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKlRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 FNFGQFEKAFDILVTQAGYYGIHRKIAEKR-AEHYLEKLGLW----EKRNIQARMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 162 EPTAGVDIELRRSMWDFLTEMnENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFL----NQLSEESFI 233
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFtspkNELTEKYVI 253
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-195 |
8.27e-22 |
|
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: 90.66 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSkTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIIS--SLTKKTSGTVEIFGHNLDTHPSLAKQQLGV 82
Cdd:cd03217 1 LEIKDLH-VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 vpqefnFGQFEKAFDIlvtqagyYGIhrkiaekRAEHYLeklglwekRNIQARmLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03217 80 ------FLAFQYPPEI-------PGV-------KNADFL--------RYVNEG-FSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190
....*....|....*....|....*....|...
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMNENGTSIILTTHY 195
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREEGKSVLIITHY 163
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-216 |
8.98e-22 |
|
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: 92.18 E-value: 8.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGF--------QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPSL 75
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 AK---QQLGVVPQEfNFGQF---EKAFDILVTQAGYYGIHRKIAEK-RAEHYLEKLGL-WEKRNIQARMLSGGMKRRLMI 147
Cdd:TIGR02769 83 RRafrRDVQLVFQD-SPSAVnprMTVRQIIGEPLRHLTSLDESEQKaRIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-194 |
9.43e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.47 E-value: 9.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 10 LSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL----DTHPSLAKQQLGVVPQ 85
Cdd:PRK10908 7 VSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 EFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180
....*....|....*....|....*....
gi 1595846010 166 GVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-196 |
9.61e-22 |
|
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: 95.12 E-value: 9.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP-SLAKQQLGVV 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFgqfekaFDILVTQAGYYG--------IHRKIAEKRAEHYLEKL--GLWEKRNIQARMLSGGMKRRLMIARAMMH 153
Cdd:TIGR02868 415 AQDAHL------FDTTVRENLRLArpdatdeeLWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1595846010 154 EPKLLILDEPTAGVDIELRRSMwdfLTEMN--ENGTSIILTTHYL 196
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADEL---LEDLLaaLSGRTVVLITHHL 530
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-195 |
9.67e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.67 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKK--TSGTVEIFGHN---LDTHP------SLAKQQlgvvPQEF-- 87
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDGEDileLSPDEraragiFLAFQY----PVEIpg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 88 -NFGQFEKAfdiLVTQAGYYGIHRKIAEKRAEHYLEKLGLWE---KRNIQARmLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:COG0396 92 vSVSNFLRT---ALNARRGEELSAREFLKLLKEKMKELGLDEdflDRYVNEG-FSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190
....*....|....*....|....*....|..
gi 1595846010 164 TAGVDIELRRSMWDFLTEMNENGTSIILTTHY 195
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-214 |
1.12e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.42 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPSLA--KQQLGVVPQEFNFGQFEKAF 96
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItDKKVKLSdiRKKVGLVFQYPEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 97 --DILVTQAGYyGIHRKIAEKRAEHYLEKLGLwEKRNIQARM---LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:PRK13637 102 ekDIAFGPINL-GLSEEEIENRVKRAMNIVGL-DYEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1595846010 172 RRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK13637 180 RDEILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-216 |
6.49e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 91.30 E-value: 6.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAKQQLGVVPQEFNFGQFEKAFDI 98
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQHYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 99 LVtqagyYGI---------HRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK10851 95 IA-----FGLtvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 170 ELRRSMWDFLTEMNE--NGTSIILtTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK10851 170 QVRKELRRWLRQLHEelKFTSVFV-THDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-212 |
6.61e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 6.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALV-LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLAK 77
Cdd:PRK09700 1 MATPYIsMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 QQLGVVPQEFNFGQfekafDILVTQAGYYGIH--RKI----------AEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRL 145
Cdd:PRK09700 80 LGIGIIYQELSVID-----ELTVLENLYIGRHltKKVcgvniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-194 |
1.07e-20 |
|
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: 86.35 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEifghnldthpslakqqlgvVP 84
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------WG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKafdilvtqagyygihrkiaekraehyleklglwekrniqarmLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03221 61 STVKIGYFEQ------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 1595846010 165 AGVDIELRRSMWDFLTemNENGTsIILTTH 194
Cdd:cd03221 99 NHLDLESIEALEEALK--EYPGT-VILVSH 125
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-199 |
2.45e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.22 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDThPSLAKqqlGVV 83
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER---GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGL--WEKRNIQarMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLegAEKRYIW--QLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1595846010 162 EPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEA 199
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-216 |
2.56e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 90.93 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTYR-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDtHPSLA--KQQLGVVP 84
Cdd:TIGR02203 334 RNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA-DYTLAslRRQVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFgqfekaFDILVTQAGYYGIHRKIAEKRAEHYLEK-----------LGLWEKRNIQARMLSGGMKRRLMIARAMMH 153
Cdd:TIGR02203 413 QDVVL------FNDTIANNIAYGRTEQADRAEIERALAAayaqdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 154 EPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSII----LTThyLEEAEmlcrQIAIIDRGVIKE 216
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLViahrLST--IEKAD----RIVVMDDGRIVE 547
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-229 |
3.56e-20 |
|
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: 87.04 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 23 GINLTVPEGEFYALLGPNGAGKSTT----IGIISSLTKKTSGTVEIFGHNLDTHpSLAKQQLGVVPQE----FN--FGQF 92
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDGRPLLPL-SIRGRHIATIMQNprtaFNplFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 93 EKAFDILVTqagyYGIHRKIAEKRAEHYLEKLGLWEKRNI---QARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:TIGR02770 83 NHAIETLRS----LGKLSKQARALILEALEAVGLPDPEEVlkkYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 170 ELRRSMWDFLTEMNE-NGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDTSMKSFLNQLSE 229
Cdd:TIGR02770 159 VNQARVLKLLRELRQlFGTGILLITHDLGVVARIADEVAVMDDGrIVERGTVKEIFYNPKHE 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-226 |
5.27e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA-KQQLG 81
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQE---FNfgqfekafdilvtqagyyGIHR---KIAEKRA-----EHYLEKLGLwEK--RNIQA---------RMLSG 139
Cdd:PRK11160 418 VVSQRvhlFS------------------ATLRdnlLLAAPNAsdealIEVLQQVGL-EKllEDDKGlnawlgeggRQLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 140 GMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEMLcRQIAIIDRGVIKEDTS 219
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKT-VLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
....*..
gi 1595846010 220 MKSFLNQ 226
Cdd:PRK11160 557 HQELLAQ 563
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-218 |
1.09e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 86.66 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNG--------FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDThpsLA 76
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAK---LN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 77 KQQlgvvpqefnfgqfEKAF--DI-LVTQAGY------YGIHRKIAE--------------KRAEHYLEKLGL----WEK 129
Cdd:PRK10419 81 RAQ-------------RKAFrrDIqMVFQDSIsavnprKTVREIIREplrhllsldkaerlARASEMLRAVDLddsvLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 130 RNIQarmLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAI 208
Cdd:PRK10419 148 RPPQ---LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMV 224
|
250
....*....|
gi 1595846010 209 IDRGVIKEDT 218
Cdd:PRK10419 225 MDNGQIVETQ 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-199 |
1.20e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 86.58 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP-SLAKQQLGVVP 84
Cdd:PRK13632 10 VENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNfGQFEKAF---DILvtqagyYG-----IHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13632 90 QNPD-NQFIGATvedDIA------FGlenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNENGT-SIILTTHYLEEA 199
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA 206
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-212 |
1.76e-19 |
|
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: 87.46 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 24 INLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFG---------HNLDTHpslaKQQLGVVPQEfnfgqfek 94
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargIFLPPH----RRRIGYVFQE-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 95 A--FDIL-VTQAGYYGIHRKIAEKRAEHY---LEKLGLWE--KRNIQArmLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:COG4148 86 ArlFPHLsVRGNLLYGRKRAPRAERRISFdevVELLGIGHllDRRPAT--LSGGERQRVAIGRALLSSPRLLLMDEPLAA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1595846010 167 VDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:COG4148 164 LDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-194 |
2.05e-19 |
|
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: 88.20 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVL--RDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTT----IGIISSLTKKTSGTVEIFGHNLDT 71
Cdd:COG4172 1 MMSMPLLsvEDLSVAFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 72 HPSLAKQQL-----GVVPQE--------FNFGQfekafdilvtQAG-----YYGIHRKIAEKRAEHYLEKLGLwekRNIQ 133
Cdd:COG4172 81 LSERELRRIrgnriAMIFQEpmtslnplHTIGK----------QIAevlrlHRGLSGAAARARALELLERVGI---PDPE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 134 ARM------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTH 194
Cdd:COG4172 148 RRLdayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITH 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-214 |
2.38e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRngfqaLKGINLTVPEGE---FYALLGpngAGKSTTIGIISSLTKKTSGTVEIFGHNLD-THPSLAKQQ 79
Cdd:COG1129 256 VLEVEGLSVGGV-----VRDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 -LGVVPQE-------------FN--FGQFEKafdilVTQAGYygIHRKIAEKRAEHYLEKLGLweK-RNIQARM--LSGG 140
Cdd:COG1129 328 gIAYVPEDrkgeglvldlsirENitLASLDR-----LSRGGL--LDRRRERALAEEYIKRLRI--KtPSPEQPVgnLSGG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 141 MKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-216 |
2.74e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTY--RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLaKQQLGVV 83
Cdd:TIGR00958 482 QDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYL-HRQVALV 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQE---FN--------FGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEklgLWEKRNiqarMLSGGMKRRLMIARAMM 152
Cdd:TIGR00958 561 GQEpvlFSgsvreniaYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTE---VGEKGS----QLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSmwdFLTEMNENGTSIILTTHYLEEAEMlCRQIAIIDRGVIKE 216
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQL---LQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-254 |
2.74e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.70 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 3 DALVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAKQQLGV 82
Cdd:PRK11432 5 NFVVLKNITKRFGSN-TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEFN-FGQFEkafdiLVTQAGY----YGIHRKIAEKRAEHYLE--KLGLWEKRNIQarMLSGGMKRRLMIARAMMHEP 155
Cdd:PRK11432 83 VFQSYAlFPHMS-----LGENVGYglkmLGVPKEERKQRVKEALElvDLAGFEDRYVD--QISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 156 KLLILDEPTAGVDIELRRSMWDFLTEMNE--NGTSIILtTHYLEEAEMLCRQIAIIDRGVIKEDTSMKS--------FLN 225
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYV-THDQSEAFAVSDTVIVMNKGKIMQIGSPQElyrqpasrFMA 234
|
250 260
....*....|....*....|....*....
