|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-233 |
4.53e-110 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 318.93 E-value: 4.53e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVP 84
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLNEESFI 233
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFL 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-301 |
9.01e-81 |
|
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: 246.92 E-value: 9.01e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 12 KTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVPQEFNFGQ 91
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 92 FEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 172 RRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDT--SMKDFLNQLNEESFIFD----------LAA 238
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGrIIAEGTpeELKRRLGKDTLESRPRDiqslkvevsmLIA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 239 PIEPLHVDIIGVRFNLiDPVTLEVTmDKAHTLNQLFQLMEAQGIQVRSMRNKSNRLEELFVKM 301
Cdd:TIGR01188 240 ELGETGLGLLAVTVDS-DRIKILVP-DGDETVPEIVEAAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-218 |
1.71e-78 |
|
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: 238.04 E-value: 1.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 9 DLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVPQEFN 88
Cdd:cd03265 5 NLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 89 FGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 169 IELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDT 218
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGrIIAEGT 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-214 |
9.84e-78 |
|
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: 234.60 E-value: 9.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVP 84
Cdd:cd03230 1 IEVRNLSKRYGK-KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFgqfektfdilvtqagyygipkkIAEKRAEEYLEklglwekrntqgrmLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03230 80 EEPSL----------------------YENLTVRENLK--------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 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 |
1.22e-74 |
|
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: 228.16 E-value: 1.22e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG-FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVV 83
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQefnfgqfektFDILVT----------QAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:cd03263 81 PQ----------FDALFDeltvrehlrfYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMnEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIK 215
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-232 |
7.38e-72 |
|
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: 222.04 E-value: 7.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFqALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVP 84
Cdd:COG4555 2 IEVENLSKKYGKVP-ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLNEESF 232
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENL 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-305 |
4.30e-61 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 196.48 E-value: 4.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDthpSEAKQCLGVV 83
Cdd:COG4152 1 MLELKGLTKRFGD-KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 164 TAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLNEESFIFDLAAPIEPL 243
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADGDAGWL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 244 HvDIIGVRFNLIDPVTLEVTMDKAHTLNQLFQLMEAQGiQVRSMRNKSNRLEELFVKMVEKN 305
Cdd:COG4152 237 R-ALPGVTVVEEDGDGAELKLEDGADAQELLRALLARG-PVREFEEVRPSLNEIFIEVVGEK 296
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-217 |
4.48e-60 |
|
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: 190.87 E-value: 4.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGeFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVP 84
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 165 AGVDIELRRSMWEFLTEMNEkGTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-273 |
6.08e-60 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 194.15 E-value: 6.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYK-----NGF---------------QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVE 63
Cdd:COG4586 1 IIEVENLSKTYRvyekePGLkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 64 IFGHNldthPSE-----AKQcLGVVpqefnFGQfeKT-----------FDILvtqAGYYGIPKKIAEKRAEEYLEKLGLW 127
Cdd:COG4586 81 VLGYV----PFKrrkefARR-IGVV-----FGQ--RSqlwwdlpaidsFRLL---KAIYRIPDAEYKKRLDELVELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 128 EKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRI 206
Cdd:COG4586 146 ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDRV 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 207 AIIDRGVIKEDTSMKDFLNQLNEESFI-FDLAAPIEPLHVDiIGVRFNLIDPVTLEVTMDKAHTLNQL 273
Cdd:COG4586 226 IVIDHGRIIYDGSLEELKERFGPYKTIvLELAEPVPPLELP-RGGEVIEREGNRVRLEVDPRESLAEV 292
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
3.78e-58 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 186.83 E-value: 3.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNldthPSEAKQCL 80
Cdd:COG1121 3 MMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP----PRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEFNFgqfEKTFDILV---------TQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAM 151
Cdd:COG1121 78 GYVPQRAEV---DWDFPITVrdvvlmgryGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDT 218
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHGP 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-226 |
4.10e-56 |
|
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: 181.38 E-value: 4.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVV 83
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQE-----FN--------FG--QFektfdilvtqagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIA 148
Cdd:COG1122 81 FQNpddqlFAptveedvaFGpeNL--------------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-212 |
8.95e-55 |
|
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: 177.27 E-value: 8.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS-EAKQCLGVVP 84
Cdd:cd03225 2 LKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNfGQF--EKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03225 82 QNPD-DQFfgPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 163 PTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-217 |
4.30e-54 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 176.33 E-value: 4.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVV 83
Cdd:TIGR03864 1 ALEVAGLSFRY-GARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 pqefnFGQFEKTFDILVTQ-----AGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:TIGR03864 80 -----FQQPTLDLDLSVRQnlryhAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 159 ILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMlCRRIAIIDRGVIKED 217
Cdd:TIGR03864 155 LLDEPTVGLDPASRAAITAHVRALaRDQGLSVLWATHLVDEIEA-SDRLVVLHRGRVLAD 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-214 |
1.75e-53 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 174.22 E-value: 1.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAK---- 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKElaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 --QCLGVVPQEFNFgqfEKTFDIL--VTQAGYY-GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:cd03255 80 rrRHIGFVFQSFNL---LPDLTALenVELPLLLaGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDrGVI 214
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRD-GKI 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-214 |
1.24e-52 |
|
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: 172.17 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKN---GFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLG 81
Cdd:cd03266 2 ITADALTKRFRDvkkTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQefNFGQFEK--TFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03266 82 FVSD--STGLYDRltARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
2.22e-52 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 171.38 E-value: 2.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAK 77
Cdd:COG1136 1 MSPLLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDI-SSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 ------QCLGVVPQEFN-FGqfekTFDIL--VTQAGYY-GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMI 147
Cdd:COG1136 80 larlrrRHIGFVFQFFNlLP----ELTALenVALPLLLaGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMlCRRIAIIDRGVIKEDTS 219
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSDER 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
4.17e-52 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 171.81 E-value: 4.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTD---ALTLRDLSKTY---KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS 74
Cdd:COG1116 1 MSAaapALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 75 EakqcLGVVPQEFN------------FGqfektfdiLVTQagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMK 142
Cdd:COG1116 81 D----RGVVFQEPAllpwltvldnvaLG--------LELR----GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 143 RRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDR--GVIKED 217
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-214 |
5.95e-52 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 169.77 E-value: 5.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDThpsEAKQCLGVVP 84
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
9-214 |
1.44e-51 |
|
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: 168.87 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 9 DLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEakqcLGVVPQEFN 88
Cdd:cd03235 4 DLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR----IGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 89 FgqfEKTFDILV---------TQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03235 79 I---DRDFPISVrdvvlmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-218 |
2.46e-51 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 168.69 E-value: 2.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA----KQCL 80
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEFNFgQFEKT-FD--ILVTQAGyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:COG2884 82 GVVFQDFRL-LPDRTvYEnvALPLRVT--GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDT 218
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-209 |
5.09e-51 |
|
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: 168.03 E-value: 5.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEakqcLG 81
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFN------------FGqfektfdiLVTQagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIAR 149
Cdd:cd03293 77 YVFQQDAllpwltvldnvaLG--------LELQ----GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAII 209
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-212 |
1.03e-50 |
|
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: 165.11 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYKNGFqALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS-EAKQCLGVVP 84
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QefnfgqfektfdilvtqagyygipkkiaekraeeyleklglwekrntqgrmLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-214 |
5.23e-50 |
|
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: 164.70 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNlDTHPSEAKQCLGVVP 84
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVTQAGYYGIPKKiaekRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-214 |
3.14e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 164.07 E-value: 3.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL--- 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 -GVVPQEFNfgqfektfdiLVTQ-----------AGYYGIPKKI------AEK-RAEEYLEKLGLWEKRNTQGRMLSGGM 141
Cdd:COG3638 82 iGMIFQQFN----------LVPRlsvltnvlagrLGRTSTWRSLlglfppEDReRALEALERVGLADKAYQRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
4.91e-48 |
|
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: 161.36 E-value: 4.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL 80
Cdd:COG0411 1 SDPLLEVRGLTKRFG-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVV-----PQEFN------------FGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKR 143
Cdd:COG0411 80 GIArtfqnPRLFPeltvlenvlvaaHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 144 RLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDT 218
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGrVIAEGT 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-212 |
5.09e-48 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 163.05 E-value: 5.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGFqALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQefnFGQFEKTFDI---LVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK13537 83 GVVPQ---FDNLDPDFTVrenLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-198 |
3.67e-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: 158.71 E-value: 3.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 2 TDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSG-SVEIFGHNL-DTHPSEAKQC 79
Cdd:COG1119 1 DPLLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 LGVVPQEF--NFGQFEKTFDILVTqaGYYGI------PKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAM 151
Cdd:COG1119 80 IGLVSPALqlRFPRDETVLDVVLS--GFFDSiglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKG-TSIILTTHYLEE 198
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE 205
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-218 |
1.51e-46 |
|
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: 156.83 E-value: 1.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVV- 83
Cdd:cd03219 1 LEVRGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 ----PQEF-NFGQFEktfDILV---TQAGYYGIPKKI------AEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIAR 149
Cdd:cd03219 80 tfqiPRLFpELTVLE---NVMVaaqARTGSGLLLARArreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDT 218
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGrVIAEGT 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-214 |
2.22e-46 |
|
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: 157.13 E-value: 2.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE--AKQcLG 81
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelARR-IA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFgqfekTFDILVTQA---------GYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:COG1120 79 YVPQEPPA-----PFGLTVRELvalgryphlGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-226 |
4.55e-46 |
|
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: 162.77 E-value: 4.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY----KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL 80
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 ----GVVPQefN-FGQF---EKTFDILVTQAGYYGI-PKKIAEKRAEEYLEKLGLWEK-RNTQGRMLSGGMKRRLMIARA 150
Cdd:COG1123 341 rrrvQMVFQ--DpYSSLnprMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 151 MMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-217 |
3.80e-45 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 153.26 E-value: 3.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVpq 85
Cdd:cd03267 22 SLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVV-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 efnFGQFEK-TFDILVTQAGY-----YGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03267 100 ---FGQKTQlWWDLPVIDSFYllaaiYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-213 |
7.74e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 155.37 E-value: 7.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFqALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVV 83
Cdd:PRK13536 41 AIDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQefnFGQFEKTFDI---LVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13536 120 PQ---FDNLDLEFTVrenLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGV 213
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-217 |
9.19e-45 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 151.89 E-value: 9.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAKQCL- 80
Cdd:cd03257 2 LEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDL-LKLSRRLRKIr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 ----GVVPQE----FN-----FGQFEKTFDILvtqagYYGIPKKIAEKRAEEYLEKLGLWEKR-NTQGRMLSGGMKRRLM 146
Cdd:cd03257 81 rkeiQMVFQDpmssLNprmtiGEQIAEPLRIH-----GKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-165 |
1.31e-44 |
|
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: 148.95 E-value: 1.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL--DTHPSEAKQcLGVVPQEFNFGQFEKTFDI 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdDERKSLRKE-IGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 99 LVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNT----QGRMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-225 |
3.71e-44 |
|
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: 150.42 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS----EAK 77
Cdd:cd03258 2 IELKNVSKVFGDTggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKD-FLN 225
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEvFAN 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
4.17e-44 |
|
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: 150.51 E-value: 4.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL 80
Cdd:COG1127 2 SEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 ----GVVPQE---FN---------FGQFEKTfdilvtqagyyGIPKKIAEKRAEEYLEKLGLwekRNTQGRM---LSGGM 141
Cdd:COG1127 81 rrriGMLFQGgalFDsltvfenvaFPLREHT-----------DLSEAEIRELVLEKLELVGL---PGAADKMpseLSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSM 220
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
....*
gi 491152796 221 KDFLN 225
Cdd:COG1127 227 EELLA 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-225 |
4.97e-44 |
|
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: 149.89 E-value: 4.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE--AKQCLGV 82
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFN-FGQF--EKTFDIlvtqAGYYGIPKKIAEKRAE--EYLEKLGlwEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:cd03224 80 VPEGRRiFPELtvEENLLL----GAYARRRAKRKARLERvyELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLN 225
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-214 |
1.71e-43 |
|
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: 148.05 E-value: 1.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAKQCLGVVP 84
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFN------------FGqfektfdiLVTQagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:cd03259 79 QDYAlfphltvaeniaFG--------LKLR----GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-214 |
4.25e-43 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 151.02 E-value: 4.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDA-LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQc 79
Cdd:COG3842 1 MAMPaLELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 LGVVPQEF----------N--FGqfektfdiLVTQagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMI 147
Cdd:COG3842 79 VGMVFQDYalfphltvaeNvaFG--------LRMR----GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-226 |
6.35e-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: 6.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNG-FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKT---SGSVEIFGHNLDTHP-SE 75
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSeAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 76 AKQCLGVVPQE----FN----FGQFEKTFDILvtqagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMI 147
Cdd:COG1123 81 RGRRIGMVFQDpmtqLNpvtvGDQIAEALENL-------GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-212 |
9.73e-43 |
|
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: 145.02 E-value: 9.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTH---PSEAKQCLG 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedeLPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFgqfektfdilvtqagyygIPKKIAekraeeyLEKLGLwekrntqgrMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:cd03229 80 MVFQDFAL------------------FPHLTV-------LENIAL---------GLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-214 |
1.24e-42 |
|
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: 146.94 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL---- 80
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEFNF-GQFEKTFDILVTQAGY-------YGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:cd03256 81 GMIFQQFNLiERLSVLENVLSGRLGRrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-245 |
1.28e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.46 E-value: 1.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS----EAK 77
Cdd:COG1135 2 IELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQEFN-FGQfeKT-FD-------ILvtqagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIA 148
Cdd:COG1135 82 RKIGMIFQHFNlLSS--RTvAEnvalpleIA-------GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHyleeaEM-----LCRRIAIIDRGVIKEDTSMKD 222
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH-----EMdvvrrICDRVAVLENGRIVEQGPVLD 227
|
250 260
....*....|....*....|....*.
gi 491152796 223 -FLNQLNE--ESFIFDLAAPIEPLHV 245
Cdd:COG1135 228 vFANPQSEltRRFLPTVLNDELPEEL 253
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-214 |
1.09e-41 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 143.44 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQC---LG 81
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFgqFE-KTfdIL--VTQAGYY--GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:cd03262 80 MVFQQFNL--FPhLT--VLenITLAPIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 157 LLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-208 |
1.56e-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: 140.31 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVP 84
Cdd:COG4133 3 LEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVTQAGYYGIPkkIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLR--ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEmLCRRIAI 208
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA-AARVLDL 202
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-214 |
2.66e-40 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 138.33 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTH-PSEAKQcLGVV 83
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARR-AGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 pqefnfgqfektfdiLVTQagyygipkkiaekraeeyleklglwekrntqgrmLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:cd03216 79 ---------------MVYQ----------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 164 TAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-225 |
2.84e-40 |
|
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: 140.50 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE--AKQCLGV 82
Cdd:COG0410 4 LEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFN-FGQFektfdilvT-----QAGYYGIPKKIAEKRA-EEYLE---KLGlwEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:COG0410 83 VPEGRRiFPSL--------TveenlLLGAYARRDRAEVRADlERVYElfpRLK--ERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLN 225
Cdd:COG0410 153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-217 |
1.89e-39 |
|
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: 138.08 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSL-----TKKTSGSVEIFGHN---LDTHPSEA 76
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDiydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 KQCLGVVPQEFNFgqFEKT-FDILVTQAGYYGI-PKKIAEKRAEEYLEKLGLWE--KRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:cd03260 80 RRRVGMVFQKPNP--FPGSiYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKgTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-214 |
2.09e-39 |
|
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: 136.41 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAK-QCLGVVP 84
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELaRKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QefnfgqfektfdilvtqagyygipkkiaekraeeYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 165 AGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03214 126 SHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-225 |
3.03e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 138.40 E-value: 3.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQC- 79
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 LGVVPQEfnfgqfektfdilvtqagYYGI--PKK-----IAE-----------KRAEEYLEKLGLWEK-RNTQGRMLSGG 140
Cdd:COG1124 81 VQMVFQD------------------PYASlhPRHtvdriLAEplrihglpdreERIAELLEQVGLPPSfLDRYPHQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 141 MKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTS 219
Cdd:COG1124 143 QRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELT 222
|
....*.