gi 1595846010 226 QLSEESFIFDlaEPIAPLQLNIIGVKFNL 254
Cdd:PRK11432 235 SFMGDANIFP--ATLSGDYVDIYGYRLPR 261
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-236 |
3.26e-19 |
|
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: 84.85 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYR-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLGV 82
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQEF---------NFGQFEKAFDI--LVTQAGYYGIHRKIAEKRaEHYLEKLGLwekrniQARMLSGGMKRRLMIARAM 151
Cdd:cd03252 81 VLQENvlfnrsirdNIALADPGMSMerVIEAAKLAGAHDFISELP-EGYDTIVGE------QGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 152 MHEPKLLILDEPTAGVDIE----LRRSMWDFLTemnenGTSIILTTHYLeEAEMLCRQIAIIDRGVIKEDTSMKSFLNQL 227
Cdd:cd03252 154 IHNPRILIFDEATSALDYEsehaIMRNMHDICA-----GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
....*....
gi 1595846010 228 SEESFIFDL 236
Cdd:cd03252 228 GLYAYLYQL 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-228 |
3.51e-19 |
|
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: 87.55 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 3 DALVLRDLSKTY----RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEI-FGHN-LD-THPSL 75
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwVDmTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 -----AKQQLGVVPQEFNFGQFEKAFDILvTQAGYYGIHRKIAEKRAEHYLEKLGLWEK--RNIQARM---LSGGMKRRL 145
Cdd:TIGR03269 358 dgrgrAKRYIGILHQEYDLYPHRTVLDNL-TEAIGLELPDELARMKAVITLKMVGFDEEkaEEILDKYpdeLSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 146 MIARAMMHEPKLLILDEPTAGVD----IELRRSMWDFLTEMNEngtSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMK 221
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
....*..
gi 1595846010 222 SFLNQLS 228
Cdd:TIGR03269 514 EIVEELT 520
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-214 |
4.34e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.62 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSlAKQQLGVVPQE 86
Cdd:PRK11000 6 LRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP-AERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 FNFGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 167 VDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-226 |
4.47e-19 |
|
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: 87.49 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHPSLAKQQLGVV 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQE-FNF----------GQFEKAFDILVTQAgyygihRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:TIGR01193 554 PQEpYIFsgsilenlllGAKENVSQDEIWAA------CEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMNENgtSIILTTHYLEEAEMLCRqIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQSDK-IIVLDHGKIIEQGSHDELLDR 698
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-228 |
4.83e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA--KQQLGVVp 84
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgiRKLVGIV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 qefnFGQFEKAFdilvtqagyygIHRKIAE-----------------KRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMI 147
Cdd:PRK13644 83 ----FQNPETQF-----------VGRTVEEdlafgpenlclppieirKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRqIAIIDRGVIKEDTSMKSFLNQL 227
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADR-IIVMDRGKIVLEGEPENVLSDV 226
|
.
gi 1595846010 228 S 228
Cdd:PRK13644 227 S 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-212 |
6.97e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.30 E-value: 6.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKqQLGVVPQefnfgqfekafdI 98
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrqLAR-RLALLPQ------------H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 99 LVTQAGyYGIHRKIAEKRAEHylekLGLW------EKRNIQARM---------------LSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK11231 85 HLTPEG-ITVRELVAYGRSPW----LSLWgrlsaeDNARVNQAMeqtrinhladrrltdLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 158 LILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-214 |
7.19e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGV- 82
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVa 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 -VPQE-------------FNF---GQFEKAFdilvtqAGYYGIHRKIAEKRAEHYLEKLGLwekR----NIQARMLSGGM 141
Cdd:COG3845 337 yIPEDrlgrglvpdmsvaENLilgRYRRPPF------SRGGFLDRKAIRAFAEELIEEFDV---RtpgpDTPARSLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-194 |
8.85e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.59 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKqQLGVVP 84
Cdd:COG4604 4 IKNVSKRYGGK-VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSreLAK-RLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QE--FN----------FGQFE------KAFDilvtqagyygiHRKIAEkraehYLEKLGLwekRNIQARM---LSGGMKR 143
Cdd:COG4604 82 QEnhINsrltvrelvaFGRFPyskgrlTAED-----------REIIDE-----AIAYLDL---EDLADRYldeLSGGQRQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 144 RLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTH 194
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH 194
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-216 |
9.97e-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: 83.73 E-value: 9.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTV----------EIFGHNLDTHPS 74
Cdd:TIGR02323 4 LQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtyimrsgaelELYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 75 LAKQQLGVVPQE------------FNFGQfekafDILVTQAGYYGIHRKIAEKraehYLEKLGLWEKR-NIQARMLSGGM 141
Cdd:TIGR02323 83 LMRTEWGFVHQNprdglrmrvsagANIGE-----RLMAIGARHYGNIRATAQD----WLEEVEIDPTRiDDLPRAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-175 |
1.02e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.28 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDThpslakqqlgVV 83
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE----------LE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEfnfgqfekaFDI-LVTQ--AGY----------YG----------IHRKIAEkrAEHYLEKLGLWEKRniqARMLSGG 140
Cdd:PRK11650 73 PAD---------RDIaMVFQnyALYphmsvrenmaYGlkirgmpkaeIEERVAE--AARILELEPLLDRK---PRELSGG 138
|
170 180 190
....*....|....*....|....*....|....*
gi 1595846010 141 MKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQM 173
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-203 |
1.37e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 83.24 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEifghnldtHPslAKQQL 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------RN--GKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEFNF--------GQF------EKAFDILVTqagyygIHRKIAEKRAEHYLEKlglwekrniqarmLSGGMKRRLM 146
Cdd:PRK09544 70 GYVPQKLYLdttlpltvNRFlrlrpgTKKEDILPA------LKRVQAGHLIDAPMQK-------------LSGGETQRVL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYL-----EEAEMLC 203
Cdd:PRK09544 131 LARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLhlvmaKTDEVLC 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-208 |
1.54e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 85.73 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL---DTHPSLAK 77
Cdd:PRK11288 1 SSPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 ------QQLGVVP-----QEFNFGQFEKAFDIlvtqagyygIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLM 146
Cdd:PRK11288 80 gvaiiyQELHLVPemtvaENLYLGQLPHKGGI---------VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAI 208
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-218 |
1.63e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LAKQQLGVVPQE---FNFGQFE 93
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakIMREAVAIVPEGrrvFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 94 KAfdilVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRR 173
Cdd:PRK11614 99 EN----LAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1595846010 174 SMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDT 218
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGhVVLEDT 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-226 |
1.87e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.46 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLaKQQLGVVPQEFNFGQFEKAFD 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASL-RNQVALVSQNVHLFNDTIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 98 ILVTQAGYYGIHRKIAEKRAEH---YLEKL--GLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELR 172
Cdd:PRK11176 437 IAYARTEQYSREQIEEAARMAYamdFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 173 RSMWDFLTEMNENGTSIILtTHYL---EEAEmlcrQIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:PRK11176 517 RAIQAALDELQKNRTSLVI-AHRLstiEKAD----EILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-231 |
3.28e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.13 E-value: 3.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDA-LVLRDLSkTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSL-----TKKTSGTVEIFGHNL---DT 71
Cdd:PRK14239 1 MTEPiLQVSDLS-VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIyspRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 72 HPSLAKQQLGVV---PQEFNFGQFEKafdiLVTQAGYYGIHRK-IAEKRAEHYLEKLGLWEKrnIQARM------LSGGM 141
Cdd:PRK14239 80 DTVDLRKEIGMVfqqPNPFPMSIYEN----VVYGLRLKGIKDKqVLDEAVEKSLKGASIWDE--VKDRLhdsalgLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEAEMLCRQIA-IIDRGVIKEDTSM 220
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGfFLDGDLIEYNDTK 232
|
250
....*....|.
gi 1595846010 221 KSFLNQLSEES 231
Cdd:PRK14239 233 QMFMNPKHKET 243
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-216 |
5.91e-18 |
|
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: 81.00 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLGV 82
Cdd:cd03244 3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE-FNF-GQFEKAFDILvtqaGYYgihrkiAEKRAEHYLEKLGLWEKRNIQARML-----------SGGMKRRLMIAR 149
Cdd:cd03244 83 IPQDpVLFsGTIRSNLDPF----GEY------SDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 150 AMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLeEAEMLCRQIAIIDRGVIKE 216
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCT-VLTIAHRL-DTIIDSDRILVLDKGRVVE 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-215 |
8.39e-18 |
|
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: 82.47 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYrnGFQALKgINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-------DTHPSlaKQQLG 81
Cdd:TIGR02142 4 RFSKRL--GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkgiFLPPE--KRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEfnfgqfEKAFDIL-VTQAGYYGIHRKIAEKRA---EHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKL 157
Cdd:TIGR02142 79 YVFQE------ARLFPHLsVRGNLRYGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 158 LILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIK 215
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-191 |
1.41e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.09 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLaKQQLG 81
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRtvTRASL-RRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQE---FNFGQFEkafDILVTQAGYYGIHRKIAEKRAE--HYLEKLGLWEKRNI--QARMLSGGMKRRLMIARAMMHE 154
Cdd:PRK13657 413 VVFQDaglFNRSIED---NIRVGRPDATDEEMRAAAERAQahDFIERKPDGYDTVVgeRGRQLSGGERQRLAIARALLKD 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 1595846010 155 PKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIIL 191
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELMKGRTTFII 526
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-217 |
1.48e-17 |
|
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: 79.56 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLGVVP 84
Cdd:cd03245 5 FRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QE---FN---------FGQFEKAFDIL--VTQAGY--------YGIHRKIAEkraehyleklglwekrniQARMLSGGMK 142
Cdd:cd03245 85 QDvtlFYgtlrdnitlGAPLADDERILraAELAGVtdfvnkhpNGLDLQIGE------------------RGRGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 143 RRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEnGTSIILTTH---YLEeaemLCRQIAIIDRGVIKED 217
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHrpsLLD----LVDRIIVMDSGRIVAD 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
5-196 |
1.51e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.27 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRngfqaLKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTkKTSGTVEIFGHNLD--THPSLAKQQlGV 82
Cdd:COG4138 1 LQLNDVAVAGR-----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSdwSAAELARHR-AY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQefnfgQFEKAFDILVTQagYYGIHR------KIAEKRAEHYLEKLGLWEK--RNIQArmLSGGMKRRLMIARAMMH- 153
Cdd:COG4138 74 LSQ-----QQSPPFAMPVFQ--YLALHQpagassEAVEQLLAQLAEALGLEDKlsRPLTQ--LSGGEWQRVRLAAVLLQv 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 154 ------EPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYL 196
Cdd:COG4138 145 wptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-168 |
2.87e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 79.74 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGF----QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLAK--Q 78
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 79 QLGVVPQ------------EFNF------GQFekafdilvtqagyYGIHRKIAEKRAEHYLEKL-----GLwEKR-NIQA 134
Cdd:COG1101 81 YIGRVFQdpmmgtapsmtiEENLalayrrGKR-------------RGLRRGLTKKRRELFRELLatlglGL-ENRlDTKV 146
|
170 180 190
....*....|....*....|....*....|....
gi 1595846010 135 RMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:COG1101 147 GLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-245 |
4.83e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.41 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVeIFGHNLDTHPSLAK--QQLGVVPQ--EFNFG----Q 91
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEKlrKHIGIVFQnpDNQFVgsivK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 92 FEKAFDILVTQAGYYGIHRKIAEKraehyLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVSEA-----LKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 172 RRSMWDFLTEMN-ENGTSIILTTHYLEEAeMLCRQIAIIDRG-VIKEDTSMKSFLNQLSEESFIFDLAEPIAPLQL 245
Cdd:PRK13648 178 RQNLLDLVRKVKsEHNITIISITHDLSEA-MEADHVIVMNKGtVYKEGTPTEIFDHAEELTRIGLDLPFPIKINQM 252
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
8-202 |
6.12e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.61 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSkTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-----------HPSLA 76
Cdd:PRK13539 6 EDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpdvaeachylgHRNAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 77 KQQLGVVpqefnfgqfekafDILVTQAGYYGIHrkiaEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13539 85 KPALTVA-------------ENLEFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHY---LEEAEML 202
Cdd:PRK13539 148 IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-216 |
9.01e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.52 E-value: 9.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSL-AKQQLGVVPQEFNfGQF----- 92
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWdVRRQVGMVFQNPD-NQFvgatv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 93 --EKAFDiLVTQagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIE 170
Cdd:PRK13635 100 qdDVAFG-LENI----GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1595846010 171 LRRSMWDFLTEMNENGT-SIILTTHYLEEAEMLCRqIAIIDRGVIKE 216
Cdd:PRK13635 175 GRREVLETVRQLKEQKGiTVLSITHDLDEAAQADR-VIVMNKGEILE 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-199 |
1.01e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTYRNgFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSL-----TKKTSGTVEIFGHNL---DTHPSLAKQQ 79
Cdd:PRK14243 14 ENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLyapDVDPVEVRRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVPQEFNfgQFEKA-FDILVTQA---GYYGIHRKIAEKRaehyLEKLGLWE----KRNIQARMLSGGMKRRLMIARAM 151
Cdd:PRK14243 93 IGMVFQKPN--PFPKSiYDNIAYGArinGYKGDMDELVERS----LRQAALWDevkdKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLEEA 199
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQA 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-212 |
1.02e-16 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 77.12 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTtigIISSL---TKKTSGTVEIFGHnldthpslakqqLGVVPQE---FN----- 88
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS------------IAYVSQEpwiQNgtire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 89 ---FG---------------QFEKAFDILVtqagyYGIHRKIAEKraehyleklGLwekrniqarMLSGGMKRRLMIARA 150
Cdd:cd03250 85 nilFGkpfdeeryekvikacALEPDLEILP-----DGDLTEIGEK---------GI---------NLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWD--FLTEMNENGTsIILTTH---YLEEAEmlcrQIAIIDRG 212
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKT-RILVTHqlqLLPHAD----QIVVLDNG 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
15-194 |
1.02e-16 |
|
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: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 15 RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL-------GVVPqef 87
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylghlpGLKP--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 88 nfgqfekAFDILVTQAGYYGIHRKiAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGV 167
Cdd:TIGR01189 87 -------ELSALENLHFWAAIHGG-AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180
....*....|....*....|....*..
gi 1595846010 168 DIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:TIGR01189 159 DKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-197 |
1.30e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 77.69 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISS--LTKKTSGTVEIFGHNLDTHPSLAKQQLGVvpqefnFGQFEKAFDI 98
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERARAGL------FLAFQYPEEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 99 L-VTQAGYygIHRKIAEKRAEHYLEKLGLWE-----KRNIQA---------RML----SGGMKRRLMIARAMMHEPKLLI 159
Cdd:TIGR01978 90 PgVSNLEF--LRSALNARRSARGEEPLDLLDfekllKEKLALldmdeeflnRSVnegfSGGEKKRNEILQMALLEPKLAI 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLE 197
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR 205
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-200 |
2.17e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.37 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTyRNGFQALKGINLTVPEGEFYALLGPNGAGKST----TIGIISSlTKKTSGTVEIFGHNLDTHPSLAKQqL 80
Cdd:COG4136 2 LSLENLTIT-LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTllaaIAGTLSP-AFSASGEVLLNGRRLTALPAEQRR-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQE------FNFGQfEKAFDILVTqagyygIHRKIAEKRAEHYLEKLGLwekRNIQARM---LSGGMKRRLMIARAM 151
Cdd:COG4136 79 GILFQDdllfphLSVGE-NLAFALPPT------IGRAQRRARVEQALEEAGL---AGFADRDpatLSGGQRARVALLRAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDF-LTEMNENGTSIILTTHYLEEAE 200
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAP 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-223 |
3.00e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 3 DALVLRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSL-----TKKTSGTVEIFGHNLDTHPSLa 76
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddNPNSKITVDGITLTAKTVWDI- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 77 KQQLGVVPQEFNfGQFEKAF--DILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHE 154
Cdd:PRK13640 83 REKVGIVFQNPD-NQFVGATvgDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 155 PKLLILDEPTAGVDIELRRSMWDFLTE-MNENGTSIILTTHYLEEAEMlCRQIAIIDRG-VIKEDTSMKSF 223
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEANM-ADQVLVLDDGkLLAQGSPVEIF 231
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
22-216 |
3.19e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.95 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 22 KGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSL-AKQQLGVVPQEFNfgqfeKAFDI-- 98
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNAT-----TPGDItv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 99 --LVTQAGY-----YGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:PRK10253 99 qeLVARGRYphqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1595846010 172 RRSMWDFLTEMN-ENGTSIILTTHYLEEAemlCRQ----IAIIDRGVIKE 216
Cdd:PRK10253 179 QIDLLELLSELNrEKGYTLAAVLHDLNQA---CRYashlIALREGKIVAQ 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
4.80e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 4.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP------- 73
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 74 ---SLAKQQLGVVPQE------------FNFGQfekafDILVTQAGYYGihrKIAEKrAEHYLEKLGLWEKR-NIQARML 137
Cdd:PRK11701 82 errRLLRTEWGFVHQHprdglrmqvsagGNIGE-----RLMAVGARHYG---DIRAT-AGDWLERVEIDAARiDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 138 SGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-194 |
9.13e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.75 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 17 GFQA-----LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLGVVPQEFN-F 89
Cdd:PRK10247 14 GYLAgdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTlF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 90 GqfEKAFDILVTQagyYGI-HRKIAEKRAEHYLEKLGLWE---KRNIQArmLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:PRK10247 94 G--DTVYDNLIFP---WQIrNQQPDPAIFLDDLERFALPDtilTKNIAE--LSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190
....*....|....*....|....*....|
gi 1595846010 166 GVDIELRRSMWDFLTEMN-ENGTSIILTTH 194
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYVrEQNIAVLWVTH 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-222 |
1.26e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 75.54 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSL--AKQQLGVVPQEFNfGQFEKAF-- 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENVwdIRHKIGMVFQNPD-NQFVGATve 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 97 DILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMW 176
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1595846010 177 DFLTEMNE-NGTSIILTTHYLEEaemlcrqIAIIDRGVIKEDTSMKS 222
Cdd:PRK13650 181 KTIKGIRDdYQMTVISITHDLDE-------VALSDRVLVMKNGQVES 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-216 |
2.01e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.83 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKT--YRNGF------QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP-SL 75
Cdd:PRK15112 5 LEVRNLSKTfrYRTGWfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 AKQQLGVVPQE----FNFGQ-FEKAFDI-LVTQAGYYGIHRkiaEKRAEHYLEKLGLW-EKRNIQARMLSGGMKRRLMIA 148
Cdd:PRK15112 85 RSQRIRMIFQDpstsLNPRQrISQILDFpLRLNTDLEPEQR---EKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 149 RAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNE-NGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHQGEVVE 230
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-216 |
2.09e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 76.68 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT--HPSLaKQQLGVVP 84
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlsHSVL-RQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QefnfgqfekafDILVTQAGYYG---IHRKIAEKRAEHYLEKL-----------GLWEKRNIQARMLSGGMKRRLMIARA 150
Cdd:PRK10790 422 Q-----------DPVVLADTFLAnvtLGRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENgTSIILTTHYLE---EAEmlcrQIAIIDRGVIKE 216
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLStivEAD----TILVLHRGQAVE 554
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-240 |
2.24e-15 |
|
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: 76.38 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGH-------NLDTHPSLAKQQ 79
Cdd:TIGR03269 3 VKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHvalcekcGYVERPSKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVV-----PQEFNFGQFEKAFDILVT----------------------------QAGYYGihrKIAEKRAEHYLEKLGL 126
Cdd:TIGR03269 82 CPVCggtlePEEVDFWNLSDKLRRRIRkriaimlqrtfalygddtvldnvlealeEIGYEG---KEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 127 WEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTE-MNENGTSIILTTHYLEEAEMLCRQ 205
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1595846010 206 IAIIDRGVIKE----DTSMKSFLNQLS--EESFIFDLAEPI 240
Cdd:TIGR03269 239 AIWLENGEIKEegtpDEVVAVFMEGVSevEKECEVEVGEPI 279
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-194 |
2.53e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKK---TSGTVEIFGHNLDThpSLAKQQLGVVPQ-EFNFGQFeKAF 96
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDA--KEMRAISAYVQQdDLFIPTL-TVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 97 DILVTQAgYYGIHRKIAEK----RAEHYLEKLGLWEKRNI------QARMLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:TIGR00955 118 EHLMFQA-HLRMPRRVTKKekreRVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180
....*....|....*....|....*...