gi 491152796 220 MKDFLN 225
Cdd:COG1124 223 VADLLA 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-226 |
4.36e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 137.43 E-value: 4.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQC---LG 81
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLrrkVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFN-FGQfeKTfdIL--VTQAGYY--GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:COG1126 81 MVFQQFNlFPH--LT--VLenVTLAPIKvkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 157 LLILDEPTAGVDIELRRsmwEFLTEMNE---KGTSIILTTHyleeaEM-----LCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:COG1126 157 VMLFDEPTSALDPELVG---EVLDVMRDlakEGMTMVVVTH-----EMgfareVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-212 |
4.39e-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: 146.70 E-value: 4.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYK-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVPQ 85
Cdd:TIGR01257 931 VKNLVKIFEpSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQ 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 EFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:TIGR01257 1011 HNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491152796 166 GVDIELRRSMWEFLTEMnEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-212 |
6.83e-39 |
|
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: 134.82 E-value: 6.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGV 82
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFgqFEKTfdilvtqagyygipkkIAEkraeeyleklglwekrNtqgrMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03228 81 VPQDPFL--FSGT----------------IRE----------------N----ILSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 163 PTAGVDIELRRSMWEFLTEMnEKGTSIILTTHYLEEAEMlCRRIAIIDRG 212
Cdd:cd03228 123 ATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-215 |
1.11e-38 |
|
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: 135.46 E-value: 1.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfgHNLDTHPSEAKQCLGVVPQ 85
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL--NGKPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 EFNFGQFEKTfdilVTQAGYYGIPKKIAEK-RAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03226 79 DVDYQLFTDS----VREELLLGLKELDAGNeQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIK 215
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-214 |
1.54e-37 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 133.52 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFG---HNLDTHpseaKQCLG 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGkdiTNLPPH----KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-214 |
2.27e-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: 132.53 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA----KQCLGV 82
Cdd:cd03292 3 FINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEF----NFGQFEK-TFDILVTQAgyygiPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:cd03292 83 VFQDFrllpDRNVYENvAFALEVTGV-----PPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-222 |
2.28e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 139.01 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEAKQC 79
Cdd:COG3845 2 MPPALELRGITKRF-GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 -LGVVPQEFnfgqfeKTFDIL-VTQ--------AGYYGIPKKIAEKRAEEYLEKLGL--------WEkrntqgrmLSGGM 141
Cdd:COG3845 81 gIGMVHQHF------MLVPNLtVAEnivlglepTKGGRLDRKAARARIRELSERYGLdvdpdakvED--------LSVGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 142 KRRLMIARAMMHEPKLLILDEPTAG-----VDiELrrsmWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG---- 212
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVltpqeAD-EL----FEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGkvvg 221
|
250
....*....|.
gi 491152796 213 -VIKEDTSMKD 222
Cdd:COG3845 222 tVDTAETSEEE 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-209 |
4.11e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 138.23 E-value: 4.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEAKQc 79
Cdd:COG1129 1 AEPLLEMRGISKSF-GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 LGV--VPQEFN------------FGQFEKTFDIlvtqagyygIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRL 145
Cdd:COG1129 79 AGIaiIHQELNlvpnlsvaenifLGREPRRGGL---------IDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 146 MIARAMMHEPKLLILDEPTA---GVDIElrrSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAII 209
Cdd:COG1129 150 EIARALSRDARVLILDEPTAsltEREVE---RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-214 |
4.88e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 135.27 E-value: 4.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTH-PSEAKQClGVV 83
Cdd:COG1118 3 IEVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRERRV-GFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEF----------N--FGqfektFDILvtqagyyGIPKKIAEKRAEEYLEKLGL--WEKRN-TQgrmLSGGMKRRLMIA 148
Cdd:COG1118 81 FQHYalfphmtvaeNiaFG-----LRVR-------PPSKAEIRARVEELLELVQLegLADRYpSQ---LSGGQRQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-219 |
6.22e-37 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 132.08 E-value: 6.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP--SEAKQCLGV 82
Cdd:COG1137 4 LEAENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE---F-------NFgqfektFDILVTQagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:COG1137 83 LPQEasiFrkltvedNI------LAVLELR----KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 153 HEPKLLILDEPTAGVD----IELRRsMWEFLTemnEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDTS 219
Cdd:COG1137 153 TNPKFILLDEPFAGVDpiavADIQK-IIRHLK---ERGIGVLITDHNVRETLGICDRAYIISEGkVLAEGTP 220
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-215 |
1.04e-36 |
|
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: 130.98 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVP 84
Cdd:TIGR03740 1 LETKNLSKRFGKQ-TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEF-NFGQFEKtfdiLVTQAGYYGIPkkiaEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:TIGR03740 80 PLYeNLTAREN----LKVHTTLLGLP----DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 164 TAGVDI----ELRrsmwEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIK 215
Cdd:TIGR03740 152 TNGLDPigiqELR----ELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-218 |
1.11e-36 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 131.02 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA---- 76
Cdd:COG4181 8 IIELRGLTKTVGTGageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDArarl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 -KQCLGVVPQEFNfgqfektfdiLV---TQAGYYGIP-----KKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMI 147
Cdd:COG4181 88 rARHVGFVFQSFQ----------LLptlTALENVMLPlelagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMlCRRIAIIDRGVIKEDT 218
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDT 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-233 |
1.58e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 130.88 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHN-LDTHPSEAKQCLGVV 83
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDiREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEfnFGQF-----EKTFDILVTQAGYygiPKKIAEKRAEEYLEKLGL--WEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:cd03295 81 IQQ--IGLFphmtvEENIALVPKLLKW---PKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 157 LLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFL-NQLNE--ESF 232
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILrSPANDfvAEF 235
|
.
gi 491152796 233 I 233
Cdd:cd03295 236 V 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-214 |
3.21e-36 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 129.97 E-value: 3.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP--SEAKQCLGV 82
Cdd:cd03218 1 LRAENLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFN-FGQFEKTFDILVTqAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:cd03218 80 LPQEASiFRKLTVEENILAV-LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 162 EPTAGVD----IELRRsmweFLTEMNEKGTSIILTTHYLEEAemlcrrIAIIDRGVI 214
Cdd:cd03218 159 EPFAGVDpiavQDIQK----IIKILKDRGIGVLITDHNVRET------LSITDRAYI 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-226 |
1.58e-35 |
|
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: 134.50 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGV 82
Cdd:COG4988 336 SIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE---FN--------FGQFEKTfDILVTQAgyygipkkIAEKRAEEYLEKL--GLwekrNT----QGRMLSGGMKRRL 145
Cdd:COG4988 416 VPQNpylFAgtirenlrLGRPDAS-DEELEAA--------LEAAGLDEFVAALpdGL----DTplgeGGRGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNeKGTSIILTTHYLEEAEmLCRRIAIIDRGVIKEDTSMKDFLN 225
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLA 560
|
.
gi 491152796 226 Q 226
Cdd:COG4988 561 K 561
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-225 |
2.48e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 130.31 E-value: 2.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTY---KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS----EAKQ 78
Cdd:PRK11153 3 ELKNISKVFpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 CLGVVPQEFNfgqfektfdiLV---TQAGYYGIPKKIA-------EKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIA 148
Cdd:PRK11153 83 QIGMIFQHFN----------LLssrTVFDNVALPLELAgtpkaeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKD-FLN 225
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEvFSH 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-217 |
2.69e-35 |
|
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: 134.96 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTY-KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAKQCLG 81
Cdd:COG2274 473 DIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQE---FN--------FGQFEKTFDILVTQAgyygipkKIAEkrAEEYLEKL--GLwekrNTQ----GRMLSGGMKRR 144
Cdd:COG2274 553 VVLQDvflFSgtirenitLGDPDATDEEIIEAA-------RLAG--LHDFIEALpmGY----DTVvgegGSNLSGGQRQR 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 145 LMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNeKGTSIILTTHYLEEAEmLCRRIAIIDRGVIKED 217
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIR-LADRIIVLDKGRIVED 690
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-194 |
3.69e-35 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 126.00 E-value: 3.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 14 YKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS---EAKQCLGVVPQEFNFG 90
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKgllERRQRVGLVFQDPDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QFEKTFDILVTQAGY-YGIPKKIAEKRAEEYLEKLGL--WEKRNTQgrMLSGGMKRRLMIARAMMHEPKLLILDEPTAGV 167
Cdd:TIGR01166 81 LFAADVDQDVAFGPLnLGLSEAEVERRVREALTAVGAsgLRERPTH--CLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180
....*....|....*....|....*..
gi 491152796 168 DIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-218 |
5.50e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.89 E-value: 5.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS---EAKQCLG 81
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKsllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFGQFEKTFDILVTQAGY-YGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13639 82 IVFQNPDDQLFAPTVEEDVAFGPLnLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDT 218
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGkIIKEGT 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-218 |
8.02e-35 |
|
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: 126.46 E-value: 8.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL----GV 82
Cdd:cd03261 3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrmGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE---FN---------FGQFEKTfdilvtqagyyGIPKKIAEKRAEEYLEKLGLwekRNTQGRM---LSGGMKRRLMI 147
Cdd:cd03261 82 LFQSgalFDsltvfenvaFPLREHT-----------RLSEEEIREIVLEKLEAVGL---RGAEDLYpaeLSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 148 ARAMMHEPKLLILDEPTAGVD-------IELRRSMWEfltemnEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDT 218
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKK------ELGLTSIMVTHDLDTAFAIADRIAVLYDGkIVAEGT 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-214 |
9.95e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.04 E-value: 9.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDaLTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKqc 79
Cdd:COG3839 1 MAS-LELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPPKDRN-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 LGVVPQEF----------N--FGqfektfdiLVTQagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMI 147
Cdd:COG3839 77 IAMVFQSYalyphmtvyeNiaFP--------LKLR----KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-214 |
1.09e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGVV 83
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFG------QFEKTFDILvtqagyygiPKKIAEKRAEEYLEKLGL----WEKRNTQgrmLSGGMKRRLMIARAMMH 153
Cdd:COG4619 80 PQEPALWggtvrdNLPFPFQLR---------ERKFDRERALELLERLGLppdiLDKPVER---LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTE-MNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-215 |
3.23e-34 |
|
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: 132.44 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 2 TDALTLRDLSKTYK-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL 80
Cdd:TIGR01257 1935 TDILRLNELTKVYSgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQefnfgqFEKTFDILVTQAGYY------GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHE 154
Cdd:TIGR01257 2015 GYCPQ------FDAIDDLLTGREHLYlyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 155 PKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIK 215
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-225 |
1.19e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.28 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGhnLDTHPSEAKQCL-----GVVPQEFN-FGQF 92
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLirqeaGMVFQQFYlFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 93 EKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELR 172
Cdd:PRK09493 93 TALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 173 RSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLN 225
Cdd:PRK09493 173 HEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-208 |
2.37e-33 |
|
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: 124.78 E-value: 2.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY---KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKK---TSGSVEIFGHNLDTHPSEAKQ 78
Cdd:COG0444 2 LEVRNLKVYFptrRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 -----CLGVVPQE----FN-----FGQFEKTFDIlvtqagYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGR---MLSGGM 141
Cdd:COG0444 82 kirgrEIQMIFQDpmtsLNpvmtvGDQIAEPLRI------HGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAI 208
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAV 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-216 |
2.40e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 122.81 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD--THPSEA-----KQC 79
Cdd:COG4161 5 LKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsQKPSEKairllRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 LGVVPQEFNFGQFEKTFDILvTQA--GYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENL-IEApcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-214 |
4.05e-33 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 121.21 E-value: 4.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKqcLGVV 83
Cdd:cd03301 1 VELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVtDLPPKDRD--IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 164 TAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-226 |
6.76e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 127.19 E-value: 6.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTY-KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLG 81
Cdd:COG4987 333 SLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFgqfektFD------ILVT--QAGyygipkkiaEKRAEEYLEKLGL--WEKR-----NT----QGRMLSGGMK 142
Cdd:COG4987 413 VVPQRPHL------FDttlrenLRLArpDAT---------DEELWAALERVGLgdWLAAlpdglDTwlgeGGRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 143 RRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWE-FLTEMNEKgtSIILTTHYLEEAEmLCRRIAIIDRGVIKEDTSMK 221
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLAdLLEALAGR--TVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHE 554
|
....*
gi 491152796 222 DFLNQ 226
Cdd:COG4987 555 ELLAQ 559
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-230 |
1.37e-32 |
|
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: 120.46 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP--SEAKQCLGV 82
Cdd:TIGR04406 2 LVAENLIKSYK-KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFN-FGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:TIGR04406 81 LPQEASiFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 162 EPTAGVD----IELRRsmweFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNqlNEE 230
Cdd:TIGR04406 161 EPFAGVDpiavGDIKK----IIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA--NEK 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
5-225 |
3.22e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.35 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG----FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHN--LDTHPSEAKQ 78
Cdd:PRK13651 3 IKVKNIVKIFNKKlpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 CL-----------------------GVVPQEFNFGQFEKTF--DILVTqAGYYGIPKKIAEKRAEEYLEKLGLWE---KR 130
Cdd:PRK13651 83 VLeklviqktrfkkikkikeirrrvGVVFQFAEYQLFEQTIekDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDEsylQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 131 NTQGrmLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIID 210
Cdd:PRK13651 162 SPFE--LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*
gi 491152796 211 RGVIKEDTSMKDFLN 225
Cdd:PRK13651 240 DGKIIKDGDTYDILS 254
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-222 |
3.28e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.10 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNG---------------------FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTS 59
Cdd:COG1134 1 MSSMIEVENVSKSYRLYhepsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 60 GSVEIFGHnldthpseakqclgVVPQ-EFNFGqfektFD---------ILVtqAGYYGIPKKIAEKRAEEYLEKLGLWEK 129
Cdd:COG1134 81 GRVEVNGR--------------VSALlELGAG-----FHpeltgreniYLN--GRLLGLSRKEIDEKFDEIVEFAELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 130 RNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELR-RSMwEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAI 208
Cdd:COG1134 140 IDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQkKCL-ARIRELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|....
gi 491152796 209 IDRGVIKEDTSMKD 222
Cdd:COG1134 219 LEKGRLVMDGDPEE 232
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-216 |
3.95e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.58 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGV 82
Cdd:COG1132 339 EIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE---FN--------FGQFEKTFDiLVTQAgyygipkkiAEK-RAEEYLEKL--GLwekrNTQ----GRMLSGGMKRR 144
Cdd:COG1132 419 VPQDtflFSgtirenirYGRPDATDE-EVEEA---------AKAaQAHEFIEALpdGY----DTVvgerGVNLSGGQRQR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 145 LMIARAMMHEPKLLILDEPTAGVDIE----LRRSMWEFLTEMnekgTSII----LTThyLEEAEmlcrRIAIIDRGVIKE 216
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTEtealIQEALERLMKGR----TTIViahrLST--IRNAD----RILVLDDGRIVE 554
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-216 |
5.79e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.27 E-value: 5.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD--THPSEA-----KQCLGVVPQEFNF-- 89
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsKTPSDKairelRRNVGMVFQQYNLwp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 90 ------GQFEKTFDILvtqagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:PRK11124 96 hltvqqNLIEAPCRVL-------GLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 164 TAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK11124 169 TAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-214 |
6.43e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.14 E-value: 6.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHnlDTHPS---EAK 77
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR--EVNAEnekWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQEFNFGQFEKT-FDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13647 79 SKVGLVFQDPDDQVFSSTvWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 157 LLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-214 |
7.70e-31 |
|
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: 115.90 E-value: 7.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQaLKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEaKQCLGVVP 84
Cdd:cd03299 1 LKVENLSKDWKE-FK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVtqagyYGI-----PKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03299 78 QNYALFPHMTVYKNIA-----YGLkkrkvDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-275 |
8.39e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 117.04 E-value: 8.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY--KNGFQ--ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAK--- 77
Cdd:PRK13634 3 ITFQKVEHRYqyKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 --QCLGVVpqeFNFGQ---FEKTF--DILVTQAGYyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRM-LSGGMKRRLMIAR 149
Cdd:PRK13634 83 lrKKVGIV---FQFPEhqlFEETVekDICFGPMNF-GVSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDflnqln 228
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE------ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 229 eesfIFDLAAPIEPLHVDI-------------IGVRFNlIDPVTLEvtmDKAHTLNQLFQ 275
Cdd:PRK13634 233 ----IFADPDELEAIGLDLpetvkfkraleekFGISFP-KPCLTLE---ELAHEVVQLLR 284
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
5-212 |
2.07e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.10 E-value: 2.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS---EAKQCLG 81
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNfgqfEKTFDILVTQAGYYG-----IPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13636 86 MVFQDPD----NQLFSASVYQDVSFGavnlkLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 157 LLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
5-222 |
2.42e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 114.54 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE--AKQCLGV 82
Cdd:TIGR03410 1 LEVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHerARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQefnfGQfeKTFDILVT----QAGYYGIPKKiaEKRAEEYLEKL--GLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:TIGR03410 80 VPQ----GR--EIFPRLTVeenlLTGLAALPRR--SRKIPDEIYELfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 157 LLILDEPTAGV------DIE--LRRsmwefLTEmnEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKD 222
Cdd:TIGR03410 152 LLLLDEPTEGIqpsiikDIGrvIRR-----LRA--EGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-217 |
3.30e-30 |
|
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: 113.78 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 18 FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGhnldthpseakqclGVVPQ-EFNFGqFEKTF 96
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------------RVSSLlGLGGG-FNPEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 97 ---DILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRR 173
Cdd:cd03220 100 tgrENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491152796 174 SMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-225 |
3.91e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 114.22 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP--SEAKQCLGV 82
Cdd:PRK10895 4 LTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFGQFEKTFDILVtqaGYYGIPKKIA----EKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLM---AVLQIRDDLSaeqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 159 ILDEPTAGVD----IELRRsmweFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLN 225
Cdd:PRK10895 160 LLDEPFAGVDpisvIDIKR----IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-206 |
6.70e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.19 E-value: 6.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQ---ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSeAKQcl 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPG-ADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEF----------N--FG-QFEktfdilvtqagyyGIPKKIAEKRAEEYLEKLGL--------WEkrntqgrmLSG 139
Cdd:COG4525 79 GVVFQKDallpwlnvldNvaFGlRLR-------------GVPKAERRARAEELLALVGLadfarrriWQ--------LSG 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 140 GMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRI 206
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRL 205
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-216 |
7.59e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 113.69 E-value: 7.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS--------- 74
Cdd:PRK11264 3 AIEVKNLVKKFH-GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 75 EAKQCLGVVPQEFN-FGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:PRK11264 82 QLRQHVGFVFQNFNlFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-216 |
2.70e-29 |
|
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: 112.05 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQcLGVV 83
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFGQFEKTFDI----LVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03296 80 FQHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-214 |
1.32e-28 |
|
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: 108.07 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQA-LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAKQCLGV 82
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEfnfgqfektfDILvtqagyygIPKKIAEKraeeyleklglwekrntqgrMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03246 81 LPQD----------DEL--------FSGSIAEN--------------------ILSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 163 PTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMlCRRIAIIDRGVI 214
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
18-218 |
2.26e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.22 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 18 FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVPQEF---------- 87
Cdd:NF033858 279 FTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFslygeltvrq 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 88 NfgqfektfdiLVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGV 167
Cdd:NF033858 359 N----------LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 168 DIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEmLCRRIAIIDRG-VIKEDT 218
Cdd:NF033858 429 DPVARDMFWRLLIELSrEDGVTIFISTHFMNEAE-RCDRISLMHAGrVLASDT 480
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
8-214 |
2.42e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 110.28 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 8 RDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVVPQE 86
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 FNfgqfEKTFDILVTQAGYYG-----IPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK13652 87 PD----DQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-212 |
3.09e-28 |
|
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: 108.71 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAKQclgVVPQEFNFGQFEKTFD--I 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVREniA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 99 LVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEF 178
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 491152796 179 LTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:TIGR01184 157 LMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
3.69e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGFQ-----ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfgHNLDT---- 71
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTsdee 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 72 HPSEAKQCLGVVPQEFNfGQFEKTfdILVTQAGY----YGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMI 147
Cdd:PRK13633 79 NLWDIRNKAGMVFQNPD-NQIVAT--IVEEDVAFgpenLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAeMLCRRIAIIDRG-VIKEDTSMKDF 223
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGkVVMEGTPKEIF 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
5-232 |
3.94e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 108.69 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFqaLKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKqcLGVV 83
Cdd:COG3840 2 LRLDDLTYRY-GDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtALPPAERP--VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFgqfektFDIL-VTQAGYYGI-PK-KIAE---KRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:COG3840 77 FQENNL------FPHLtVAQNIGLGLrPGlKLTAeqrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLNEESF 232
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCrERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-203 |
4.31e-28 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 109.59 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGhnLDTHPSEAKQCL 80
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG--QPTRQALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEfnfGQFEKTFDILVTQA---GYYG------IPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAM 151
Cdd:PRK15056 81 AYVPQS---EEVDWSFPVLVEDVvmmGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLC 203
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFC 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-212 |
6.10e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.47 E-value: 6.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKqcl 80
Cdd:PRK11607 16 LTPLLEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQR--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 gvvPQEFNFGQFEKTFDILVTQAGYYGI-----PKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEP 155
Cdd:PRK11607 92 ---PINMMFQSYALFPHMTVEQNIAFGLkqdklPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 156 KLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-210 |
1.43e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.51 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGFQA---LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAk 77
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 qcLGVVPQEfNFGQFEKTFDILV---------TQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIA 148
Cdd:PRK10535 80 --LAQLRRE-HFGFIFQRYHLLShltaaqnveVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIID 210
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRD 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-212 |
2.00e-27 |
|
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: 105.21 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSktyknGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAKQcLGV 82
Cdd:cd03215 4 VLEVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIR-AGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 vpqefnfgqfektfdilvtqaGYygipkkIAEKRAEEYLeKLGLWEKRNTQ-GRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:cd03215 78 ---------------------AY------VPEDRKREGL-VLDLSVAENIAlSSLLSGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-212 |
2.21e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.16 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGV 82
Cdd:PRK13548 2 MLEARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFgqfekTFDILVTQ-----AGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM----- 152
Cdd:PRK13548 81 LPQHSSL-----SFPFTVEEvvamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 153 -HEPKLLILDEPTAGVDI-------ELRRSmwefLTEmnEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLahqhhvlRLARQ----LAH--ERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-199 |
2.35e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 16 NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHnldthpseakQCLGVVPQEfnfGQFEKT 95
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQR---SEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 96 FDILVTQA---------GYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:NF040873 70 LPLTVRDLvamgrwarrGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 491152796 167 VDIELRRSMWEFLTEMNEKGTSIILTTHYLEEA 199
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV 182
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-222 |
2.81e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.27 E-value: 2.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGV-- 82
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTVfq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 ---------VPQEFNFG-QFEKTfdilvtqagyygiPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:PRK09452 94 syalfphmtVFENVAFGlRMQKT-------------PAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKD 222
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-226 |
2.93e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.02 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTK--KTSGS-VEIFGHNL-------- 69
Cdd:PRK09984 1 MQTIIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVqregrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 70 DTHPSEAKQclGVVPQEFNF-GQFEKTFDILVTQAGYYGIPK-------KIAEKRAEEYLEKLGLWEKRNTQGRMLSGGM 141
Cdd:PRK09984 80 DIRKSRANT--GYIFQQFNLvNRLSVLENVLIGALGSTPFWRtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSM 220
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
....*.
gi 491152796 221 KDFLNQ 226
Cdd:PRK09984 238 QQFDNE 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-214 |
3.15e-27 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 106.96 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 20 ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-----KQCLGVVPQefNFGQFEK 94
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrRKKISMVFQ--SFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 95 -------TFDILVTqagyyGIPKKIAEKRAEEYLEKLGL--WEKRNTqgRMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:cd03294 117 rtvlenvAFGLEVQ-----GVPRAEREERAAEALELVGLegWEHKYP--DELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 166 GVDIELRRSMW-EFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03294 190 ALDPLIRREMQdELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-207 |
4.80e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 106.27 E-value: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKST---TISIISSLTK--KTSGSVEIFGHNL---DTH 72
Cdd:COG1117 8 LEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgaRVEGEILLDGEDIydpDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 73 PSEAKQCLGVVPQEFNfgQFEKT-FDILVtqAG--YYGI-PKKIAEKRAEEYLEKLGLWE----KRNTQGRMLSGGMKRR 144
Cdd:COG1117 87 VVELRRRVGMVFQKPN--PFPKSiYDNVA--YGlrLHGIkSKSELDEIVEESLRKAALWDevkdRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 145 LMIARAMMHEPKLLILDEPTAGVD------IElrrsmwEFLTEMNEKGTsIILTTHYLEEAemlcRRIA 207
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpistakIE------ELILELKKDYT-IVIVTHNMQQA----ARVS 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-169 |
4.99e-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: 4.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE--AKQcLGV 82
Cdd:COG4559 2 LEAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelARR-RAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE----FNFGQFEktfdilVTQAGYY--GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAM----- 151
Cdd:COG4559 80 LPQHsslaFPFTVEE------VVALGRAphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwe 153
|
170 180
....*....|....*....|
gi 491152796 152 --MHEPKLLILDEPTAGVDI 169
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDL 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
5-212 |
9.05e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 105.46 E-value: 9.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVp 84
Cdd:PRK11300 6 LSVSGLMMRF-GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFN----FGQFEKTFDILVTQ---------AGYYGIP-----KKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLM 146
Cdd:PRK11300 84 RTFQhvrlFREMTVIENLLVAQhqqlktglfSGLLKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-217 |
1.87e-26 |
|
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: 102.78 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYK-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVV 83
Cdd:cd03247 1 LSINNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFgqFEKTFdilvtqagyygipkkiaekraeeyleklglwekRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:cd03247 81 NQRPYL--FDTTL---------------------------------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491152796 164 TAGVDIELRRSMWEFLTEMnEKGTSIILTTHYLEEAEMLcRRIAIIDRGVIKED 217
Cdd:cd03247 126 TVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-214 |
4.34e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 103.12 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSL---TKKTSGSVEIFGHNLdtHPSEAKQCLGVVPQEFNFGQF--- 92
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPR--KPDQFQKCVAYVRQDDILLPGltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 93 EKTFDILVTQAGYYGIPKKIAEKRAEEYLEK-LGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491152796 172 RRSMWEFLTEMNEKGTSIILTTHYlEEAEM--LCRRIAIIDRGVI 214
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEI 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-215 |
1.27e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVeifghnldTHPSEAKqcLGVVPQE 86
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV--------SIPKGLR--IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 FNFG-----------------QFEKTFDILVTQ-AGYYGIPKKIAEK--------------RAEEYLEKLGLwEKRNTQG 134
Cdd:COG0488 70 PPLDddltvldtvldgdaelrALEAELEELEAKlAEPDEDLERLAELqeefealggweaeaRAEEILSGLGF-PEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 135 RM--LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRsmW--EFLteMNEKGTsIILTTH---YLEEaemLCRRIA 207
Cdd:COG0488 149 PVseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFL--KNYPGT-VLVVSHdryFLDR---VATRIL 220
|
....*...
gi 491152796 208 IIDRGVIK 215
Cdd:COG0488 221 ELDRGKLT 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
5-232 |
1.28e-25 |
|
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: 101.06 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSkTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIIS--SLTKKTSGSVEIFGHNL-DTHPSE-AKQCL 80
Cdd:cd03217 1 LEIKDLH-VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDItDLPPEErARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEfnfgqfektfdilvtqagyygiPKKIAEKRAEEYLEKLGlwekrntQGrmLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:cd03217 80 FLAFQY----------------------PPEIPGVKNADFLRYVN-------EG--FSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEML-CRRIAIIDRGVIKEdTSMKDFLNQLNEESF 232
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK-SGDKELALEIEKKGY 200
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-212 |
1.55e-25 |
|
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: 101.22 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 14 YKNGFQALKgINLTVPEgEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFG-------HNLDTHPSEAKqcLGVVPQE 86
Cdd:cd03297 8 KRLPDFTLK-IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQRK--IGLVFQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 FN-FGQFEktfdilVTQAGYYGIPKKIAEK---RAEEYLEKLGL--WEKRNTQGrmLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:cd03297 84 YAlFPHLN------VRENLAFGLKRKRNREdriSVDELLDLLGLdhLLNRYPAQ--LSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-216 |
1.58e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.23 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTK-----KTSGSVEIFGHNL---DTH 72
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIyspDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 73 PSEAKQCLGVVPQEFNFGQFEKTFDILVTQAGYYGI--PKKIAEKRAEEYLEKLGLWE----KRNTQGRMLSGGMKRRLM 146
Cdd:PRK14267 80 PIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTsIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYT-IVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-226 |
1.86e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.97 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL----DT----HPSEA 76
Cdd:PRK10619 6 LNVIDLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrDKdgqlKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 KQC------LGVVPQEFNFGQFEKTFD-ILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKrnTQGRM---LSGGMKRRLM 146
Cdd:PRK10619 85 NQLrllrtrLTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDER--AQGKYpvhLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-196 |
1.87e-25 |
|
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: 105.91 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP-SEAKQCLGVV 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDqDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFgqfektFDILVTQAGYYGIP--------KKIAEKRAEEYLEKL--GLWEKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:TIGR02868 415 AQDAHL------FDTTVRENLRLARPdatdeelwAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEkGTSIILTTHYL 196
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-214 |
2.09e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 105.52 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTH--PSEAKQ 78
Cdd:PRK15439 8 APPLLCARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-ARltPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 cLGV--VPQE-FNFGQFEKTFDILvtqagyYGIPKK-IAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHE 154
Cdd:PRK15439 86 -LGIylVPQEpLLFPNLSVKENIL------FGLPKRqASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 155 PKLLILDEPTAGVD-IELRRsMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK15439 159 SRILILDEPTASLTpAETER-LFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
4-227 |
2.19e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 102.52 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNG--FQ--ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL--DTHPSEAK 77
Cdd:PRK13649 2 GINLQNVSYTYQAGtpFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQEFNFGQ---FEKTF--DILVTQAGYyGIPKKIAEKRAEEYLEKLGLWEK-RNTQGRMLSGGMKRRLMIARAM 151
Cdd:PRK13649 82 QIRKKVGLVFQFPEsqlFEETVlkDVAFGPQNF-GVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQL 227
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDV 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-220 |
2.93e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 101.05 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAK---- 77
Cdd:PRK11629 6 LQCDNLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 -QCLGVVPQefnFGQFEKTFDILVTQA-----GyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAM 151
Cdd:PRK11629 86 nQKLGFIYQ---FHHLLPDFTALENVAmplliG--KKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSM 220
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLM 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-195 |
3.41e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKK--TSGSVEIFGHN-LDTHPSE-AKQCLGVV---PQEF---NFG 90
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYevTSGSILLDGEDiLELSPDErARAGIFLAfqyPVEIpgvSVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QFEKTfdiLVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKrntqgrML--------SGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:COG0396 96 NFLRT---ALNARRGEELSAREFLKLLKEKMKELGLDED------FLdryvnegfSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190
....*....|....*....|....*....|...