gi 1595846010 167 VDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-195 |
2.61e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 16 NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISS--LTKKTSGTVEIFGHNLDTHPSLAKQQLGVvpqefnFGQFE 93
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI------FLAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 94 KAFDIL-VTQAGY----YGIHRKIAEKRAEHYLEKLGLWEKR----NIQARML--------SGGMKRRLMIARAMMHEPK 156
Cdd:CHL00131 92 YPIEIPgVSNADFlrlaYNSKRKFQGLPELDPLEFLEIINEKlklvGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHY 195
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-233 |
3.33e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 73.46 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNgfQALKgINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNlDTHPSLAKQQLGVVP 84
Cdd:PRK10771 2 LKLTDITWLYHH--LPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFgqfekaFDIL-VTQAGYYGIH---RKIAEKRA--EHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:PRK10771 78 QENNL------FSHLtVAQNIGLGLNpglKLNAAQREklHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 159 ILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSEESFI 233
Cdd:PRK10771 152 LLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASAL 227
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-168 |
4.91e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 74.38 E-value: 4.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALV-LRDLSKTY--RNGF--------QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL 69
Cdd:COG4608 3 MAEPLLeVRDLKKHFpvRGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 70 dTHPSLAK-----QQLGVVPQE----FNFGQfeKAFDILvtqAGYYGIH----RKIAEKRAEHYLEKLGLwekRNIQAR- 135
Cdd:COG4608 83 -TGLSGRElrplrRRMQMVFQDpyasLNPRM--TVGDII---AEPLRIHglasKAERRERVAELLELVGL---RPEHADr 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1595846010 136 ---MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:COG4608 154 yphEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-206 |
4.97e-15 |
|
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: 72.14 E-value: 4.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 15 RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDthpslakQQLGVVPQEFNF-GQFE 93
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-------FQRDSIARGLLYlGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 94 KAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDielRR 173
Cdd:cd03231 83 GIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD---KA 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1595846010 174 SMWDFLTEMN---ENGTSIILTTHY-LEEAEMLCRQI 206
Cdd:cd03231 160 GVARFAEAMAghcARGGMVVLTTHQdLGLSEAGAREL 196
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-194 |
6.88e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.84 E-value: 6.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 3 DALVLRDLSKTYRNGFQALKGINLTVPEGEfyALL--GPNGAGKSTTIGIISSLTKKTSGTVeifghnldTHPSLAKqqL 80
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR--V 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQefnfgqfeKAFDILVT--QAGYY-GIHRKIAEKRAEHYLEKLGL------------WEKRniqarmLSGGMKRRL 145
Cdd:COG4178 429 LFLPQ--------RPYLPLGTlrEALLYpATAEAFSDAELREALEAVGLghlaerldeeadWDQV------LSLGEQQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEnGTSIILTTH 194
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP-GTTVISVGH 542
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-196 |
7.22e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 73.85 E-value: 7.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTY--RNGF-------QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT 71
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvKRGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 72 HPSLAKQQLGVVPQefnfgqfekafdiLVTQAGYYGIH--RKI----------------AEKR--AEHYLEKLGLW-EKR 130
Cdd:PRK11308 82 ADPEAQKLLRQKIQ-------------IVFQNPYGSLNprKKVgqileepllintslsaAERRekALAMMAKVGLRpEHY 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 131 NIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRS----MWDFLTEMnenGTSIILTTHYL 196
Cdd:PRK11308 149 DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQvlnlMMDLQQEL---GLSYVFISHDL 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-194 |
7.23e-15 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 74.78 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDT-HPSLAKQQLGVVPQE---F------NFG 90
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPQDvelFdgtiaeNIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 91 QFEKAFDILVTQAGYY-GIHRKIAeKRAEHYLEKLGlwekrnIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:COG4618 428 RFGDADPEKVVAAAKLaGVHEMIL-RLPDGYDTRIG------EGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD 500
|
170 180
....*....|....*....|....*
gi 1595846010 170 ELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:COG4618 501 EGEAALAAAIRALKARGATVVVITH 525
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-216 |
1.38e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 74.09 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--THPSLaKQQLG 81
Cdd:COG5265 357 EVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRdvTQASL-RAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQE---FNfgqfekafDILvtqagYYGI--------HRKIAE--KRA--EHYLEKL-----------GLwekrniqar 135
Cdd:COG5265 436 IVPQDtvlFN--------DTI-----AYNIaygrpdasEEEVEAaaRAAqiHDFIESLpdgydtrvgerGL--------- 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 136 MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSII----LTThyLEEAEmlcrQIAIIDR 211
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLViahrLST--IVDAD----EILVLEA 567
|
....*
gi 1595846010 212 GVIKE 216
Cdd:COG5265 568 GRIVE 572
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-225 |
1.52e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 73.53 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHP-----SLAKQQLGVVPQEFNFGQFEK 94
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelrEVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 95 AFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 175 MWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLN 225
Cdd:PRK10070 203 MQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-194 |
2.28e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL-------GVVPqefNFGQFE 93
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLcfvghrsGINP---YLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 94 KAFDILVTQAGYYGIHRKIAEKRAEHYLEklglwekrnIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDielRR 173
Cdd:PRK13540 94 NCLYDIHFSPGAVGITELCRLFSLEHLID---------YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---EL 161
|
170 180
....*....|....*....|....
gi 1595846010 174 SMWDFLTEMNEN---GTSIILTTH 194
Cdd:PRK13540 162 SLLTIITKIQEHrakGGAVLLTSH 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-209 |
3.51e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.51 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEI--------FGhnlDTHPSLA 76
Cdd:NF040905 2 LEMRGITKTF-PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEIlfdgevcrFK---DIRDSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 77 K------QQLGVVPQ----EFNFgqfekafdiLVTQAGYYG-IHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRL 145
Cdd:NF040905 78 LgiviihQELALIPYlsiaENIF---------LGNERAKRGvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAII 209
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVL 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-233 |
4.80e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQ- 79
Cdd:PRK10762 1 MQALLQLKGIDKAF-PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 -LGVVPQEFNF-GQFEKAFDIL-----VTQAGyyGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMM 152
Cdd:PRK10762 80 gIGIIHQELNLiPQLTIAENIFlgrefVNRFG--RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 153 HEPKLLILDEPT-AGVDIElRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAII-DRGVIKEdtsmkSFLNQLSEE 230
Cdd:PRK10762 158 FESKVIIMDEPTdALTDTE-TESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFrDGQFIAE-----REVADLTED 231
|
...
gi 1595846010 231 SFI 233
Cdd:PRK10762 232 SLI 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-196 |
6.46e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.93 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 18 FQALKGINLTVPEGEFYALLGPNGAGKSTT----IGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVPQEFNFGQ-- 91
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSslaiMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 92 ------FEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWE---KRNIQARMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:PRK11022 100 tslnpcYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMN--ENgTSIILTTHYL 196
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQqkEN-MALVLITHDL 214
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-216 |
1.40e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 22 KGINLTVPEGEFYALLGPNGAGKSTT----IGIISSLTKKTSGTVEIFGHNLdtHP-SLAKQQLGVVPQefnfgQFEKAF 96
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPV--APcALRGRKIATIMQ-----NPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 97 DILVTQAGY-------YGIHRKIAekRAEHYLEKLGLWEKRNI---QARMLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:PRK10418 93 NPLHTMHTHaretclaLGKPADDA--TLTAALEAVGLENAARVlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 167 VDIELRRSMWDFLTE-MNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK10418 171 LDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-223 |
1.41e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 69.74 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSL-AKQQLGVVPQEFNfGQFEKAF--D 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWnLRRKIGMVFQNPD-NQFVGATveD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 98 ILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWD 177
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1595846010 178 FLTEMNENGTSIILT-THYLEEAEMLCRQIAIIDRGVIKEDTSMKSF 223
Cdd:PRK13642 182 VIHEIKEKYQLTVLSiTHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-215 |
1.42e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.29 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 24 INLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL-DTHP--SLA--KQQLGVVPQE------------ 86
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfDAEKgiCLPpeKRRIGYVFQDarlfphykvrgn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 -------FNFGQFEKAFDILvtqagyyGIhrkiaekraEHYLEKLglwekrniqARMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:PRK11144 97 lrygmakSMVAQFDKIVALL-------GI---------EPLLDRY---------PGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGVIK 215
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-194 |
1.49e-13 |
|
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: 67.18 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNldthpslakqQLGVVP 84
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------DLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QE--FNFGQFEkafDILVtqagyygihrkiaekraehYLeklglWEkrniqaRMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03223 71 QRpyLPLGTLR---EQLI-------------------YP-----WD------DVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMnenGTSIILTTH 194
Cdd:cd03223 118 ATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-212 |
1.88e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 70.62 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIF--------GHNLDTHP--- 73
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsgsplkaSNIRDTERagi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 74 SLAKQQLGVVPqefNFGQFEKAF-DILVTQAGYYgIHRKIAEKRAEHYLEKLGLWEKRNIQARM-LSGGMKRRLMIARAM 151
Cdd:TIGR02633 81 VIIHQELTLVP---ELSVAENIFlGNEITLPGGR-MAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-194 |
2.17e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.88 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPS--LA-KQQLG 81
Cdd:PRK13638 2 LATSDLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRglLAlRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFNFGQFEKAFDI-LVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSdIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 1595846010 161 DEPTAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-168 |
2.58e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.52 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTK-----KTSGTVEIFGHNL---DTHPSL 75
Cdd:PRK14258 7 AIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyerRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 76 AKQQLGVVPQEFNFGQFEkAFDILVTQAGYYGIHRKIA-EKRAEHYLEKLGLWE----KRNIQARMLSGGMKRRLMIARA 150
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMS-VYDNVAYGVKIVGWRPKLEiDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCIARA 164
|
170
....*....|....*...
gi 1595846010 151 MMHEPKLLILDEPTAGVD 168
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLD 182
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-226 |
2.65e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.88 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 2 TDALVLRDLSKTYRNG----FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAK 77
Cdd:PRK13645 4 SKDIILDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 Q------QLGVVpqeFNFGQFEKAFDILVTQAGYYGIH----RKIAEKRAEHYLEKLGLWEKRNIQARM-LSGGMKRRLM 146
Cdd:PRK13645 84 EvkrlrkEIGLV---FQFPEYQLFQETIEKDIAFGPVNlgenKQEAYKKVPELLKLVQLPEDYVKRSPFeLSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRG-VIKEDTSMKSFL 224
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGkVISIGSPFEIFS 240
|
..
gi 1595846010 225 NQ 226
Cdd:PRK13645 241 NQ 242
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-226 |
3.04e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.16 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 18 FQALKGINLTVPEGEFYALLGPNGAGKS----TTIGIISS---------------LTKKTSGTV-EIFGHN--------- 68
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDnwhvtadrfrwngidLLKLSPRERrKIIGREiamifqeps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 69 --LDTHPSLAKQQLGVVPQEFNFGQFEKAFDilvtqagyygiHRKiaeKRAEHYLEKLGLwekRNIQARM------LSGG 140
Cdd:COG4170 100 scLDPSAKIGDQLIEAIPSWTFKGKWWQRFK-----------WRK---KRAIELLHRVGI---KDHKDIMnsypheLTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 141 MKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTS 219
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
....*..