gi 491152796 163 PTAGVDIELRRSMWEFLTEMNEKGTSIILTTHY 195
Cdd:COG0396 167 TDSGLDIDALRIVAEGVNKLRSPDRGILIITHY 199
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-228 |
3.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.12 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfGHNLDTHPSEAKQC------LGVVPQEFNFGQF 92
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIkpvrkkVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 93 EKTF--DILVTQAGYyGIPKKIAEKRAEEYLEKLGL----WEKRNTQgrmLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:PRK13643 99 EETVlkDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLadefWEKSPFE---LSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 167 VDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLN 228
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-226 |
4.94e-25 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 100.38 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY-KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGV 82
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE---FN--------FGQFEKTFDILVTQAgyygipkKIAEkrAEEYLEKL--GLWEKRNTQGRMLSGGMKRRLMIAR 149
Cdd:cd03251 81 VSQDvflFNdtvaeniaYGRPGATREEVEEAA-------RAAN--AHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSII----LTThyLEEAEmlcrRIAIIDRGVIKEDTSMKDFLN 225
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFViahrLST--IENAD----RIVVLEDGKIVERGTHEELLA 225
|
.
gi 491152796 226 Q 226
Cdd:cd03251 226 Q 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-170 |
6.37e-25 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 100.31 E-value: 6.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTY--KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGV 82
Cdd:cd03249 2 EFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFgqfektFDILVTQAGYYGIPKKIAE------KRAEEYLEKLGLWEKRNTQ----GRMLSGGMKRRLMIARAMM 152
Cdd:cd03249 82 VSQEPVL------FDGTIAENIRYGKPDATDEeveeaaKKANIHDFIMSLPDGYDTLvgerGSQLSGGQKQRIAIARALL 155
|
170
....*....|....*...
gi 491152796 153 HEPKLLILDEPTAGVDIE 170
Cdd:cd03249 156 RNPKILLLDEATSALDAE 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-226 |
8.82e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.14 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLG 81
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFgqFEKTF-DILVTQAgyygipKKIAEKRAEEYLEKLGLwEKRNTQ-----------GRMLSGGMKRRLMIAR 149
Cdd:PRK11160 418 VVSQRVHL--FSATLrDNLLLAA------PNASDEALIEVLQQVGL-EKLLEDdkglnawlgegGRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNeKGTSIILTTHYLEEAEMLcRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
8.97e-25 |
|
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: 99.43 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYK----NG--FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIF--GHNLDTH 72
Cdd:COG4778 1 MTTLLEVENLSKTFTlhlqGGkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 73 PSEAKQCLGVVPQEFNF-GQFEK------TFDIlVTQAGY-YGIPKKIAEKRAEEYLEKLGLWEKR-----NTqgrmLSG 139
Cdd:COG4778 81 QASPREILALRRRTIGYvSQFLRviprvsALDV-VAEPLLeRGVDREEARARARELLARLNLPERLwdlppAT----FSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 140 GMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-214 |
1.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.51 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 20 ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL---DTHPSEAKQCLGVVPQEFNFGQFEKTf 96
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQYPEYQLFEET- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 97 dilvtqagyygIPKKIA-------------EKRAEEYLEKLGL-WEKRNTQGRM-LSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK13637 101 -----------IEKDIAfgpinlglseeeiENRVKRAMNIVGLdYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-216 |
1.33e-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: 99.22 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 8 RDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP-SEAKQCLGVVPQE 86
Cdd:cd03254 6 ENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 ---FNFGQFE--KTFDILVTQAgyyGIPKKIAEKRAEEYLEKL--GLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:cd03254 86 tflFSGTIMEniRLGRPNATDE---EVIEAAKEAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMNEKGTSII----LTThyLEEAEmlcrRIAIIDRGVIKE 216
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIiahrLST--IKNAD----KILVLDDGKIIE 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-216 |
1.94e-24 |
|
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: 98.84 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGVV 83
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSlRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQE---FN--------FGQFEKTFDILVTQAGYYGIPKKIaEKRAEEYLEKLGlwEKrntqGRMLSGGMKRRLMIARAMM 152
Cdd:cd03253 81 PQDtvlFNdtigynirYGRPDATDEEVIEAAKAAQIHDKI-MRFPDGYDTIVG--ER----GLKLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILtTHYLEEAeMLCRRIAIIDRGVIKE 216
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVI-AHRLSTI-VNADKIIVLKDGRIVE 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-226 |
2.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGH--NLDTHPSEAKQCLGVVPQEFNFGQ---FE 93
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhiTPETGNKNLKKLRKKVSLVFQFPEaqlFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 94 KTF--DILVTQAGYyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRM-LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIE 170
Cdd:PRK13641 101 NTVlkDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 171 LRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDTSMKDFLNQ 226
Cdd:PRK13641 180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGkLIKHASPKEIFSDK 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
2.39e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.84 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfGHNLDthpseakqcLGV 82
Cdd:COG0488 314 KVLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFGQFEKT-FDILVTQAgyygipKKIAEKRAEEYLEKLGLWEKR-NTQGRMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:COG0488 383 FDQHQEELDPDKTvLDELRDGA------PGGTEQEVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMneKGTsIILTTH--YLeeAEMLCRRIAIIDRGVIKE 216
Cdd:COG0488 457 DEPTNHLDIETLEALEEALDDF--PGT-VLLVSHdrYF--LDRVATRILEFEDGGVRE 509
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-200 |
2.44e-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: 102.75 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEA---KQCl 80
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL-ADADADswrDQI- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQefNFGQFEKT--FDILVTQAGyygipkkIAEKRAEEYLEKLGLWEKRNT-----------QGRMLSGGMKRRLMI 147
Cdd:TIGR02857 399 AWVPQ--HPFLFAGTiaENIRLARPD-------ASDAEIREALERAGLDEFVAAlpqgldtpigeGGAGLSGGQAQRLAL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEkGTSIILTTHYLEEAE 200
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAA 521
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-228 |
2.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.85 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG----FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-----DTHPSE 75
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 76 AKQCLGVVPQEFNFGQFEKTF--DILVTQAGyYGIPKKIAEKRAEEYLEKLGLweKRNTQGR---MLSGGMKRRLMIARA 150
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVerEIIFGPKN-FKMNLDEVKNYAHRLLMDLGF--SRDVMSQspfQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 151 MMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLN 228
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
5-216 |
4.14e-24 |
|
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: 98.72 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGF--------QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSE 75
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 76 AK---QCLGVVPQEfNFGQF--EKTFDILVTQA--GYYGIPKKIAEKRAEEYLEKLGL-WEKRNTQGRMLSGGMKRRLMI 147
Cdd:TIGR02769 83 RRafrRDVQLVFQD-SPSAVnpRMTVRQIIGEPlrHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-229 |
4.59e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.06 E-value: 4.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTK-----KTSGSVEIFGHNLDTHP-SEAK- 77
Cdd:PRK14247 4 IEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDvIELRr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 --QCLGVVPQEF-NFGQFEKTfdILVTQAGYYGIPKKIAEKRAEEYLEKLGLWE----KRNTQGRMLSGGMKRRLMIARA 150
Cdd:PRK14247 83 rvQMVFQIPNPIpNLSIFENV--ALGLKLNRLVKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 151 MMHEPKLLILDEPTAGVDIELRRSMWEFLTEMnEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKD-FLNQLNE 229
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREvFTNPRHE 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-194 |
1.95e-23 |
|
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: 94.93 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG-----FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTK--KTSGSVEIFGHNLdtHPSEAK 77
Cdd:cd03213 4 LSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPL--DKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQEfnfgqfektfDILvtqagyygipkkIAEKRAEEYLE---KLglwekrntqgRMLSGGMKRRLMIARAMMHE 154
Cdd:cd03213 82 KIIGYVPQD----------DIL------------HPTLTVRETLMfaaKL----------RGLSGGERKRVSIALELVSN 129
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491152796 155 PKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
3-217 |
2.47e-23 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 95.35 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAKQCL 80
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQE---FnFGQFEktfDILVTQAGYygipkkIAEKRAEEYLEKLGLWEKRNTQ-----------GRMLSGGMKRRLM 146
Cdd:cd03245 81 GYVPQDvtlF-YGTLR---DNITLGAPL------ADDERILRAAELAGVTDFVNKHpngldlqigerGRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEkGTSIILTTH---YLEeaemLCRRIAIIDRGVIKED 217
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHrpsLLD----LVDRIIVMDSGRIVAD 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-226 |
2.68e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.61 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 16 NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVPQEF-NFGQFEK 94
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIkNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 95 TFDIlVTQAGYY------------------GIPKKIAEKRAEEYLEKLGLWE---KRNTQGrmLSGGMKRRLMIARAMMH 153
Cdd:PRK13631 117 RVSM-VFQFPEYqlfkdtiekdimfgpvalGVKKSEAKKLAKFYLNKMGLDDsylERSPFG--LSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDTSMKDFLNQ 226
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGkILKTGTPYEIFTDQ 267
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-199 |
5.70e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAkqclGVV 83
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 491152796 164 TAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEA 199
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEA 192
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-216 |
7.44e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 96.69 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEAKqcLGVVPQEFNFGQFEKTFD 97
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSrLHARDRK--VGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 98 ILVtqagyYGI---PKK------IAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:PRK10851 94 NIA-----FGLtvlPRRerpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 169 IELRRSMWEFLTEMNE--KGTSIILtTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK10851 169 AQVRKELRRWLRQLHEelKFTSVFV-THDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-217 |
7.45e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.13 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGsvEIFGHNldTHPSEAKQCLGVVP 84
Cdd:PRK11247 13 LLLNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG--ELLAGT--APLAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFD-ILVTQAGYYgipkkiaEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:PRK11247 88 QDARLLPWKKVIDnVGLGLKGQW-------RDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 164 TAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-214 |
8.62e-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: 93.71 E-value: 8.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 26 LTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAKQCLGVVPQEFN-FGQFEktfdiLVTQAG 104
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNlFAHLT-----VEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 105 YYGIP----KKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLT 180
Cdd:cd03298 93 LGLSPglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 491152796 181 EMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:cd03298 173 DLHaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-212 |
9.93e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 91.74 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVeifghnldTHPSEAKqcLGVVP 84
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------TWGSTVK--IGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QefnfgqfektfdilvtqagyygipkkiaekraeeyleklglwekrntqgrmLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 165 AGVDIELRRSMWEFLTemNEKGTsIILTTH--YLEEAemLCRRIAIIDRG 212
Cdd:cd03221 99 NHLDLESIEALEEALK--EYPGT-VILVSHdrYFLDQ--VATKIIELEDG 143
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-222 |
1.09e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.93 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD--THPSEAKQ 78
Cdd:PRK09700 2 ATPYISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 CLGVVPQEFNfgqfekTFDILVTQAGYY----------GIPK---KIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRL 145
Cdd:PRK09700 81 GIGIIYQELS------VIDELTVLENLYigrhltkkvcGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGV-----IKEDTSM 220
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVSN 234
|
..
gi 491152796 221 KD 222
Cdd:PRK09700 235 DD 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-233 |
1.70e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 14 YKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTK------KTSGSVEIFGHNL-DTHPSEAKQCLGVVPQE 86
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 FNFGQFEKTFDILVTQAGYYGIP-KKIAEKRAEEYLEKLGLW----EKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMnEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFL----NQLNEESFI 233
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFtspkNELTEKYVI 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-218 |
1.75e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.30 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAK-----QCLGVVPQEFNFGQFEKT 95
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 96 FDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491152796 176 WEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDrGVIKEDT 218
Cdd:PRK10584 186 ADLLFSLNrEHGTTLILVTHDLQLAARCDRRLRLVN-GQLQEEA 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-241 |
1.76e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.28 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGhnLDT-HPS---EAKQCLGV 82
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTgDFSklqGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQ--EFNFGQFEKTFDILVTQAGYYGIPKKIaEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEI-RKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMlCRRIAIIDRGVIKEDTSMKDFLNQLNEESFIFDLAAPI 240
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLI 239
|
.
gi 491152796 241 E 241
Cdd:PRK13644 240 E 240
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-223 |
2.10e-22 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 95.57 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTiSIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGV 82
Cdd:NF000106 12 NAVEVRGLVKHFGE-VKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG* 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 -----VPQEFNFGQFEKTFDIlvtqAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:NF000106 90 hrpvr*GRRESFSGRENLYMI----GR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDF 223
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-200 |
2.33e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.50 E-value: 2.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD--THPSEAKQCLG 81
Cdd:NF033858 1 VARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdaRHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQ----------------EFnFGQFektfdilvtqagyYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRL 145
Cdd:NF033858 80 YMPQglgknlyptlsvfenlDF-FGRL-------------FGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK--GTSIILTTHYLEEAE 200
Cdd:NF033858 146 GLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAE 202
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-241 |
3.96e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 93.52 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP-SEAKQCLG 81
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENlKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQ-------------EFNFGQFEKTFDilvtqagyygiPKKIAEKrAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIA 148
Cdd:PRK13632 87 IIFQnpdnqfigatvedDIAFGLENKKVP-----------PKKMKDI-IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGT-SIILTTHYLEEAeMLCRRIAIIDRGVI------KEDTSMK 221
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEA-ILADKVIVFSEGKLiaqgkpKEILNNK 233
|
250 260
....*....|....*....|.
gi 491152796 222 DFLNQLNEES-FIFDLAAPIE 241
Cdd:PRK13632 234 EILEKAKIDSpFIYKLSKKLK 254
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-214 |
4.29e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.29 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFG---HNLDThpSEAKQCLG 81
Cdd:PRK09536 4 IDVSDLSVEF-GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvEALSA--RAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQE----FNFgQFEKTFDILVT-QAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK09536 81 SVPQDtslsFEF-DVRQVVEMGRTpHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 157 LLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-286 |
5.23e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.40 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAKQCLGV 82
Cdd:PRK11432 5 NFVVLKNITKRFGSN-TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFN-FGQFEktfdiLVTQAGY----YGIPKKIAEKRAEEYLE--KLGLWEKRNTQgrMLSGGMKRRLMIARAMMHEP 155
Cdd:PRK11432 83 VFQSYAlFPHMS-----LGENVGYglkmLGVPKEERKQRVKEALElvDLAGFEDRYVD--QISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 156 KLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKD--------FLNQ 226
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQElyrqpasrFMAS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 227 LNEESFIFDlaAPIEPLHVDIIGVRFNLIDPVTLEVTMD--------KAHTLNQlfQLMEAQGIQVRS 286
Cdd:PRK11432 236 FMGDANIFP--ATLSGDYVDIYGYRLPRPAAFAFNLPDGectvgvrpEAITLSE--QGEESQRCTIKH 299
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-224 |
6.85e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.83 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG--------FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA 76
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 KqclgvvpqefnfgqfeKTF--DI-LVTQAGYYGI-PKK-----IAE--------------KRAEEYLEKLGL----WEK 129
Cdd:PRK10419 84 R----------------KAFrrDIqMVFQDSISAVnPRKtvreiIREplrhllsldkaerlARASEMLRAVDLddsvLDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 130 RNTQgrmLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAI 208
Cdd:PRK10419 148 RPPQ---LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMV 224
|
250
....*....|....*.