gi 1595846010 220 MKSFLNQ 226
Cdd:COG4170 243 TEQILKS 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-214 |
3.40e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKtyrNGFqalKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVV- 83
Cdd:PRK15439 269 LTVEDLTG---EGF---RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVy 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 -PQEFN-FGQFEKA------FDILVTQAGYYgIHRKIAEKRAEHYLEKLGL-WEKRNIQARMLSGGMKRRLMIARAMMHE 154
Cdd:PRK15439 343 lPEDRQsSGLYLDAplawnvCALTHNRRGFW-IKPARENAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 155 PKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
5-196 |
4.88e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRngfqaLKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTkKTSGTVEIFGHNLDT--HPSLAKQQlGV 82
Cdd:PRK03695 1 MQLNDVAVSTR-----LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsAAELARHR-AY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQefnfgQFEKAFDILVTQagYYGIHR--KIAEKRAEHYL----EKLGLWEK--RNIQArmLSGGMKRR-------LMI 147
Cdd:PRK03695 74 LSQ-----QQTPPFAMPVFQ--YLTLHQpdKTRTEAVASALnevaEALGLDDKlgRSVNQ--LSGGEWQRvrlaavvLQV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1595846010 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYL 196
Cdd:PRK03695 145 WPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-168 |
1.41e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.71 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 24 INLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdthPSLAKQQLGVVPQE----FNFGQF---EKAF 96
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSRLYTVRKRmsmlFQSGALftdMNVF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 97 DILV------TQAGYYGIHRKIAEKraehyLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:PRK11831 103 DNVAyplrehTQLPAPLLHSTVMMK-----LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-196 |
1.99e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.67 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYR--NG-FQALKGINLTVPEGEFYALLGPNGAGKSTT----IGIISSlTKKTSGTVEIFGHNLdthPSLAK 77
Cdd:PRK09473 13 LDVKDLRVTFStpDGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTafalMGLLAA-NGRIGGSATFNGREI---LNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 QQLGVVPQEfnfgQFEKAF-DILVTQAGYYGIHRKIAE--------KRAEHYLEKLGLWEKRNI---QARM------LSG 139
Cdd:PRK09473 89 KELNKLRAE----QISMIFqDPMTSLNPYMRVGEQLMEvlmlhkgmSKAEAFEESVRMLDAVKMpeaRKRMkmypheFSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 140 GMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYL 196
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDL 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-212 |
2.92e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALV-LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEI--------FGHNLDT 71
Cdd:PRK13549 1 MMEYLLeMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIifegeelqASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 72 HP---SLAKQQLGVVPQ----EFNFGQFEkafdilVTQAGYygIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRR 144
Cdd:PRK13549 80 ERagiAIIHQELALVKElsvlENIFLGNE------ITPGGI--MDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 145 LMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-223 |
3.17e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.50 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 17 GFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSG-----TVEIFGHNLDTHPSLA--KQQLGVVPQEFNF 89
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLefRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 90 GQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKrnIQARM------LSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDA--VKDRLsdspfrLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 164 TAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSF 223
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-228 |
7.96e-12 |
|
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: 66.09 E-value: 7.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQA-LKGINLTVPEGEFYALLGPNGAGKSTtigIISSLTK--KTSGTVEIFGHNLDthpSLAKQQ-- 79
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKST---LLSALLRllSTEGEIQIDGVSWN---SVTLQTwr 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 --LGVVPQE-FNF-GQFEKAFDIlvtqagyygiHRKIAEKRAEHYLEKLGLW-------EKRNIQ----ARMLSGGMKRR 144
Cdd:TIGR01271 1292 kaFGVIPQKvFIFsGTFRKNLDP----------YEQWSDEEIWKVAEEVGLKsvieqfpDKLDFVlvdgGYVLSNGHKQL 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 145 LMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYLeEAEMLCRQIAIIDRGVIKEDTSMKSFL 224
Cdd:TIGR01271 1362 MCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT-VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
....
gi 1595846010 225 NQLS 228
Cdd:TIGR01271 1440 NETS 1443
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-194 |
1.14e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 15 RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfghnlDTHPSLAKQQLGVVPQEFNFGQFEK 94
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-----DGKTATRGDRSRFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 95 AFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PRK13543 96 DLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITL 175
|
170 180
....*....|....*....|
gi 1595846010 175 MWDFLTEMNENGTSIILTTH 194
Cdd:PRK13543 176 VNRMISAHLRGGGAALVTTH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-199 |
1.15e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.04 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIIS-SLTKKTSGTVEIFGHNLDTHPSL--AKQQLGVVPQEFNFGQFEKAFD 97
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgDHPQGYSNDLTLFGRRRGSGETIwdIKKHIGYVSSSLHLDYRVSTSV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 98 ILVTQAGYY---GIHRKIAE---KRAEHYLEKLGLwEKRNIQA--RMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK10938 356 RNVILSGFFdsiGIYQAVSDrqqKLAQQWLDILGI-DKRTADApfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
170 180 190
....*....|....*....|....*....|.
gi 1595846010 170 ELRRSMWDFLTEMNENG-TSIILTTHYLEEA 199
Cdd:PRK10938 435 LNRQLVRRFVDVLISEGeTQLLFVSHHAEDA 465
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-230 |
1.17e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 15 RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSL--AKQQLGVVPQEFN---- 88
Cdd:PRK09700 273 SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdaVKKGMAYITESRRdngf 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 89 FGQFEKAFDILVTQ----AGYYG----IHRKIAEKRAEHYLEKLGL---WEKRNIQArmLSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK09700 353 FPNFSIAQNMAISRslkdGGYKGamglFHEVDEQRTAENQRELLALkchSVNQNITE--LSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 158 LILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIkedTSMKSFLNQLSEE 230
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL---TQILTNRDDMSEE 500
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-194 |
1.23e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.90 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 23 GINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL-------GV----VPQE-FNFg 90
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIktelTALEnLRF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 91 qfekafdilvtqagYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEP-----TA 165
Cdd:PRK13538 98 --------------YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPftaidKQ 163
|
170 180
....*....|....*....|....*....
gi 1595846010 166 GVDIELRRsmwdfLTEMNENGTSIILTTH 194
Cdd:PRK13538 164 GVARLEAL-----LAQHAEQGGMVILTTH 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-291 |
1.36e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.73 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALV-LRDLSKTYRNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKK-----TSGTVEIFGHNL-- 69
Cdd:PRK15134 1 MTQPLLaIENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLlh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 70 ---DTHPSLAKQQLGVVPQE----FN-FGQFEKA-FDILVTqagYYGIHRKIAEKRAEHYLEKLGLwekRNIQARM---- 136
Cdd:PRK15134 81 aseQTLRGVRGNKIAMIFQEpmvsLNpLHTLEKQlYEVLSL---HRGMRREAARGEILNCLDRVGI---RQAAKRLtdyp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 137 --LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM-NENGTSIILTTHYLEEAEMLCRQIAIIDRGV 213
Cdd:PRK15134 155 hqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 214 IKEDTSMKSFLN--------QL--SE-ESFIFDLAEPIAP-LQLNIIGVKFNlIDSSTLEVTMDKAHTLNDL-FQLL--E 278
Cdd:PRK15134 235 CVEQNRAATLFSapthpytqKLlnSEpSGDPVPLPEPASPlLDVEQLQVAFP-IRKGILKRTVDHNVVVKNIsFTLRpgE 313
|
330
....*....|...
gi 1595846010 279 SQGIRVRSMRNKS 291
Cdd:PRK15134 314 TLGLVGESGSGKS 326
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-202 |
1.64e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.61 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGtvEIFghnLDTHPSLAKQqlgvvP 84
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSG--EIL---LDGKPVTAEQ-----P 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFN------FGQFEkAFDILVTQAGYygihrKIAEKRAEHYLEKLGLWEK--------RNIQarmLSGGMKRRLMIARA 150
Cdd:PRK10522 393 EDYRklfsavFTDFH-LFDQLLGPEGK-----PANPALVEKWLERLKMAHKleledgriSNLK---LSKGQKKRLALLLA 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMW-DFLTEMNENGTSIILTTH---YLEEAEML 202
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHddhYFIHADRL 519
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-228 |
1.83e-11 |
|
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: 63.33 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQA-LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKkTSGTVEIFGHNLDTHP-SLAKQQLGV 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPlQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 VPQE-FNF-GQFEKAFDIlvtqagyYGIHR-----KIAEKRA-----EHYLEKLGLWEKRNiqARMLSGGMKRRLMIARA 150
Cdd:cd03289 82 IPQKvFIFsGTFRKNLDP-------YGKWSdeeiwKVAEEVGlksviEQFPGQLDFVLVDG--GCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 151 MMHEPKLLILDEPTAGVD----IELRRSMWDFLTemnenGTSIILTTHYLeEAEMLCRQIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDpityQVIRKTLKQAFA-----DCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
..
gi 1595846010 227 LS 228
Cdd:cd03289 227 KS 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-216 |
2.23e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGVVPQeFNFGQFEKAFDIL 99
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQ-FIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 100 VTqAGY--------YGI-HRKIAEKRAEHYLEKLGLWEKRNIQ-ARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK10261 418 QT-VGDsimeplrvHGLlPGKAAAARVAWLLERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1595846010 170 ELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK10261 497 SIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-196 |
2.38e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNL----DTHPSLAKQQLGVVPQE-------- 86
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDplaslnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 FNFGqfekafDILVT--QAGYYGIHRKIAEKRAEHYLEKLGLWEkrNIQARM---LSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK15079 115 MTIG------EIIAEplRTYHPKLSRQEVKDRVKAMMLKVGLLP--NLINRYpheFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 1595846010 162 EPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYL 196
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDL 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-212 |
2.70e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQLGV--VP 84
Cdd:PRK10982 1 MSNISKSF-PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIsmVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNFGQFEKAFDIL----VTQAGYYGIHRKIAeKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK10982 80 QELNLVLQRSVMDNMwlgrYPTKGMFVDQDKMY-RDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 161 DEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-216 |
4.12e-11 |
|
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: 63.55 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 18 FQALKGINLTVPEGEFYALLGPNGAGKSTT----IGIISSltkktSGTVEIFGHNLDTHPSLA----KQQLGVVPQE--- 86
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRAlrplRRRMQVVFQDpfg 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 -----FNFGQfekafdI----LVTQagyyGIHRKIAE--KRAEHYLEKLGLweKRNIQARM---LSGGMKRRLMIARAMM 152
Cdd:COG4172 374 slsprMTVGQ------IiaegLRVH----GPGLSAAErrARVAEALEEVGL--DPAARHRYpheFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLQrEHGLAYLFISHDLAVVRALAHRVMVMKDGKVVE 506
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-216 |
6.89e-11 |
|
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: 60.89 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYR-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA-KQQLGVVP 84
Cdd:cd03369 9 VENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QE---------FNFGQFEKAFDILVTQAgyygihRKIAEKraehyleklGLwekrniqarMLSGGMKRRLMIARAMMHEP 155
Cdd:cd03369 89 QDptlfsgtirSNLDPFDEYSDEEIYGA------LRVSEG---------GL---------NLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1595846010 156 KLLILDEPTAGVDIE--------LRRSMwdfltemneNGTSIILTTHYLEEAeMLCRQIAIIDRGVIKE 216
Cdd:cd03369 145 RVLVLDEATASIDYAtdaliqktIREEF---------TNSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-216 |
8.66e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTT----IGIISSltkktSGTVEIFG---HNLDTHPSLA-KQQLGVVPQEFNfG 90
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINS-----QGEIWFDGqplHNLNRRQLLPvRHRIQVVFQDPN-S 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 91 QFEKAFDILVTQAGYYGIHRKI-----AEKRAEHYLEKLGL-WEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVHQPTlsaaqREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 165 AGVDIELRRSMWDFLTEMNE-NGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQkHQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-214 |
1.25e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.17 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTsGTVEIFGHNL-DTHPSLAKQQLGVV 83
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELrELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 ---PQEFN--------FGQFEkAFDILVTQAgyygihrkIAEKRAEHYLEKL--GLWEKRNIQARMLSGGMKRRLMIARA 150
Cdd:PRK11174 429 gqnPQLPHgtlrdnvlLGNPD-ASDEQLQQA--------LENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTEmNENGTSIILTTHYLEEAEMlCRQIAIIDRGVI 214
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-194 |
2.60e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.05 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNldthPSLAKQQL---GVVPQEfnfgqfekafD 97
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN----RKPTKQILkrtGFVTQD----------D 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 98 IL-----VTQAGYY--------GIHRKIAEKRAEHYLEKLGLWEKRNIQA-----RMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:PLN03211 150 ILyphltVRETLVFcsllrlpkSLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190
....*....|....*....|....*....|....*
gi 1595846010 160 LDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-170 |
2.88e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGfQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTV---EifghnldthpslaKQQL 80
Cdd:PRK15064 319 ALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsE-------------NANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 GVVPQEfnfgqFEKAFDILVTQAGYYGIHRKiaEKRAEH----YLEKLgLWEKRNI--QARMLSGGMKRRLMIARAMMHE 154
Cdd:PRK15064 385 GYYAQD-----HAYDFENDLTLFDWMSQWRQ--EGDDEQavrgTLGRL-LFSQDDIkkSVKVLSGGEKGRMLFGKLMMQK 456
|
170
....*....|....*.
gi 1595846010 155 PKLLILDEPTAGVDIE 170
Cdd:PRK15064 457 PNVLVMDEPTNHMDME 472
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-194 |
3.21e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 4 ALVLRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTtigIISSLT-----KKTSGTVEIFGHNLDTHPSLAK 77
Cdd:COG2401 28 AIVLEAFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKST---LLRLLAgalkgTPVAGCVDVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 78 QqlgvVPQEFNFGQfekAFDILvTQAGY---YGIHRKIAEkraehyleklglwekrniqarmLSGGMKRRLMIARAMMHE 154
Cdd:COG2401 105 A----IGRKGDFKD---AVELL-NAVGLsdaVLWLRRFKE----------------------LSTGQKFRFRLALLLAER 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1595846010 155 PKLLILDEPTAGVDIEL-RRSMWDFLTEMNENGTSIILTTH 194
Cdd:COG2401 155 PKLLVIDEFCSHLDRQTaKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
137-191 |
6.27e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 6.27e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIIL 191
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL 450
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-214 |
7.94e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 24 INLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTH-PSLA-----------KQQLGVVP-----QE 86
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRsPRDAiragimlcpedRKAEGIIPvhsvaDN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 FNF---GQFEKAFDIlvtqagyygIHRKIAEKRAEHYLEKLGLWEKRNIQARM-LSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:PRK11288 352 INIsarRHHLRAGCL---------INNRWEAENADRFIRSLNIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 163 PTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVI 214
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
16-209 |
8.72e-10 |
|
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: 59.41 E-value: 8.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 16 NGFqALKGinLTVP-EGEFYALLGPNGAGKSTTIGIISSLTK-----------------KTSGTvEIFGH-----NLDTH 72
Cdd:COG1245 86 NGF-RLYG--LPVPkKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkRFRGT-ELQDYfkklaNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 73 PSLAKQQLGVVPQEFNfGqfeKAFDILvtqagyygihRKIAEK-RAEHYLEKLGL---WEkRNIqaRMLSGGMKRRLMIA 148
Cdd:COG1245 162 VAHKPQYVDLIPKVFK-G---TVRELL----------EKVDERgKLDELAEKLGLeniLD-RDI--SELSGGELQRVAIA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 149 RAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAII 209
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-209 |
1.03e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.66 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 5 LVLRDLS---KTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTV------------------- 62
Cdd:PRK15093 4 LDIRNLTiefKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTadrmrfddidllrlsprer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 63 -EIFGHN-----------LDTHPSLAKQQLGVVPQEFNFGQFEKAFDilvtqagyygiHRKiaeKRAEHYLEKLGLWEKR 130
Cdd:PRK15093 84 rKLVGHNvsmifqepqscLDPSERVGRQLMQNIPGWTYKGRWWQRFG-----------WRK---RRAIELLHRVGIKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 131 NIQARM---LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNEN-GTSIILTTHYLEEAEMLCRQI 206
Cdd:PRK15093 150 DAMRSFpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWADKI 229
|
...
gi 1595846010 207 AII 209
Cdd:PRK15093 230 NVL 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-231 |
1.09e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.90 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 1 MTDALVLRDLSKTyrngFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGH--NLDTHPSLAKQ 78
Cdd:PRK13546 24 MKDALIPKHKNKT----FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 79 QLGVVPQEFnfgqfekafdilvtQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:PRK13546 100 LTGIENIEF--------------KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 159 ILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE----DTSMK---SFLNQLSEES 231
Cdd:PRK13546 166 VIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDygelDDVLPkyeAFLNDFKKKS 245
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-229 |
1.72e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNG--FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGhnldthpslaKQQLGVVP 84
Cdd:PRK13545 24 LKDLFFRSKDGeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------SAALIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 85 QEFNfGQFEKAFDILVtQAGYYGIHRKIAEKRAEHYLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:PRK13545 94 SGLN-GQLTGIENIEL-KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQLSE 229
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-212 |
1.83e-09 |
|
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: 58.41 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEI-----FGHnLDTHPSL--AKQQ 79
Cdd:TIGR03719 7 MNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqpgikVGY-LPQEPQLdpTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 80 LGVVP----------QEFN-----FGQFEKAFDILVTQAGyygihrKIAEKraehyLEKLGLWE-KRNIQARM------- 136
Cdd:TIGR03719 86 RENVEegvaeikdalDRFNeisakYAEPDADFDKLAAEQA------ELQEI-----IDAADAWDlDSQLEIAMdalrcpp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 137 -------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIE----LRRSMWDFltemneNGTsIILTTH---YLEEAeml 202
Cdd:TIGR03719 155 wdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQEY------PGT-VVAVTHdryFLDNV--- 224
|
250
....*....|
gi 1595846010 203 CRQIAIIDRG 212
Cdd:TIGR03719 225 AGWILELDRG 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-194 |
2.44e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 26 LTVPEGEFYALLGPNGAGKSTTIGIIS--------------SLT---------KKTSGTV---------EIFGHNLDTHP 73
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqDLIvarlqqdppRNVEGTVydfvaegieEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 74 SLakQQLGVVPQEFNFGQFEKAFDILVTQAGYYgihrkiAEKRAEHYLEKLGLwekrNIQARM--LSGGMKRRLMIARAM 151
Cdd:PRK11147 104 IS--HLVETDPSEKNLNELAKLQEQLDHHNLWQ------LENRINEVLAQLGL----DPDAALssLSGGWLRKAALGRAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLteMNENGtSIILTTH 194
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISH 211
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-189 |
2.45e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.22 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 16 NGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVeifghnldTHPslAKQQLGVVPQE--FNFGQFE 93
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRL--------TKP--AKGKLFYVPQRpyMTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 94 KafDILVTQAGYYGIHRKIAEKRAEHYLEKLGL---------WEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:TIGR00954 533 D--QIIYPDSSEDMKRRGLSDKDLEQILDNVQLthilereggWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180
....*....|....*....|....*
gi 1595846010 165 AGVDIELRRSMWDFLTEMNENGTSI 189
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFGITLFSV 635
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-212 |
2.80e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdthPSLA----KQQLGVVPQE-FNFG---- 90
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPL---TKLQldswRSRLAVVSQTpFLFSdtva 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 91 -------------QFEKAfdilvtqAGYYGIHRKIAeKRAEHYLEKLGlweKRNIqarMLSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK10789 407 nnialgrpdatqqEIEHV-------ARLASVHDDIL-RLPQGYDTEVG---ERGV---MLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 158 LILDEPTAGVDIELRRSMWDFLTEMNENGTsIILTTHYL----EEAEMLC-RQIAIIDRG 212
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGEGRT-VIISAHRLsaltEASEILVmQHGHIAQRG 531
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-195 |
6.74e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLT--KKTSGTVEIFGHNL-DTHPS--------LAKQQLGVVPQEFNF 89
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLlELSPEdragegifMAFQYPVEIPGVSNQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 90 GQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGLWE---KRNIQARmLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:PRK09580 97 FFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEdllTRSVNVG-FSGGEKKRNDILQMAVLEPELCILDESDSG 175
|
170 180
....*....|....*....|....*....
gi 1595846010 167 VDIELRRSMWDFLTEMNENGTSIILTTHY 195
Cdd:PRK09580 176 LDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-194 |
6.79e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 6.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 3 DALVLRDLSKTY---RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLD--------- 70
Cdd:PRK10261 11 DVLAVENLNIAFmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqviel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 71 THPSLAKQQ------LGVVPQE--------FNFGQfEKAFDILVTQagyyGIHRKIAEKRAEHYLEKLGLWEKRNIQAR- 135
Cdd:PRK10261 91 SEQSAAQMRhvrgadMAMIFQEpmtslnpvFTVGE-QIAESIRLHQ----GASREEAMVEAKRMLDQVRIPEAQTILSRy 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 136 --MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMN-ENGTSIILTTH 194
Cdd:PRK10261 166 phQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITH 227
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-191 |
8.50e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 15 RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIF-GHNL-DTHPSLAKQQLGVVPQE------ 86
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLkDINLKWWRSKIGVVSQDpllfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 87 ----------FNFGQFEKAFDILV--TQAGYYGIHRKIAEKRA--------EHYLEKLGLWE-KRNIQ------------ 133
Cdd:PTZ00265 475 siknnikyslYSLKDLEALSNYYNedGNDSQENKNKRNSCRAKcagdlndmSNTTDSNELIEmRKNYQtikdsevvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 134 ----------------------ARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEM--NENGTSI 189
Cdd:PTZ00265 555 kvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITI 634
|
..