gi 491152796 209 IDRGVIKEDTSMKDFL 224
Cdd:PRK10419 225 MDNGQIVETQPVGDKL 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-231 |
8.09e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.15 E-value: 8.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDA-LTLRDLSkTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSL-----TKKTSGSVEIFGHNL---DT 71
Cdd:PRK14239 1 MTEPiLQVSDLS-VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIyspRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 72 HPSEAKQCLGVVPQEFNfgqfekTFDILVTQAGYYGI------PKKIAEKRAEEYLEKLGLWEKrnTQGRM------LSG 139
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPN------PFPMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGASIWDE--VKDRLhdsalgLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 140 GMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTsIILTTHYLEEAEMLCRRIAIIDRGVIKEDTS 219
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
250
....*....|...
gi 491152796 220 MKD-FLNQLNEES 231
Cdd:PRK14239 231 TKQmFMNPKHKET 243
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
10-194 |
1.15e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.09 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 10 LSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA----KQCLGVVPQ 85
Cdd:PRK10908 7 VSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQIGMIFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 EFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:PRK10908 87 DHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
|
170 180
....*....|....*....|....*....
gi 491152796 166 GVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:PRK10908 167 NLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-214 |
1.76e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTykngfQALKGINLTVPEGE---FYALLGpngAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEA-KQ 78
Cdd:COG1129 256 VLEVEGLSVG-----GVVRDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAiRA 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 CLGVVPQE-------------FNFgqfekTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLweK---RNTQGRMLSGGMK 142
Cdd:COG1129 328 GIAYVPEDrkgeglvldlsirENI-----TLASLDRLSRGGLLDRRRERALAEEYIKRLRI--KtpsPEQPVGNLSGGNQ 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 143 RRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG1129 401 QKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
8-214 |
2.06e-21 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 90.61 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 8 RDLSKTYKN--GFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE-AKQCLGVVP 84
Cdd:cd03248 15 QNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEfnfgqfEKTFDILVTQAGYYGIPKKIAEK--------RAEEYLEKL--GLWEKRNTQGRMLSGGMKRRLMIARAMMHE 154
Cdd:cd03248 95 QE------PVLFARSLQDNIAYGLQSCSFECvkeaaqkaHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 155 PKLLILDEPTAGVDIELRRSMWEFLTEMNEKgTSIILTTHYLEEAEMlCRRIAIIDRGVI 214
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-211 |
2.59e-21 |
|
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: 93.98 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDA--LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKS-TTISIISSL---TKKTSGSVEIFGHNLdT 71
Cdd:COG4172 1 MMSMplLSVEDLSVAFGQGggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLpdpAAHPSGSILFDGQDL-L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 72 HPSEAKQC------LGVVPQE--------FNFGQfektfdilvtQAG-----YYGIPKKIAEKRAEEYLEKLGLwekRNT 132
Cdd:COG4172 80 GLSERELRrirgnrIAMIFQEpmtslnplHTIGK----------QIAevlrlHRGLSGAAARARALELLERVGI---PDP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 133 QGRM------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEeaemLCRR 205
Cdd:COG4172 147 ERRLdayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLG----VVRR 222
|
....*.
gi 491152796 206 IAiiDR 211
Cdd:COG4172 223 FA--DR 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-214 |
2.65e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.79 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSeAKQCLGVVPQ 85
Cdd:PRK11000 5 TLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP-AERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 EFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 166 GVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-216 |
3.03e-21 |
|
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: 89.86 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 8 RDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAKQCLGVVPQ 85
Cdd:cd03244 6 KNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 E-FNF-GQFEKTFDILvtqaGYYgipkkiAEKRAEEYLEKLGLWEKRNTQ-----------GRMLSGGMKRRLMIARAMM 152
Cdd:cd03244 86 DpVLFsGTIRSNLDPF----GEY------SDEELWQALERVGLKEFVESLpggldtvveegGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFL-TEMneKGTSIILTTHYLeEAEMLCRRIAIIDRGVIKE 216
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIrEAF--KDCTVLTIAHRL-DTIIDSDRILVLDKGRVVE 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
5-226 |
3.34e-21 |
|
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: 94.04 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVV 83
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQE-FNF----------GQFEKTFDILVTQAgyygipKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:TIGR01193 554 PQEpYIFsgsilenlllGAKENVSQDEIWAA------CEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKgtSIILTTHYLEEAEMlCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-194 |
1.09e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE--AKQcLGVV 83
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelAKR-LAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQE--FN----------FGQFEktfdilvtqagyY--GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIAR 149
Cdd:COG4604 81 RQEnhINsrltvrelvaFGRFP------------YskGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTH 194
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-214 |
1.49e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 90.29 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAkqclgv 82
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElEPADR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 vpqefnfgqfektfDI-LVTQ--AGY----------YG-----IPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRR 144
Cdd:PRK11650 77 --------------DIaMVFQnyALYphmsvrenmaYGlkirgMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 145 LMIARAMMHEPKLLILDEPTAGVDIELRRSM-WEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLRVQMrLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
5-199 |
2.08e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.69 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSL-----TKKTSGSVEIFGHNL---DTHPSEA 76
Cdd:PRK14243 11 LRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipGFRVEGKVTFHGKNLyapDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 KQCLGVVPQEFNfgQFEKT-FDILVTQA---GYYGIPKKIAEKRaeeyLEKLGLWE----KRNTQGRMLSGGMKRRLMIA 148
Cdd:PRK14243 90 RRRIGMVFQKPN--PFPKSiYDNIAYGArinGYKGDMDELVERS----LRQAALWDevkdKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTsIILTTHYLEEA 199
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQA 213
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-226 |
3.93e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 90.46 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY--KNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD--THPSEAKQCl 80
Cdd:PRK11176 342 IEFRNVTFTYpgKEV-PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLASLRNQV- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQefNFGQFEKTF--DILVTQAGYYGIPKKIAEKR---AEEYLEKL--GLWEKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:PRK11176 420 ALVSQ--NVHLFNDTIanNIAYARTEQYSREQIEEAARmayAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILtTHYL---EEAEMlcrrIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLstiEKADE----ILVVEDGEIVERGTHAELLAQ 568
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-226 |
4.33e-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: 90.55 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYK-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGV 82
Cdd:TIGR02203 331 VEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFgqfektFDILVTQAGYYGIPKKIAEKRAEEYLEK-----------LGLWEKRNTQGRMLSGGMKRRLMIARAM 151
Cdd:TIGR02203 411 VSQDVVL------FNDTIANNIAYGRTEQADRAEIERALAAayaqdfvdklpLGLDTPIGENGVLLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSII----LTThyLEEAEmlcrRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLViahrLST--IEKAD----RIVVMDDGRIVERGTHNELLAR 557
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
9-215 |
9.48e-20 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 88.25 E-value: 9.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 9 DLSKTYknGFQALKgINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDThpSEAKQCL-------G 81
Cdd:TIGR02142 4 RFSKRL--GDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFD--SRKGIFLppekrriG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEfnfgqfEKTFDIL-VTQAGYYGIPKKIAEKRA---EEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:TIGR02142 79 YVFQE------ARLFPHLsVRGNLRYGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIK 215
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHaEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-224 |
1.02e-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: 86.00 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYK-NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAKQCLGV 82
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE---FNFGQFEktfDILVTQAGYyGIPKKIAEKR---AEEYLEKLGlwEKRNT----QGRMLSGGMKRRLMIARAMM 152
Cdd:cd03252 81 VLQEnvlFNRSIRD---NIALADPGM-SMERVIEAAKlagAHDFISELP--EGYDTivgeQGAGLSGGQRQRIAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMwefLTEMNE--KGTSIILTTHYLeEAEMLCRRIAIIDRGVIKEDTSMKDFL 224
Cdd:cd03252 155 HNPRILIFDEATSALDYESEHAI---MRNMHDicAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-194 |
1.15e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 89.34 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKK---TSGSVEIFGHnldthPSEAKQ----CLGVVPQEFNFGQFe 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM-----PIDAKEmraiSAYVQQDDLFIPTL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 94 KTFDILVTQAGYY---GIPKKIAEKRAEEYLEKLGLWEKRNT----QGRM--LSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:TIGR00955 115 TVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTrigvPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190
....*....|....*....|....*....|
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-229 |
1.34e-19 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 85.50 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 23 GINLTVPEGEFYALLGPNGAGKSTT----ISIISSLTKKTSGSVEIFGHNLDthPSEAKQ-CLGVVPQE--------FNF 89
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTclaiLGLLPPGLTQTSGEILLDGRPLL--PLSIRGrHIATIMQNprtafnplFTM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 90 G-QFEKTFDILvtqagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGR---MLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:TIGR02770 82 GnHAIETLRSL-------GKLSKQARALILEALEAVGLPDPEEVLKKypfQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 166 GVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDTSMKDFLNQLNE 229
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLfGTGILLITHDLGVVARIADEVAVMDDGrIVERGTVKEIFYNPKHE 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-216 |
1.87e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKN--GFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD--THPSEA 76
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqyDHHYLH 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 KQCLGVvpqefnfGQFEKTFDILVTQAGYYGIPKKIAEK--------RAEEYLEKL--GLWEKRNTQGRMLSGGMKRRLM 146
Cdd:TIGR00958 555 RQVALV-------GQEPVLFSGSVRENIAYGLTDTPDEEimaaakaaNAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIA 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEfltEMNEKGTSIILTTHYLEEAEMlCRRIAIIDRGVIKE 216
Cdd:TIGR00958 628 IARALVRKPRVLILDEATSALDAECEQLLQE---SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-214 |
2.05e-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: 88.32 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTY----KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEI-FGHN-LD-THP-- 73
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEwVDmTKPgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 74 ---SEAKQCLGVVPQEFNFGQFEKTFDILvTQAGYYGIPKKIAEKRAEEYLEKLGLWEK--RNTQGRM---LSGGMKRRL 145
Cdd:TIGR03269 358 dgrGRAKRYIGILHQEYDLYPHRTVLDNL-TEAIGLELPDELARMKAVITLKMVGFDEEkaEEILDKYpdeLSEGERHRV 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 146 MIARAMMHEPKLLILDEPTAGVD----IELRRSMWEFLTEMNEkgtSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-217 |
2.65e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGF----QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPSEAK--Q 78
Cdd:COG1101 2 LELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 CLGVVPQ------------EFNF------GQFeKTFDILVTQagyygipKKIAEKRaeEYLEKLGL-WEKR-NTQGRMLS 138
Cdd:COG1101 81 YIGRVFQdpmmgtapsmtiEENLalayrrGKR-RGLRRGLTK-------KRRELFR--ELLATLGLgLENRlDTKVGLLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 139 GGMKRRLMIARAMMHEPKLLILDEPTAGVDIelRRSmwEFLTEM-----NEKGTSIILTTHYLEEAEMLCRRIAIIDRGV 213
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLELtekivEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
....
gi 491152796 214 IKED 217
Cdd:COG1101 227 IILD 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-216 |
3.18e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 3.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALT-LRDLSKTYKNG-FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS-EAK 77
Cdd:PRK10253 1 MTESVArLRGEQLTLGYGkYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQEFNfGQFEKTFDILVTQAGYYGIP-----KKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:PRK10253 81 RRIGLLAQNAT-TPGDITVQELVARGRYPHQPlftrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAemlCRR----IAIIDRGVIKE 216
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQA---CRYashlIALREGKIVAQ 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
21-232 |
3.73e-19 |
|
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: 84.62 E-value: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISS--LTKKTSGSVEIFGHNLDTHPSEAKQCLGVV-----PQEF---NFG 90
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERARAGLFlafqyPEEIpgvSNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QFEKTFDILVTQAGYYGiPKKIAE--KRAEEYLEKLGLWE---KRN-TQGrmLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:TIGR01978 96 EFLRSALNARRSARGEE-PLDLLDfeKLLKEKLALLDMDEeflNRSvNEG--FSGGEKKRNEILQMALLEPKLAILDEID 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLC-RRIAIIDRGVIKEDTSMkDFLNQLNEESF 232
Cdd:TIGR01978 173 SGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDV-ELAKELEAKGY 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-200 |
4.66e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTIS-IISSLTK--KTSGSVEIFGHNLDTHPSEAKQcLG 81
Cdd:COG4136 2 LSLENLTITL-GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPafSASGEVLLNGRRLTALPAEQRR-IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQE------FNFGQfektfDILvtqagyYGIPKKI--AEKRA--EEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAM 151
Cdd:COG4136 80 ILFQDdllfphLSVGE-----NLA------FALPPTIgrAQRRArvEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEF-LTEMNEKGTSIILTTHYLEEAE 200
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDAP 198
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-216 |
4.70e-19 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 84.50 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP----SEAKQCL 80
Cdd:TIGR02323 4 LQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELElyqlSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 ------GVVPQE------------FNFGQfektfDILVTQAGYYGipkKIAEKrAEEYLEKLGLWEKR-NTQGRMLSGGM 141
Cdd:TIGR02323 83 lmrtewGFVHQNprdglrmrvsagANIGE-----RLMAIGARHYG---NIRAT-AQDWLEEVEIDPTRiDDLPRAFSGGM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLvRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-216 |
4.85e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.07 E-value: 4.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS-EAKQCLGV 82
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNfGQFEKTF--DILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13635 86 VFQNPD-NQFVGATvqDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMNEKGT-SIILTTHYLEEAEMlCRRIAIIDRGVIKE 216
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-216 |
1.07e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGV 82
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFnfGQFEKTF--DILVTQAGYYGIPKKIAEKRAE--EYLEK--LGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK13657 414 VFQDA--GLFNRSIedNIRVGRPDATDEEMRAAAERAQahDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 157 LLILDEPTAGVDIELRRSMWEFLTE-MNEKGTSII---LTThyLEEAEmlcrRIAIIDRGVIKE 216
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDElMKGRTTFIIahrLST--VRNAD----RILVFDNGRVVE 549
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
5-218 |
1.08e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSE--AKQCLGV 82
Cdd:PRK11614 6 LSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFgqFEK-TFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK11614 85 VPEGRRV--FSRmTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDT 218
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGhVVLEDT 220
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-212 |
1.46e-18 |
|
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: 82.13 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQ----ALKGINLTVPEGEFYALLGPNGAGKSttiSIISSL---TKKTSGSVEIFGHnldthpseak 77
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKS---SLLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 qcLGVVPQE---FN--------FGqfeKTFDilvtqagyygipkkiaEKRAEEYLEK------LGLWEKR-NTQ----GR 135
Cdd:cd03250 68 --IAYVSQEpwiQNgtirenilFG---KPFD----------------EERYEKVIKAcalepdLEILPDGdLTEigekGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 136 MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWE--FLTEMNEKGTsIILTTH---YLEEAEmlcrRIAIID 210
Cdd:cd03250 127 NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKT-RILVTHqlqLLPHAD----QIVVLD 201
|
..
gi 491152796 211 RG 212
Cdd:cd03250 202 NG 203
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-242 |
2.27e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVV 83
Cdd:PRK11231 3 LRTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQefnfgQFEKTFDILVTQAGYYGIPKKIA---------EKRAEEYLEKLG---LWEKRNTQgrmLSGGMKRRLMIARAM 151
Cdd:PRK11231 82 PQ-----HHLTPEGITVRELVAYGRSPWLSlwgrlsaedNARVNQAMEQTRinhLADRRLTD---LSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDTSMKDFLNQLNEE 230
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGhVMAQGTPEEVMTPGLLRT 233
|
250
....*....|..