gi 1595846010 190 IL 191
Cdd:PTZ00265 635 II 636
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-210 |
1.07e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 25 NLTVPEGEFYALLGPNGAGKSttigiisSLTKKTSGTVEIFGHNLD---THP---SLAKQQlGVVPQEFNfgqfEKAFDI 98
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKS-------ALARALAGELPLLSGERQsqfSHItrlSFEQLQ-KLVSDEWQ----RNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 99 LVTQAGYYGihRKIAE---------KRAEHYLEKLG---LWEKRNIQarmLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:PRK10938 91 LSPGEDDTG--RTTAEiiqdevkdpARCEQLAQQFGitaLLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1595846010 167 VDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIID 210
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLA 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-203 |
1.11e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLA-KQQLGVVPQefnfgQFEKAFDIL 99
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfARKVAYLPQ-----QLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 100 VTQ---AGYYGIH----RKIAEKRaEHYLEKLGLWEKRNIQARM---LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK10575 102 VRElvaIGRYPWHgalgRFGAADR-EKVEEAISLVGLKPLAHRLvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190
....*....|....*....|....*....|....*
gi 1595846010 170 ELRRSMWDFLTEMN-ENGTSIILTTHYLEEAEMLC 203
Cdd:PRK10575 181 AHQVDVLALVHRLSqERGLTVIAVLHDINMAARYC 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-230 |
1.99e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
90
....*....|....*
gi 1595846010 217 DtsmksFLNQ-LSEE 230
Cdd:PRK13549 486 D-----LINHnLTQE 495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-172 |
2.78e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYrNGFQalkginLTVPEGEFYA-----LLGPNGAGKSTTIGIISSLTKKTSGTVEifghnldthpslAKQQLGVV 83
Cdd:PRK13409 345 DLTKKL-GDFS------LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVD------------PELKISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEFNFGQFEKAFDILvtqagyygihRKIAEKRAEHY-----LEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:PRK13409 406 PQYIKPDYDGTVEDLL----------RSITDDLGSSYykseiIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170
....*....|....
gi 1595846010 159 ILDEPTAGVDIELR 172
Cdd:PRK13409 476 LLDEPSAHLDVEQR 489
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-209 |
5.90e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 13 TYRNGFQALKGINLTVP-EGEFYALLGPNGAGKSTTIGIISSLTKKTSGTV-------EIFGH--------------NLD 70
Cdd:cd03236 7 VHRYGPNSFKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdEILDEfrgselqnyftkllEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 71 THPSLAKQQLGVVPQEFNfgqfEKAFDILvtqagyygihRKIAEKRA-EHYLEKLGLWE--KRNIQArmLSGGMKRRLMI 147
Cdd:cd03236 87 VKVIVKPQYVDLIPKAVK----GKVGELL----------KKKDERGKlDELVDQLELRHvlDRNIDQ--LSGGELQRVAI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1595846010 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAII 209
Cdd:cd03236 151 AAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-234 |
6.21e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.21 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTI-GIISSLTKKTSGTVEIFGhnldthpslakqQLGVVPQE---FNFGQFEKAF 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLIsAMLGELSHAETSSVVIRG------------SVAYVPQVswiFNATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 97 DILVTQAGYYGihRKIAEKRAEHYLEKLGLWEKRNIQAR--MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PLN03232 701 FGSDFESERYW--RAIDVTALQHDLDLLPGRDLTEIGERgvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 175 MWDFLTEMNENGTSIILTT---HYLEEAEmlcrQIAIIDRGVIKEDTSMKsflnQLSEESFIF 234
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTnqlHFLPLMD----RIILVSEGMIKEEGTFA----ELSKSGSLF 833
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
137-217 |
7.63e-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: 53.29 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRGVIKE 216
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
.
gi 1595846010 217 D 217
Cdd:TIGR02633 484 D 484
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-170 |
1.18e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfGHNLDthpsLAKqqlgvvpqefnFGQFEKAFDILV 100
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----VAY-----------FDQHRAELDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 101 TqagyygIHRKIAEKRAE--------H---YLEKLGLWEKRNIQ-ARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:PRK11147 399 T------VMDNLAEGKQEvmvngrprHvlgYLQDFLFHPKRAMTpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
..
gi 1595846010 169 IE 170
Cdd:PRK11147 473 VE 474
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
16-185 |
1.20e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 16 NGFqALKGinLTVP-EGEFYALLGPNGAGKSTTIGIISSLTK----KTSGTV---EIF----GHNLDTH-PSLAKQQLGV 82
Cdd:PRK13409 86 NGF-KLYG--LPIPkEGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPswdEVLkrfrGTELQNYfKKLYNGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 83 V--PQEFNfgQFEKAFDILVTQagyygIHRKIAEK-RAEHYLEKLGL---WEkRNIQArmLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13409 163 VhkPQYVD--LIPKVFKGKVRE-----LLKKVDERgKLDEVVERLGLeniLD-RDISE--LSGGELQRVAIAAALLRDAD 232
|
170 180
....*....|....*....|....*....
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNEN 185
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAEG 261
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-208 |
1.35e-07 |
|
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: 50.44 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTkktsgtveiFGHNLDTHPSLAKQQLGVVPQefnfgqFEKAFDILV 100
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLAL---------GGAQSATRRRSGVKAGCIVAA------VSAELIFTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 101 TQagyygihrkiaekraehyleklglwekrniqarmLSGGMKRRLMIARAMMHEPK----LLILDEPTAGVDIELRRSMW 176
Cdd:cd03227 76 LQ----------------------------------LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|..
gi 1595846010 177 DFLTEMNENGTSIILTTHYLEEAEMLCRQIAI 208
Cdd:cd03227 122 EAILEHLVKGAQVIVITHLPELAELADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
9-170 |
1.43e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVeiFGHnldthpslAKQQLGVVPQEFN 88
Cdd:PLN03073 513 DASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--FRS--------AKVRMAVFSQHHV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 89 FGQFEKAFDILVTQAGYYGihrkIAEKRAEHYLEKLGLWEKRNIQAR-MLSGGMKRRLMIARAMMHEPKLLILDEPTAGV 167
Cdd:PLN03073 583 DGLDLSSNPLLYMMRCFPG----VPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
...
gi 1595846010 168 DIE 170
Cdd:PLN03073 659 DLD 661
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-194 |
1.53e-07 |
|
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: 50.70 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSltKKTSGTVE----IFGHNLDthPSLAKQqLGVVPQEfnfgqfek 94
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLD--KNFQRS-TGYVEQQ-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 95 afDILvtqagyygihrkiaekraehyLEKLGLWEKRNIQA--RMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELR 172
Cdd:cd03232 88 --DVH---------------------SPNLTVREALRFSAllRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAA 144
|
170 180
....*....|....*....|..
gi 1595846010 173 RSMWDFLTEMNENGTSIILTTH 194
Cdd:cd03232 145 YNIVRFLKKLADSGQAILCTIH 166
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-226 |
1.79e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 7 LRDLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKST-TIGIISsLTKKTSGTVEIFGHNL-DTHPSLAKQQLGVV 83
Cdd:TIGR00957 1287 FRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSlTLGLFR-INESAEGEIIIDGLNIaKIGLHDLRFKITII 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQE---FN---------FGQFEKAFDILVTQAGYYGIHRKIAEKRAEHYLEKLGlwekrniqaRMLSGGMKRRLMIARAM 151
Cdd:TIGR00957 1366 PQDpvlFSgslrmnldpFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGG---------ENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 152 MHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTsiILTTHYLEEAEMLCRQIAIIDRGVIKEDTSMKSFLNQ 226
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT--VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-172 |
2.28e-07 |
|
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: 50.87 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFY-----ALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSL--AKQQLGVvpqefnfgq 91
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYikADYEGTV--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 92 fekafdilvtqagYYGIHRKIAEKRAEHY-----LEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:cd03237 79 -------------RDLLSSITKDFYTHPYfkteiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
....*.
gi 1595846010 167 VDIELR 172
Cdd:cd03237 146 LDVEQR 151
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-181 |
2.98e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVeifghnldthpSLAKQ-QLGVVPQ---EFnFGQFEKAF 96
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----------GLAKGiKLGYFAQhqlEF-LRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 97 DILVTQAgyygihRKIAEKRAEHYLEKLGLW-EKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:PRK10636 396 QHLARLA------PQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
....*.
gi 1595846010 176 WDFLTE 181
Cdd:PRK10636 470 TEALID 475
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-168 |
6.39e-07 |
|
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: 49.18 E-value: 6.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 15 RNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTK---KTSGTVEIFGHNLDTHPSLAKQQLGVVPQEfnfgq 91
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKEFAEKYPGEIIYVSEE----- 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1595846010 92 fekafdilvtqagyygiHRKIAEKRAEHYLEkLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:cd03233 92 -----------------DVHFPTLTVRETLD-FALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-172 |
6.47e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYrNGFQalkginLTVPEGEFY-----ALLGPNGAGKSTTIGIISSLTKKTSGTVEifghnldthpslAKQQLGVV 83
Cdd:COG1245 346 DLTKSY-GGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVD------------EDLKISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 84 PQEfnfgqFEKAFDILVTQAGYYGIHRKIAEKRAEH-YLEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:COG1245 407 PQY-----ISPDYDGTVEEFLRSANTDDFGSSYYKTeIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170
....*....|
gi 1595846010 163 PTAGVDIELR 172
Cdd:COG1245 482 PSAHLDVEQR 491
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-181 |
6.65e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.70 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 8 RDLSKTYrNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfGHNLD------THPSLAKQQlg 81
Cdd:TIGR03719 326 ENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlayvdqSRDALDPNK-- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 82 VVPQEFNFGQfekafDILvtQAGYYGIhrkiaEKRAehYLEKLGLweKRNIQARM---LSGGMKRRLMIARAMMHEPKLL 158
Cdd:TIGR03719 402 TVWEEISGGL-----DII--KLGKREI-----PSRA--YVGRFNF--KGSDQQKKvgqLSGGERNRVHLAKTLKSGGNVL 465
|
170 180
....*....|....*....|...
gi 1595846010 159 ILDEPTAGVDIELRRSMWDFLTE 181
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLN 488
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-170 |
1.57e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 6 VLRDLSKTYRNGFQALKGINLTvpegeFY-----ALLGPNGAGKSTTIGIISSLTKKTSG--------TVEIfghnLDTH 72
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEGearpapgiKVGY----LPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 73 PSL--AKQQLGVVP----------QEFN-----FGQFEKAFDILVTQAGyygihrKIAEKraehyLEKLGLWekrNIQAR 135
Cdd:PRK11819 79 PQLdpEKTVRENVEegvaevkaalDRFNeiyaaYAEPDADFDALAAEQG------ELQEI-----IDAADAW---DLDSQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 136 M------------------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIE 170
Cdd:PRK11819 145 LeiamdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-168 |
1.85e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 18 FQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLT----KKTSGTVEIFGHNLDthpSLAKQQLGVV----PQEFNF 89
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPE---EIKKHYRGDVvynaETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 90 GQFeKAFDILVTQAG-------YYGIHRKI-AEKRAEHYLEKLGLWEKRNIQA-----RMLSGGMKRRLMIARAMMHEPK 156
Cdd:TIGR00956 151 PHL-TVGETLDFAARcktpqnrPDGVSREEyAKHIADVYMATYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAK 229
|
170
....*....|..