gi 491152796 231 sfIFDLAAPIEP 242
Cdd:PRK11231 234 --VFDVEAEIHP 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-214 |
2.53e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.08 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGV- 82
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVa 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 -VPQE-------------FNFgqfektfdILvtqaGYYGIP---------KKIAEKRAEEYLEKLGLwekR----NTQGR 135
Cdd:COG3845 337 yIPEDrlgrglvpdmsvaENL--------IL----GRYRRPpfsrggfldRKAIRAFAEELIEEFDV---RtpgpDTPAR 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 136 MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG3845 402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-203 |
2.81e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEifghnldthpSEAKQCL 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEFNFgqfEKTFDILVTQAgyygIPKKIAEKRAE--EYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:PRK09544 70 GYVPQKLYL---DTTLPLTVNRF----LRLRPGTKKEDilPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 159 ILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYL-----EEAEMLC 203
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLMVSHDLhlvmaKTDEVLC 193
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-208 |
2.89e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEA-KQ 78
Cdd:PRK11288 1 SSPYLSFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAAlAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 CLGVVPQEFNF------------GQFEKTFDIlvtqagyygIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLM 146
Cdd:PRK11288 80 GVAIIYQELHLvpemtvaenlylGQLPHKGGI---------VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAI 208
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-229 |
6.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.09 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGFQ--ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAK 77
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLtEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQ-------------EFNFGQFEKtfdilvtqagyyGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRR 144
Cdd:PRK13650 81 HKIGMVFQnpdnqfvgatvedDVAFGLENK------------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 145 LMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEmLCRRIAIIDRGVIKEDTSMKDF 223
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
....*.
gi 491152796 224 LNQLNE 229
Cdd:PRK13650 228 FSRGND 233
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
5-195 |
1.11e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 80.84 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISS--LTKKTSGSVEIFGHNLDTHPSEAKQCLGV 82
Cdd:CHL00131 8 LEIKNLHASV-NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 vpqefnFGQFEKTFDIL-VTQAG-----------YYGIPKK--------IAEKraeeyLEKLGLWEK---RN-TQGrmLS 138
Cdd:CHL00131 87 ------FLAFQYPIEIPgVSNADflrlaynskrkFQGLPELdplefleiINEK-----LKLVGMDPSflsRNvNEG--FS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 139 GGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHY 195
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-194 |
1.24e-17 |
|
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: 83.26 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGVVPQE---F------NFG 90
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElGRHIGYLPQDvelFdgtiaeNIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QFEKTFDILVTQAGyygipkKIAekRAEEYLEKL--GLwekrNTQ----GRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:COG4618 428 RFGDADPEKVVAAA------KLA--GVHEMILRLpdGY----DTRigegGARLSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190
....*....|....*....|....*....|
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITH 525
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-212 |
1.41e-17 |
|
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: 82.07 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 24 INLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFG---------HNLDTHpseaKQCLGVVPQE---F---- 87
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargIFLPPH----RRRIGYVFQEarlFphls 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 88 ---NfgqfektfdiLvtQAGYYGIPKKIAEKRAEEYLEKLG---LWEKRNTQgrmLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:COG4148 94 vrgN----------L--LYGRKRAPRAERRISFDEVVELLGighLLDRRPAT---LSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-216 |
2.87e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.58 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP----SEA 76
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 KQCL------GVVPQE------------FNFGQfektfDILVTQAGYYGipkKIAEKrAEEYLEKLGLWEKR-NTQGRML 137
Cdd:PRK11701 82 ERRRllrtewGFVHQHprdglrmqvsagGNIGE-----RLMAVGARHYG---DIRAT-AGDWLERVEIDAARiDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 138 SGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-233 |
3.46e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.86 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNgfQALKgINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNlDTHPSEAKQCLGVVP 84
Cdd:PRK10771 2 LKLTDITWLYHH--LPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFgqfektFDIL-VTQAGYYGI-P------------KKIAEKRA-EEYLEKLglwekrNTQgrmLSGGMKRRLMIAR 149
Cdd:PRK10771 78 QENNL------FSHLtVAQNIGLGLnPglklnaaqreklHAIARQMGiEDLLARL------PGQ---LSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLN 228
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA 222
|
....*
gi 491152796 229 EESFI 233
Cdd:PRK10771 223 SASAL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-223 |
3.98e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSL---TKKTSGSVEIFGHNLDTHPS-EAK 77
Cdd:PRK13640 4 NIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVwDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCLGVVPQEFNfGQF--EKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEP 155
Cdd:PRK13640 84 EKVGIVFQNPD-NQFvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 156 KLLILDEPTAGVDIELRRSMWEFLTE-MNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDF 223
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-216 |
4.56e-17 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 81.39 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLT--KKTSGSVeIFghnldtHPSEAKQCLGV 82
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IY------HVALCEKCGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFnFGQ----------------------------------FEKTFDIL------------VTQAGYYGipkKIAEKR 116
Cdd:TIGR03269 73 ERPSK-VGEpcpvcggtlepeevdfwnlsdklrrrirkriaimLQRTFALYgddtvldnvleaLEEIGYEG---KEAVGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 117 AEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTE-MNEKGTSIILTTHY 195
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHW 228
|
250 260
....*....|....*....|.
gi 491152796 196 LEEAEMLCRRIAIIDRGVIKE 216
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKE 249
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-225 |
5.38e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 20 ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL----DTHPSEAK-QCLGVVPQEFNFGQFEK 94
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisDAELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 95 TFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRS 174
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 175 MWEFLTEMNEKGT-SIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLN 225
Cdd:PRK10070 203 MQDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
5-202 |
9.14e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.22 E-value: 9.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSkTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEA------- 76
Cdd:PRK13539 3 LEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIdDPDVAEAchylghr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 ---KQCLGVVpqefnfgqfektfDILVTQAGYYGIpkkiAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:PRK13539 82 namKPALTVA-------------ENLEFWAAFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHY---LEEAEML 202
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-194 |
1.06e-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: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTyKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFG---HNLDTHPSEAKQCLG 81
Cdd:TIGR01189 1 LAARNLACS-RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFGQFEKTFDILVTQAGYygipkkiAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:TIGR01189 80 HLPGLKPELSALENLHFWAAIHGG-------AQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-209 |
1.51e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.83 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEI--------FGhnlDTHPSEA 76
Cdd:NF040905 2 LEMRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEIlfdgevcrFK---DIRDSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 K------QCLGVVPQ----EFNFgqfektfdiLVTQAGYYG-IPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRL 145
Cdd:NF040905 78 LgiviihQELALIPYlsiaENIF---------LGNERAKRGvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAII 209
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVL 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
5-168 |
1.80e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 78.62 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY--KNGF--------QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdTHPS 74
Cdd:COG4608 8 LEVRDLKKHFpvRGGLfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI-TGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 75 EAK-----QCLGVVpqefnfgqFEKTF----------DILVTQAGYYGI-PKKIAEKRAEEYLEKLGLweKRNTQGR--- 135
Cdd:COG4608 87 GRElrplrRRMQMV--------FQDPYaslnprmtvgDIIAEPLRIHGLaSKAERRERVAELLELVGL--RPEHADRyph 156
|
170 180 190
....*....|....*....|....*....|...
gi 491152796 136 MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-196 |
2.03e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.47 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTY--KNGF-------QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT 71
Cdd:PRK11308 2 QQPLLQAIDLKKHYpvKRGLfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 72 HPSEA----KQCLGVVPQefN-FGQF---EKTFDILvtqagyyGIPKKI------AEKR--AEEYLEKLGLweKRNTQGR 135
Cdd:PRK11308 82 ADPEAqkllRQKIQIVFQ--NpYGSLnprKKVGQIL-------EEPLLIntslsaAERRekALAMMAKVGL--RPEHYDR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 136 ---MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYL 196
Cdd:PRK11308 151 yphMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDL 215
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-194 |
4.18e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.70 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTYKNGFQALKGINLTVPEGEfyALL--GPNGAGKSTTISIISSLTKKTSGSVeifghnldTHPSEAKQCL 80
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 gvVPQefnfgqfeKTFDILVT--QAGYY-GIPKKIAEKRAEEYLEKLGL------------WEKRntqgrmLSGGMKRRL 145
Cdd:COG4178 431 --LPQ--------RPYLPLGTlrEALLYpATAEAFSDAELREALEAVGLghlaerldeeadWDQV------LSLGEQQRL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491152796 146 MIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMnEKGTSIILTTH 194
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE-LPGTTVISVGH 542
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
20-240 |
4.69e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 20 ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGsvEIFGHNLDTHP---SEAKQCLGVVPQ--EFNFGQFEK 94
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAITDdnfEKLRKHIGIVFQnpDNQFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 95 TFDI---LVTQAgyygIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:PRK13648 102 KYDVafgLENHA----VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 172 RRSMWEFLTEMN-EKGTSIILTTHYLEEAeMLCRRIAIIDRGVIKEDTSMKDFLNQLNEESFI-FDLAAPI 240
Cdd:PRK13648 178 RQNLLDLVRKVKsEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEELTRIgLDLPFPI 247
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-224 |
8.74e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.60 E-value: 8.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKT--YKNGF------QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP-SE 75
Cdd:PRK15112 5 LEVRNLSKTfrYRTGWfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDySY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 76 AKQCLGVVPQE----FN----FGQFEKTFDILVTQagyygIPKKIAEKRAEEYLEKLGLW-EKRNTQGRMLSGGMKRRLM 146
Cdd:PRK15112 85 RSQRIRMIFQDpstsLNprqrISQILDFPLRLNTD-----LEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 147 IARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFL 224
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-194 |
1.45e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.37 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 17 GFQA-----LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA--KQCLGVVPQEFNF 89
Cdd:PRK10247 14 GYLAgdakiLNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 90 GqfEKTFDILVtqagyygIPKKIAEKRAEE-----YLEKLGLWEKRNTQG-RMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:PRK10247 94 G--DTVYDNLI-------FPWQIRNQQPDPaifldDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|..
gi 491152796 164 TAGVDIELRRSMWEFLTEMN-EKGTSIILTTH 194
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVrEQNIAVLWVTH 196
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-212 |
1.58e-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: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGV 82
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQefnfgqfektfDILVTQAGYYG---IPKKIAEKRAEEYLEKL-----------GLWEKRNTQGRMLSGGMKRRLMIA 148
Cdd:PRK10790 420 VQQ-----------DPVVLADTFLAnvtLGRDISEEQVWQALETVqlaelarslpdGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKgTSIILTTHYLE---EAE--MLCRRIAIIDRG 212
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLStivEADtiLVLHRGQAVEQG 556
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-216 |
3.40e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.78 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY-KNGFqALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDT-HPSEAKQCLGV 82
Cdd:PRK10522 323 LELRNVTFAYqDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAeQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFgqfektFDILVTQAGyygipKKIAEKRAEEYLEKLGLWEKRNTQ-GRM----LSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK10522 402 VFTDFHL------FDQLLGPEG-----KPANPALVEKWLERLKMAHKLELEdGRIsnlkLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 158 LILDEPTAGVDIELRRSMW-EFLTEMNEKGTSIILTTH---YLEEAEmlcrRIAIIDRGVIKE 216
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYqVLLPLLQEMGKTIFAISHddhYFIHAD----RLLEMRNGQLSE 529
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-216 |
3.57e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.36 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS-EAKQCLGVVPQEFNfGQF--EKTFD 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwNLRRKIGMVFQNPD-NQFvgATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 98 ILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWE 177
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491152796 178 FLTEMNEKGTSIILT-THYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK13642 182 VIHEIKEKYQLTVLSiTHDLDEAASSDRILVMKAGEIIKE 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-206 |
4.11e-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: 72.53 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEAKQCL---------GVVPQEFNFg 90
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDfQRDSIARGLLylghapgikTTLSVLENL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QFEKTFDilvtqagyygipkkiAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDie 170
Cdd:cd03231 95 RFWHADH---------------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491152796 171 lRRSMWEFLTEMN---EKGTSIILTTHY-LEEAEMLCRRI 206
Cdd:cd03231 158 -KAGVARFAEAMAghcARGGMVVLTTHQdLGLSEAGAREL 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-196 |
7.40e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTkKTSGSVEIFGHNLDT-HPSEAKQCLGVVPQefnfgQFEKTFDIL 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQ-----QQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 100 VTQ--AGYY--GIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMH-------EPKLLILDEPTAGVD 168
Cdd:COG4138 86 VFQylALHQpaGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
170 180
....*....|....*....|....*...
gi 491152796 169 IELRRSMWEFLTEMNEKGTSIILTTHYL 196
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-214 |
7.86e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.70 E-value: 7.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKtykNGFqalKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVV- 83
Cdd:PRK15439 269 LTVEDLTG---EGF---RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVy 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 --------------PQEFNfgqfekTFDILVTQAGYYGIPKKIAeKRAEEYLEKLGL-WEKRNTQGRMLSGGMKRRLMIA 148
Cdd:PRK15439 343 lpedrqssglyldaPLAWN------VCALTHNRRGFWIKPAREN-AVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-217 |
1.29e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 17 GFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSG-----SVEIFGHNLDTHPS--EAKQCLGVVPQEFNF 89
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 90 GQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWE----KRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:PRK14271 113 FPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDavkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491152796 166 GVDIELRRSMWEFLTEMNEKGTsIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-212 |
1.35e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.09 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIF--GHNL---DTHPSEAK-- 77
Cdd:TIGR02633 2 LEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLkasNIRDTERAgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 ----QCLGVVPqefNFGQFEKTF--DILVTQAGYYGIPKKIaeKRAEEYLEKLGLWEKRNTQGRM-LSGGMKRRLMIARA 150
Cdd:TIGR02633 81 viihQELTLVP---ELSVAENIFlgNEITLPGGRMAYNAMY--LRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 151 MMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-233 |
1.66e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEAKQC 79
Cdd:PRK10762 1 MQALLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 80 -LGVVPQEFNF-GQFEKTFDIL-----VTQAGyyGIPKKIAEKRAEEYLEKLGLweKRNTQGRM--LSGGMKRRLMIARA 150
Cdd:PRK10762 80 gIGIIHQELNLiPQLTIAENIFlgrefVNRFG--RIDWKKMYAEADKLLARLNL--RFSSDKLVgeLSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 151 MMHEPKLLILDEPT-AGVDIElRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAII-DRGVIKEDTsmkdfLNQLN 228
Cdd:PRK10762 156 LSFESKVIIMDEPTdALTDTE-TESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFrDGQFIAERE-----VADLT 229
|
....*
gi 491152796 229 EESFI 233
Cdd:PRK10762 230 EDSLI 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-194 |
2.32e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS---EAKQCLG 81
Cdd:PRK13638 2 LATSDLWFRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQEFNFGQFEKTFDI-LVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLIL 160
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSdIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 491152796 161 DEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
5-212 |
2.48e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIF--GHNLDTH---PSEAK-- 77
Cdd:PRK13549 6 LEMKNITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfeGEELQASnirDTERAgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 ----QCLGVVPQ----EFNFGQFEktfdilVTQAGYYGIPKKIAekRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIAR 149
Cdd:PRK13549 85 aiihQELALVKElsvlENIFLGNE------ITPGGIMDYDAMYL--RAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-226 |
3.06e-14 |
|
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: 71.42 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQA-LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTkKTSGSVEIFGHNLDTHP-SEAKQCLGV 82
Cdd:cd03289 3 MTVKDLTAKYTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPlQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE-FNF-GQFEKTFDIlvtqagyYGIPK-----KIAEKRA-----EEYLEKLGLweKRNTQGRMLSGGMKRRLMIARA 150
Cdd:cd03289 82 IPQKvFIFsGTFRKNLDP-------YGKWSdeeiwKVAEEVGlksviEQFPGQLDF--VLVDGGCVLSHGHKQLMCLARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 151 MMHEPKLLILDEPTAGVD----IELRRSMWEFLTemnekGTSIILTTHYLeEAEMLCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDpityQVIRKTLKQAFA-----DCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
5-194 |
5.80e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.33 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNldthpseakqCLGVVP 84
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------DLLFLP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QE--FNFGQFEktfDILVtqagyYgiPkkiaekraeeyleklglWekrntqGRMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:cd03223 71 QRpyLPLGTLR---EQLI-----Y--P-----------------W------DDVLSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|..
gi 491152796 163 PTAGVDIELRRSMWEFLTEMnekGTSIILTTH 194
Cdd:cd03223 118 ATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-216 |
6.59e-14 |
|
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: 69.36 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGVVPQE---FNfGQFEK 94
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTIIPQDptlFS-GTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 95 TFDIlvtqagyYGipkkiaEKRAEEYLEKLGLWEKrntqGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIE---- 170
Cdd:cd03369 101 NLDP-------FD------EYSDEEIYGALRVSEG----GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAtdal 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491152796 171 LRRSMWEFLTemnekGTSIILTTHYLEEAeMLCRRIAIIDRGVIKE 216
Cdd:cd03369 164 IQKTIREEFT-----NSTILTIAHRLRTI-IDYDKILVMDAGEVKE 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-168 |
1.44e-13 |
|
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: 71.00 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVVPQE---FNfgqfek 94
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrDVTQASLRAAIGIVPQDtvlFN------ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 95 tfDILvtqaGY---YGIP----KKIAE--KRA--EEYLEklGLWEKRNTQ----GRMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:COG5265 446 --DTI----AYniaYGRPdaseEEVEAaaRAAqiHDFIE--SLPDGYDTRvgerGLKLSGGEKQRVAIARTLLKNPPILI 517
|
....*....
gi 491152796 160 LDEPTAGVD 168
Cdd:COG5265 518 FDEATSALD 526
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-226 |
1.53e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.93 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLS---KTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKK----------------TSGSVE-- 63
Cdd:COG4170 4 LDIRNLTieiDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrwngidlLKLSPRer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 64 --IFGHN-----------LDthPSE--AKQCLGVVPQEFNFGQFEKTFdilvtqagyygipkKIAEKRAEEYLEKLGLwe 128
Cdd:COG4170 84 rkIIGREiamifqepsscLD--PSAkiGDQLIEAIPSWTFKGKWWQRF--------------KWRKKRAIELLHRVGI-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 129 kRNTQGRM------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNE-KGTSIILTTHYLEEAEM 201
Cdd:COG4170 146 -KDHKDIMnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQ 224
|
250 260
....*....|....*....|....*
gi 491152796 202 LCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:COG4170 225 WADTITVLYCGQTVESGPTEQILKS 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-168 |
1.86e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.91 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTK-----KTSGSVEIFGHNL---DTHPSE 75
Cdd:PRK14258 7 AIKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyerRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 76 AKQCLGVVPQEFNFgqfektFDILVTQAGYYGI------PKKIAEKRAEEYLEKLGLWE----KRNTQGRMLSGGMKRRL 145
Cdd:PRK14258 86 LRRQVSMVHPKPNL------FPMSVYDNVAYGVkivgwrPKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRL 159
|
170 180
....*....|....*....|...
gi 491152796 146 MIARAMMHEPKLLILDEPTAGVD 168
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLD 182
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-206 |
1.87e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 69.75 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYK--NG-FQALKGINLTVPEGEFYALLGPNGAGKS-TTISIISSLTK--KTSGSVEIFGHNLDTHPSEAkq 78
Cdd:PRK09473 13 LDVKDLRVTFStpDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNLPEKE-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 cLGVVPQEfnfgQFEKTFDILVTQAGYY---------------GIPKKIAEKRAEEYLEKLGLWEKRNtqgRM------L 137
Cdd:PRK09473 91 -LNKLRAE----QISMIFQDPMTSLNPYmrvgeqlmevlmlhkGMSKAEAFEESVRMLDAVKMPEARK---RMkmypheF 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 138 SGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRI 206
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKV 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-226 |
1.90e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.27 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 2 TDALTLRDLSKTYKNG----FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAK 77
Cdd:PRK13645 4 SKDIILDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QC------LGVVPQEFNFGQFEKTF--DILVTQAgYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRM-LSGGMKRRLMIA 148
Cdd:PRK13645 84 EVkrlrkeIGLVFQFPEYQLFQETIekDIAFGPV-NLGENKQEAYKKVPELLKLVQLPEDYVKRSPFeLSGGQKRRVALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRG-VIKEDTSMKDFLNQ 226
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGkVISIGSPFEIFSNQ 242
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-196 |
2.34e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.39 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY---KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLT----KKTSGSVEIFGHNLDTHPSEAK 77
Cdd:PRK11022 4 LNVDKLSVHFgdeSAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 QCL-----GVVPQE--------FNFGqfektFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWE---KRNTQGRMLSGGM 141
Cdd:PRK11022 84 RNLvgaevAMIFQDpmtslnpcYTVG-----FQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 142 KRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYL 196
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDL 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-215 |
2.37e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.52 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 24 INLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdtHPSEAKQCL-------GVVPQE---------- 86
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEKGICLppekrriGYVFQDarlfphykvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 ---------FNFGQFEKTFDILvtqagyyGIpkkiaekraEEYLEKLGLwekrntqgrMLSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK11144 95 gnlrygmakSMVAQFDKIVALL-------GI---------EPLLDRYPG---------SLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 158 LILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIK 215
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-212 |
3.68e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKS-TTISIISSLTKK----TSGSVEIFGHNLdTHPSEA 76
Cdd:PRK15134 6 LAIENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESL-LHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 K------QCLGVVPQEfnfgqfektfdILVTQAGYYGIPKKIAE------------KRAE--EYLEKLGLwekRNTQGRM 136
Cdd:PRK15134 85 TlrgvrgNKIAMIFQE-----------PMVSLNPLHTLEKQLYEvlslhrgmrreaARGEilNCLDRVGI---RQAAKRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 137 ------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEM-NEKGTSIILTTHYLEEAEMLCRRIAII 209
Cdd:PRK15134 151 tdyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVM 230
|
...
gi 491152796 210 DRG 212
Cdd:PRK15134 231 QNG 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-194 |
7.09e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL-------GVVPqefNFGQFE 93
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLcfvghrsGINP---YLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 94 KTFDILVTQAGYYGIPKKIAEKRAEEYLE-KLGLwekrntqgrmLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDielR 172
Cdd:PRK13540 94 NCLYDIHFSPGAVGITELCRLFSLEHLIDyPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---E 160
|
170 180
....*....|....*....|....*
gi 491152796 173 RSMWEFLTEMNE---KGTSIILTTH 194
Cdd:PRK13540 161 LSLLTIITKIQEhraKGGAVLLTSH 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-214 |
8.56e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 68.72 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 8 RDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTsGSVEIFGHNL-DTHPSEAKQCLGVV--- 83
Cdd:PRK11174 353 EDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELrELDPESWRKHLSWVgqn 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFN--------FGQFEKTfDILVTQAgyygipkkIAEKRAEEYLEKL--GLWEKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:PRK11174 432 PQLPHgtlrdnvlLGNPDAS-DEQLQQA--------LENAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQ 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEmNEKGTSIILTTHYLEEAEMlCRRIAIIDRGVI 214
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-216 |
9.21e-13 |
|
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: 68.56 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTY----------KNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKkTSGSVEIFGHNLDTHPS 74
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 75 EA----KQCLGVVPQE--------FNFGQfektfdI----LVTQAGyyGIPKKIAEKRAEEYLEKLGLweKRNTQGRM-- 136
Cdd:COG4172 355 RAlrplRRRMQVVFQDpfgslsprMTVGQ------IiaegLRVHGP--GLSAAERRARVAEALEEVGL--DPAARHRYph 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 137 -LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:COG4172 425 eFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
..
gi 491152796 215 KE 216
Cdd:COG4172 505 VE 506
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-216 |
9.22e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 9.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 20 ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVPQeFNFGQFEKTFDIL 99
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQ-FIFQDPYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 100 VTqAGY--------YGI-PKKIAEKRAEEYLEKLGLW-EKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK10261 418 QT-VGDsimeplrvHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491152796 170 ELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK10261 497 SIRGQIINLLLDLQrDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-199 |
1.39e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIIS-SLTKKTSGSVEIFGHNLDTHPS--EAKQCLGVVPQEFNFGQFEKTFD 97
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgDHPQGYSNDLTLFGRRRGSGETiwDIKKHIGYVSSSLHLDYRVSTSV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 98 ILVTQAGYY---GIPKKIAE---KRAEEYLEKLGLwEKR--NTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK10938 356 RNVILSGFFdsiGIYQAVSDrqqKLAQQWLDILGI-DKRtaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
170 180 190
....*....|....*....|....*....|.
gi 491152796 170 ELRRSMWEFLTEMNEKG-TSIILTTHYLEEA 199
Cdd:PRK10938 435 LNRQLVRRFVDVLISEGeTQLLFVSHHAEDA 465
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-226 |
1.68e-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: 68.01 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQA-LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTkKTSGSVEIFGHNLDTHPSEA-KQCLGV 82
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQE-FNF-GQFEKTFDILV--TQAGYYGIPKKIAEKRA-EEYLEKLGLweKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:TIGR01271 1297 IPQKvFIFsGTFRKNLDPYEqwSDEEIWKVAEEVGLKSViEQFPDKLDF--VLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 158 LILDEPTAGVDIE----LRRSMWEFLTEmnekgTSIILTTHYLeEAEMLCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:TIGR01271 1375 LLLDEPSAHLDPVtlqiIRKTLKQSFSN-----CTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-222 |
2.41e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 18 FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLD-THPSEA-KQCLGVVPQEFNFGQFEKT 95
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAvKKGMAYITESRRDNGFFPN 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 96 FDI--------LVTQAGYYGI--------PKKIAEKRAEEYLEKLGLWEKRNTQgrmLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:PRK09700 356 FSIaqnmaisrSLKDGGYKGAmglfhevdEQRTAENQRELLALKCHSVNQNITE---LSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKD 222
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-196 |
3.12e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL----DTHPSEAKQCLGVVPQE-------- 86
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDplaslnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 FNFGQF--E--KTFdilvtqagYYGIPKKIAEKRAEEYLEKLGLWEKR-NTQGRMLSGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK15079 115 MTIGEIiaEplRTY--------HPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYL 196
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDL 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-212 |
3.90e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGV--VP 84
Cdd:PRK10982 1 MSNISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIsmVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFD-----------ILVTQAGYYGIPKKIaekraeeyLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:PRK10982 80 QELNLVLQRSVMDnmwlgryptkgMFVDQDKMYRDTKAI--------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSY 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK10982 152 NAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-194 |
6.39e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDThpseAKQCL---GVVPQEfnfgqfektfD 97
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKP----TKQILkrtGFVTQD----------D 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 98 ILVTQ---------AGYYGIPKKIAEKR----AEEYLEKLGLWEKRNTQG-----RMLSGGMKRRLMIARAMMHEPKLLI 159
Cdd:PLN03211 150 ILYPHltvretlvfCSLLRLPKSLTKQEkilvAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190
....*....|....*....|....*....|....*
gi 491152796 160 LDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-219 |
2.59e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 24 INLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLdthPSEAKQCLGVVPQE----FNFGQFEKTFDIL 99
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSRLYTVRKRmsmlFQSGALFTDMNVF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 100 VTQA----GYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:PRK11831 103 DNVAyplrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491152796 176 WEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAII-DRGVIKEDTS 219
Cdd:PRK11831 183 VKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVaDKKIVAHGSA 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-196 |
3.09e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.96 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 20 ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVVPQE-FNFGQfektfd 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtKLQLDSWRSRLAVVSQTpFLFSD------ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 98 ilvTQAGYYGIPKKIAEKRAEEYLEKLG--------LWEKRNTQ----GRMLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:PRK10789 404 ---TVANNIALGRPDATQQEIEHVARLAsvhddilrLPQGYDTEvgerGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190
....*....|....*....|....*....|.
gi 491152796 166 GVDIELRRSMWEFLTEMNEKGTsIILTTHYL 196
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRT-VIISAHRL 510
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
7-229 |
3.22e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.76 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYKNG--FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGhnldthpseaKQCLGVVP 84
Cdd:PRK13545 24 LKDLFFRSKDGeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------SAALIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNfGQFEKTFDILVtQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:PRK13545 94 SGLN-GQLTGIENIEL-KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 165 AGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLNE 229
Cdd:PRK13545 172 SVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-196 |
3.33e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 24 INLTVPEGEFYALLGPNGAGKSTTISIISSLTKkTSGSVEIFGHNLDTHP-SEAKQCLGVVPQefnfgQFEKTFDILVTQ 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSaAELARHRAYLSQ-----QQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 103 ----AGYYGIPKKIAEKRAEEYLEKLGLWEK--RNTQgrMLSGGMKRR-------LMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PRK03695 89 yltlHQPDKTRTEAVASALNEVAEALGLDDKlgRSVN--QLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*..
gi 491152796 170 ELRRSMWEFLTEMNEKGTSIILTTHYL 196
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-170 |
3.49e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGfQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfghnldthpSEAKQcLGVV 83
Cdd:PRK15064 319 ALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENAN-IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQ--EFNFGQFEKTFDIlvtqagyygipkkIAEKRAEEYLEKLglweKRNTQGRML-------------SGGMKRRLMIA 148
Cdd:PRK15064 388 AQdhAYDFENDLTLFDW-------------MSQWRQEGDDEQA----VRGTLGRLLfsqddikksvkvlSGGEKGRMLFG 450
|
170 180
....*....|....*....|..