gi 1595846010 157 LLILDEPTAGVD 168
Cdd:TIGR00956 230 IQCWDNATRGLD 241
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-194 |
2.05e-06 |
|
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: 46.60 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 31 GEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFghNLDTHPSLAKQQLGVVPqefnfgqfekafdilvtqagyygihr 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--DGEDILEEVLDQLLLII-------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 111 kiaekraehyleklglwekRNIQARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWD------FLTEMNE 184
Cdd:smart00382 54 -------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKSE 114
|
170
....*....|
gi 1595846010 185 NGTSIILTTH 194
Cdd:smart00382 115 KNLTVILTTN 124
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-225 |
2.13e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 21 LKGINLTVPEGEFYALLGPNGAGKSTTI-GIISSLTKKTSGTVEIFGhnldthpslakqQLGVVPQ-------------- 85
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLIsAMLGELPPRSDASVVIRG------------TVAYVPQvswifnatvrdnil 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 ---EFNFGQFEKAFDILVTQagyygihrkiaekraeHYLEKLGLWEKRNIQAR--MLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PLN03130 701 fgsPFDPERYERAIDVTALQ----------------HDLDLLPGGDLTEIGERgvNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 161 DEPTAGVDIELRRSMWDFLTEMNENGTSIILTT---HYLEEAEmlcrQIAIIDRGVIKEDTSMKSFLN 225
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTnqlHFLSQVD----RIILVHEGMIKEEGTYEELSN 828
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-197 |
2.21e-06 |
|
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: 47.71 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 13 TYRNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLDTHPSLAKQQL------------ 80
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysvayaaqkp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 81 ----GVVPQEFNFGQ-FEKAFDILVTQAGY---------YGIHRKIAEkraehyleklglwekRNIQarmLSGGMKRRLM 146
Cdd:cd03290 89 wllnATVEENITFGSpFNKQRYKAVTDACSlqpdidllpFGDQTEIGE---------------RGIN---LSGGQRQRIC 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1595846010 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWD--FLTEMNENGTSIILTTHYLE 197
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
130-194 |
2.33e-06 |
|
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: 48.15 E-value: 2.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 130 RNIQARMLSGGMKR---RLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:pfam13304 230 GELPAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
135-192 |
2.41e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 2.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 135 RMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILT 192
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-197 |
2.76e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 38 GPNGAGKSTTIGIISSLTKKTSGtvEIFGHNLDTHpSLAKQQLGVVPQEFNFGQFEKAFDILVTQAGYYGIHRKIAEkrA 117
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSG--NIYYKNCNIN-NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYA--A 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 118 EHYLEKLGLWEKRniqARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIElRRSMWDFLTEMNENGTSIILTTHYLE 197
Cdd:PRK13541 108 IHYFKLHDLLDEK---CYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE-NRDLLNNLIVMKANSGGIVLLSSHLE 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-242 |
4.87e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYRNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGHNLdTHPSLA--KQQLGVVPQ 85
Cdd:PLN03232 1239 DVHLRYRPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV-AKFGLTdlRRVLSIIPQ 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 ---------EFNFGQFEKAFDILVTQAgYYGIHRKIAEKRaehylEKLGLWEKRNIQARMLSGGMKRRLMIARAMMHEPK 156
Cdd:PLN03232 1318 spvlfsgtvRFNIDPFSEHNDADLWEA-LERAHIKDVIDR-----NPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 157 LLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILtTHYLEEAeMLCRQIAIIDRGVIKEDTSMKSFLNQlsEESFIFDL 236
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVI-AHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSR--DTSAFFRM 1467
|
....*.
gi 1595846010 237 AEPIAP 242
Cdd:PLN03232 1468 VHSTGP 1473
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
137-212 |
2.28e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.88 E-value: 2.28e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1595846010 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTHYLEEAEMLCRQIAIIDRG 212
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
30-215 |
2.77e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 30 EGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVeifghNLDTHpslakQQLGVVPQ-EFNFGQFE--------------- 93
Cdd:PRK15064 26 GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----SLDPN-----ERLGKLRQdQFAFEEFTvldtvimghtelwev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 94 -------------------KAFDILVTQAGYYGIhrkIAEKRAEHYLEKLGLWEKRNiQARM--LSGGMKRRLMIARAMM 152
Cdd:PRK15064 96 kqerdriyalpemseedgmKVADLEVKFAEMDGY---TAEARAGELLLGVGIPEEQH-YGLMseVAPGWKLRVLLAQALF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1595846010 153 HEPKLLILDEPTAGVDIELRRSMWDFLTEmnENGTSIILT--THYLeeaEMLCRQIAIIDRGVIK 215
Cdd:PRK15064 172 SNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIIShdRHFL---NSVCTHMADLDYGELR 231
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-194 |
8.03e-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: 43.84 E-value: 8.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 16 NGFQALKGINLTVPEGeFYALLGPNGAGKSTTIGIISSLTKKTSG---TVEIFGHNLDTHP------------------- 73
Cdd:COG3593 9 KNFRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfDEEDFYLGDDPDLpeieieltfgsllsrllrl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 74 ---SLAKQQLGVVPQEFNfGQFEKAFDILVTQAGYYG--------IHRKIAEKRAEHYLEKLGLW--EKRNIQARMLSGG 140
Cdd:COG3593 88 llkEEDKEELEEALEELN-EELKEALKALNELLSEYLkelldgldLELELSLDELEDLLKSLSLRieDGKELPLDRLGSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1595846010 141 MKRRLMIA--RAMMH-----EPKLLILDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:COG3593 167 FQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-194 |
8.25e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 19 QALKGINLTVPEGEFYALLGPNGAGKST---------TIGIIssltkkTSGTVEIFGHNLDThpSLAKQqLGVVPQEfnf 89
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTllnvlaervTTGVI------TGGDRLVNGRPLDS--SFQRS-IGYVQQQ--- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 90 gqfekafDILVTQA---------GYYGIHRKIAEKRAEHYLEK-LGLWEKRNIQARM-------LSGGMKRRLMIARAMM 152
Cdd:TIGR00956 845 -------DLHLPTStvreslrfsAYLRQPKSVSKSEKMEYVEEvIKLLEMESYADAVvgvpgegLNVEQRKRLTIGVELV 917
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1595846010 153 HEPKLLI-LDEPTAGVDIELRRSMWDFLTEMNENGTSIILTTH 194
Cdd:TIGR00956 918 AKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-169 |
8.63e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 8.63e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1595846010 113 AEKRAEHYLEKLGLWEKRNIQA-RMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKAtKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-212 |
1.28e-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: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 20 ALKGINLTVPEGEFYALLGPNGAGKSTTI--GIISSLTKKTSGTVEIFGHNldthPSLAKQQLGVvpqefnfgqfekafd 97
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVneGLYASGKARLISFLPKFSRN----KLIFIDQLQF--------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 98 ILVTQAGYYGIHRKIAEkraehyleklglwekrniqarmLSGGMKRRLMIARAMMHEPK--LLILDEPTAGVDIELRRSM 175
Cdd:cd03238 71 LIDVGLGYLTLGQKLST----------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|....*..
gi 1595846010 176 WDFLTEMNENGTSIILTTHYLeeaEMLCRQIAIIDRG 212
Cdd:cd03238 129 LEVIKGLIDLGNTVILIEHNL---DVLSSADWIIDFG 162
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-170 |
2.15e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 27 TVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIFGH------NLDThPSLAKQQLG-VVPQEFNFGQFEKAFDIL 99
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvNQET-PALPQPALEyVIDGDREYRQLEAQLHDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 100 VTQAGYYGI---HRKI-------AEKRAEHYLEKLGLWEKRNIQ-ARMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:PRK10636 102 NERNDGHAIatiHGKLdaidawtIRSRAASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
..
gi 1595846010 169 IE 170
Cdd:PRK10636 182 LD 183
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
137-169 |
4.50e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 4.50e-04
10 20 30
....*....|....*....|....*....|...
gi 1595846010 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-181 |
6.17e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 9 DLSKTYrnGFQAL-KGINLTVPEGEFYALLGPNGAGKSTTIGIISSLTKKTSGTVEIfGhnlDThpslakQQLGVVPQ-- 85
Cdd:PRK11819 329 NLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G---ET------VKLAYVDQsr 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 86 -----------EFNFGQfekafDILvtQAGYYGIHrkiaeKRAehYLEKLGL----WEKRniqARMLSGGMKRRLMIARA 150
Cdd:PRK11819 397 daldpnktvweEISGGL-----DII--KVGNREIP-----SRA--YVGRFNFkggdQQKK---VGVLSGGERNRLHLAKT 459
|
170 180 190
....*....|....*....|....*....|.
gi 1595846010 151 MMHEPKLLILDEPTAGVDIELRRSMWDFLTE 181
Cdd:PRK11819 460 LKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
11-194 |
1.42e-03 |
|
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: 39.13 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 11 SKTYRNGFQALKGINLTVpegefyallGPNGAGKSTtigIISSLTKKTSGTVEIFGHNLDTHPSLAKQQ--LGVVPQEFN 88
Cdd:cd03240 11 SFHERSEIEFFSPLTLIV---------GQNGAGKTT---IIEALKYALTGELPPNSKGGAHDPKLIREGevRAQVKLAFE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 89 FGQFEKafdilvtqagyYGIHRKIAEKRAEHYLEKlglWEKRNIQARM---LSGGMKR------RLMIARAMMHEPKLLI 159
Cdd:cd03240 79 NANGKK-----------YTITRSLAILENVIFCHQ---GESNWPLLDMrgrCSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 1595846010 160 LDEPTAGVDIE-LRRSMWDFLTEMNENGTS-IILTTH 194
Cdd:cd03240 145 LDEPTTNLDEEnIEESLAEIIEERKSQKNFqLIVITH 181
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
91-197 |
3.54e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.49 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1595846010 91 QFEKAFDIlvtqagyyGIHRKIAEKRAEHYLEKLGLWEKRN-----IQARMLSGGMKRRLMIARAMM---HEPKLLILDE 162
Cdd:COG1106 160 ELLKIADP--------GIEDIEVEEEEIEDLVERKLIFKHKggnvpLPLSEESDGTKRLLALAGALLdalAKGGVLLIDE 231
|
90 100 110
....*....|....*....|....*....|....*.
gi 1595846010 163 PTAGVDIELRRSMWD-FLTEMNENGTSIILTTHYLE 197
Cdd:COG1106 232 IEASLHPSLLRKLLKlFLDLANKNNAQLIFTTHSTE 267
|
|
| |