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIE 170
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDME 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-194 |
4.12e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.42 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGsveifghnlDTHPSEAKQClGVVPQ 85
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG---------EARPQPGIKV-GYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 EFNFGQfEKTF---------DILVTQAGY------YGIP----KKIAEKRAE--EYLEKLGLWE-KRNTQGRM------- 136
Cdd:TIGR03719 76 EPQLDP-TKTVrenveegvaEIKDALDRFneisakYAEPdadfDKLAAEQAElqEIIDAADAWDlDSQLEIAMdalrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 137 -------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIE----LRRSMWEFltemneKGTsIILTTH 194
Cdd:TIGR03719 155 wdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAEsvawLERHLQEY------PGT-VVAVTH 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-214 |
1.13e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 26 LTVPEGEFYALLGPNGAGKSTTISIIS--------------SLT---------KKTSGSV---------EIFGHNLDTHp 73
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqDLIvarlqqdppRNVEGTVydfvaegieEQAEYLKRYH- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 74 sEAKQCLGVVPQEFNFGQFEKTFDILVTQAGYYgipkkiAEKRAEEYLEKLGLweKRNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:PRK11147 103 -DISHLVETDPSEKNLNELAKLQEQLDHHNLWQ------LENRINEVLAQLGL--DPDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLteMNEKGtSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFL--KTFQG-SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-225 |
1.26e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLS---KTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKK----TSGSV--------------- 62
Cdd:PRK15093 4 LDIRNLTiefKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMrfddidllrlsprer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 63 -EIFGHNLDTHPSEAKQCLGvvPQEfNFGQFEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRM---LS 138
Cdd:PRK15093 84 rKLVGHNVSMIFQEPQSCLD--PSE-RVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFpyeLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 139 GGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNE-KGTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
....*...
gi 491152796 218 TSMKDFLN 225
Cdd:PRK15093 241 APSKELVT 248
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
22-216 |
1.35e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.48 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 22 KGINLTVPEGEFYALLGPNGAGKSTTIS----IISSLTKKTSGSVEifghnLDTHPSEAKQCLG----VVPQE----FNF 89
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAaalgILPAGVRQTAGRVL-----LDGKPVAPCALRGrkiaTIMQNprsaFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 90 GQFEKTFDILVTQAgyYGIPKKIAekRAEEYLEKLGLWEKRNTQGRM---LSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:PRK10418 95 LHTMHTHARETCLA--LGKPADDA--TLTAALEAVGLENAARVLKLYpfeMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 167 VDIELRRSMWEFLTE-MNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK10418 171 LDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVE 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-216 |
1.47e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTT----ISIISSltkktSGSVEIFGHNLdtHPSEAKQCL------GVVPQEFN 88
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINS-----QGEIWFDGQPL--HNLNRRQLLpvrhriQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 89 fGQFEKTFDILVT-----QAGYYGIPKKIAEKRAEEYLEKLGL-WEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:PRK15134 373 -SSLNPRLNVLQIieeglRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491152796 163 PTAGVDIELRRSMWEFLTEMNEK-GTSIILTTHYLEEAEMLCRRIAIIDRGVIKE 216
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVE 506
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-194 |
1.90e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 31 GEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfghnlDTHPSEAKQCLGVVPQEFNFGQFEKTFDILVTQAGYYGIPK 110
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-----DGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 111 KIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSII 190
Cdd:PRK13543 112 RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGAAL 191
|
....
gi 491152796 191 LTTH 194
Cdd:PRK13543 192 VTTH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
137-214 |
2.19e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 2.19e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-195 |
2.55e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.80 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLT--KKTSGSVEIFGHNLDTHPSEAKQCLGVvpqefnFGQFEKTFDI 98
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGI------FMAFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 99 --LVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRML---------------SGGMKRRLMIARAMMHEPKLLILD 161
Cdd:PRK09580 91 pgVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190
....*....|....*....|....*....|....
gi 491152796 162 EPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHY 195
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY 204
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-183 |
2.63e-10 |
|
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: 61.30 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 16 NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKktsgsveIFGHNLdTHPSEAKqcLGVVPQE--FNFGQFE 93
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-------VYGGRL-TKPAKGK--LFYVPQRpyMTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 94 KtfDILVTQAGYYGIPKKIAEKRAEEYLEKLGL---------WEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:TIGR00954 533 D--QIIYPDSSEDMKRRGLSDKDLEQILDNVQLthilereggWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170
....*....|....*....
gi 491152796 165 AGVDIELRRSMWEFLTEMN 183
Cdd:TIGR00954 611 SAVSVDVEGYMYRLCREFG 629
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-194 |
6.37e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.89 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 23 GINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCL-------GV----VPQE-FNFG 90
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpGIktelTALEnLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QfektfdilvTQAGYYGipkkiaEKRAEEYLEKLGLwekrntQGRM------LSGGMKRRLMIARAMMHEPKLLILDEP- 163
Cdd:PRK13538 99 Q---------RLHGPGD------DEALWEALAQVGL------AGFEdvpvrqLSAGQQRRVALARLWLTRAPLWILDEPf 157
|
170 180 190
....*....|....*....|....*....|....*
gi 491152796 164 ----TAGVDiELRRSMWEFLtemnEKGTSIILTTH 194
Cdd:PRK13538 158 taidKQGVA-RLEALLAQHA----EQGGMVILTTH 187
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
15-196 |
7.83e-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: 7.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 15 KNGFqALKGinLTVP-EGEFYALLGPNGAGKSTTISIISSLTK-----------------KTSGSvEIFGH-----NLDT 71
Cdd:COG1245 85 ENGF-RLYG--LPVPkKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkRFRGT-ELQDYfkklaNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 72 HPSEAKQCLGVVPQEFNfGqfeKTFDILvtqagyygipKKIAEK-RAEEYLEKLGL---WEKRNTQgrmLSGGMKRRLMI 147
Cdd:COG1245 161 KVAHKPQYVDLIPKVFK-G---TVRELL----------EKVDERgKLDELAEKLGLeniLDRDISE---LSGGELQRVAI 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYL 196
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-214 |
1.09e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 24 INLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTH-------------PSEAKQcLGVVP----QE 86
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRsprdairagimlcPEDRKA-EGIIPvhsvAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 87 ----------FNFGQFektfdilvtqagyygIPKKIAEKRAEEYLEKLGLweK---RNTQGRMLSGGMKRRLMIARAMMH 153
Cdd:PRK11288 351 ninisarrhhLRAGCL---------------INNRWEAENADRFIRSLNI--KtpsREQLIMNLSGGNQQKAILGRWLSE 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-226 |
1.41e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 7 LRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVVP 84
Cdd:TIGR00957 1287 FRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIGLHDLRFKITIIP 1366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QE---FN---------FGQFEK-----TFDILVTQAGYYGIPKKIAEKRAEeyleklglwekrntQGRMLSGGMKRRLMI 147
Cdd:TIGR00957 1367 QDpvlFSgslrmnldpFSQYSDeevwwALELAHLKTFVSALPDKLDHECAE--------------GGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 148 ARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTsiILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT--VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-217 |
1.50e-09 |
|
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: 58.68 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 24 INLTVPEGEFYALLGPNGAGKSTTIS-IISSLTKKTSGSVEIFGHNLDTHPS----EAKQCL--------GVVPQeFNFG 90
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPaqaiRAGIAMvpedrkrhGIVPI-LGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QfEKTFDILVTQAGYYGIPKKIAEKRAEEYLEKLGLweKRNTQ----GRmLSGGMKRRLMIARAMMHEPKLLILDEPTAG 166
Cdd:TIGR02633 358 K-NITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKV--KTASPflpiGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491152796 167 VDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKED 217
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-191 |
1.53e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 25 NLTVPEGEFYALLGPNGAGKSttisiisSLTKKTSGSVEIFGHNLD---THPS----EAKQCLgvVPQEFnfgQFEKTfD 97
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKS-------ALARALAGELPLLSGERQsqfSHITrlsfEQLQKL--VSDEW---QRNNT-D 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 98 ILVTQAGYYGipKKIAE---------KRAEEYLEKLG---LWEKRNTQgrmLSGGMKRRLMIARAMMHEPKLLILDEPTA 165
Cdd:PRK10938 90 MLSPGEDDTG--RTTAEiiqdevkdpARCEQLAQQFGitaLLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180
....*....|....*....|....*.
gi 491152796 166 GVDIELRRSMWEFLTEMNEKGTSIIL 191
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVL 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-226 |
1.59e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.19 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfghnldthpseaKQCLGV 82
Cdd:TIGR00957 636 SITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVAY 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 83 VPQEFNFGQFEKTFDILvtqagyYGipKKIAEKRAEEYLEKLGLW-----------EKRNTQGRMLSGGMKRRLMIARAM 151
Cdd:TIGR00957 704 VPQQAWIQNDSLRENIL------FG--KALNEKYYQQVLEACALLpdleilpsgdrTEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 152 MHEPKLLILDEPTAGVDIELRRSMWEFLT--EMNEKGTSIILTTH---YLEEAEMlcrrIAIIDRGVIKEDTSMKDFLNQ 226
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQELLQR 851
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
137-230 |
1.63e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 137 LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKe 216
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK- 484
|
90
....*....|....*
gi 491152796 217 dtsmKDFLNQ-LNEE 230
Cdd:PRK13549 485 ----GDLINHnLTQE 495
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-194 |
2.17e-09 |
|
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: 56.10 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLS---KTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSltKKTSGSVEifghnldthpseakqclg 81
Cdd:cd03232 4 LTWKNLNytvPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVIT------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 vvpqefnfGqfektfDILVTqagyyGIPKKIAEKRAEEYLEKLGLWEKRNT---------QGRMLSGGMKRRLMIARAMM 152
Cdd:cd03232 64 --------G------EILIN-----GRPLDKNFQRSTGYVEQQDVHSPNLTvrealrfsaLLRGLSVEQRKRLTIGVELA 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-228 |
3.84e-09 |
|
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: 57.49 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 9 DLSKTYkNGFQalkginLTVPEGEFY-----ALLGPNGAGKSTTISIISSLTKKTSGSVEifghnldthpSEAKqcLGVV 83
Cdd:COG1245 346 DLTKSY-GGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEVD----------EDLK--ISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEfnfgqFEKTFDILVTQAGYYGIPKKIAEKRAE-EYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:COG1245 407 PQY-----ISPDYDGTVEEFLRSANTDDFGSSYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491152796 163 PTAGVDIELRRSMWEFLTEMNE-KGTSIILTTHYLEEAEMLCRRIAIID-----RGVIKEDTSMKD----FLNQLN 228
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAEnRGKTAMVVDHDIYLIDYISDRLMVFEgepgvHGHASGPMDMREgmnrFLKELG 557
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-194 |
4.60e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 18 FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfghnldthpseakqclgVVPQEfNFGQFEKTFD 97
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------------DVPDN-QFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 98 IlvtqagyygIPKKIAEKRAEEYLEKLGL-----WEKRNTQgrmLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL- 171
Cdd:COG2401 105 A---------IGRKGDFKDAVELLNAVGLsdavlWLRRFKE---LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTa 172
|
170 180
....*....|....*....|...
gi 491152796 172 RRSMWEFLTEMNEKGTSIILTTH 194
Cdd:COG2401 173 KRVARNLQKLARRAGITLVVATH 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-194 |
4.83e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfGHNLDTHpseakqclgvvpqefNFGQF------EK 94
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVA---------------YFDQHraeldpEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 95 TF---------DILVTqagyyGIPKKIAEkraeeYLEKLGLWEKR-NTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPT 164
Cdd:PRK11147 399 TVmdnlaegkqEVMVN-----GRPRHVLG-----YLQDFLFHPKRaMTPVKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
170 180 190
....*....|....*....|....*....|..
gi 491152796 165 AGVDIElrrsMWEFLTEM--NEKGTsIILTTH 194
Cdd:PRK11147 469 NDLDVE----TLELLEELldSYQGT-VLLVSH 495
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-202 |
9.16e-09 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.90 E-value: 9.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTkktsgsveiFGHNLDTHPSEAKQCLGVVPQefnfgqFEKTFDILV 100
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLAL---------GGAQSATRRRSGVKAGCIVAA------VSAELIFTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 101 TQagyygipkkiaekraeeyleklglwekrntqgrmLSGGMKRRLMIARAMMHEPK----LLILDEPTAGVDIELRRSMW 176
Cdd:cd03227 76 LQ----------------------------------LSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALA 121
|
170 180
....*....|....*....|....*.
gi 491152796 177 EFLTEMNEKGTSIILTTHYLEEAEML 202
Cdd:cd03227 122 EAILEHLVKGAQVIVITHLPELAELA 147
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
52-211 |
9.39e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 52 SSLTKKTSGSVEIFGHNL-DTHPSEAKQCLGVVPQE---FN--------FGQFEKTFDIlVTQAGYYGIPKKIAEKRAEE 119
Cdd:PTZ00265 1269 DSTVFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEpmlFNmsiyenikFGKEDATRED-VKRACKFAAIDEFIESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 120 YLEKLGLWekrntqGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTthyleea 199
Cdd:PTZ00265 1348 YDTNVGPY------GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT------- 1414
|
170
....*....|..
gi 491152796 200 emLCRRIAIIDR 211
Cdd:PTZ00265 1415 --IAHRIASIKR 1424
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-172 |
1.56e-08 |
|
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: 54.34 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFY-----ALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPS--EAKQCLGVvpQEFnfgQ 91
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQyiKADYEGTV--RDL---L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 92 FEKTfDILVTQAgYYgipkkiaekrAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIEL 171
Cdd:cd03237 83 SSIT-KDFYTHP-YF----------KTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
.
gi 491152796 172 R 172
Cdd:cd03237 151 R 151
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1-235 |
1.71e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.44 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 1 MTDALTLRDLSKTykngFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGH--NLDTHPSEAKQ 78
Cdd:PRK13546 24 MKDALIPKHKNKT----FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 79 CLGVVPQEFnfgqfektfdilvtQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:PRK13546 100 LTGIENIEF--------------KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 159 ILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVIKEDTSMKDFLNQLneESFIFD 235
Cdd:PRK13546 166 VIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY--EAFLND 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-203 |
2.04e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.41 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYKnGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEA-KQCLGVVP 84
Cdd:PRK10575 13 ALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQfEKTFDILVTQAGY--------YGIPKKiaeKRAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:PRK10575 92 QQLPAAE-GMTVRELVAIGRYpwhgalgrFGAADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491152796 157 LLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTHYLEEAEMLC 203
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMAARYC 215
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
13-202 |
2.83e-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: 53.91 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 13 TYKNGFQALKGINLTVP-EGEFYALLGPNGAGKSTTISIISSLTKKTSGSV-------EIFGH--------------NLD 70
Cdd:cd03236 7 VHRYGPNSFKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdEILDEfrgselqnyftkllEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 71 THPSEAKQCLGVVPQEFNfgqfEKTFDILvtqagyygipKKIAEKRA-EEYLEKLGLWEKRNTQGRMLSGGMKRRLMIAR 149
Cdd:cd03236 87 VKVIVKPQYVDLIPKAVK----GKVGELL----------KKKDERGKlDELVDQLELRHVLDRNIDQLSGGELQRVAIAA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491152796 150 AMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEML 202
Cdd:cd03236 153 ALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYL 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-194 |
3.15e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 6 TLRDLSKTYKNGFQALKGINLTvpegeFY-----ALLGPNGAGKSTTISIISSLTKKTSGsveifghnlDTHPSEAKQCl 80
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLS-----FFpgakiGVLGLNGAGKSTLLRIMAGVDKEFEG---------EARPAPGIKV- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 81 GVVPQEfnfGQF--EKTF---------DILVTQAGY------YGIPK----KIAEKRAE--EYLEKLGLWEkRNTQGRM- 136
Cdd:PRK11819 73 GYLPQE---PQLdpEKTVrenveegvaEVKAALDRFneiyaaYAEPDadfdALAAEQGElqEIIDAADAWD-LDSQLEIa 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491152796 137 ---------------LSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIE----LRRsmweFLTEMneKGTsIILTTH 194
Cdd:PRK11819 149 mdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAEsvawLEQ----FLHDY--PGT-VVAVTH 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-168 |
3.59e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKT-YKN---------GFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIF-GHNL-D 70
Cdd:PTZ00265 373 DGKKLKDIKKIqFKNvrfhydtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLkD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 71 THPSEAKQCLGVVPQE----------------FNFGQFEKTFDILV--TQAGYYGIPKKIA--EKRAEEY------LEKL 124
Cdd:PTZ00265 453 INLKWWRSKIGVVSQDpllfsnsiknnikyslYSLKDLEALSNYYNedGNDSQENKNKRNScrAKCAGDLndmsntTDSN 532
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 125 GLWEKRN-----------------------------------TQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:PTZ00265 533 ELIEMRKnyqtikdsevvdvskkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-242 |
4.80e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.60 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 4 ALTLRDLSKTYKNGFQ-ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP-SEAKQCLG 81
Cdd:PLN03232 1234 SIKFEDVHLRYRPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGlTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 82 VVPQ---------EFNFGQFEKTFDILVTQAGYYGIPKKIAEKRAeeylekLGLWEKRNTQGRMLSGGMKRRLMIARAMM 152
Cdd:PLN03232 1314 IIPQspvlfsgtvRFNIDPFSEHNDADLWEALERAHIKDVIDRNP------FGLDAEVSEGGENFSVGQRQLLSLARALL 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 153 HEPKLLILDEPTAGVDIELRRSMWEFLTEmNEKGTSIILTTHYLEEAeMLCRRIAIIDRGVIKEDTSMKDFLNqlNEESF 232
Cdd:PLN03232 1388 RRSKILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLS--RDTSA 1463
|
250
....*....|
gi 491152796 233 IFDLAAPIEP 242
Cdd:PLN03232 1464 FFRMVHSTGP 1473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-181 |
5.51e-08 |
|
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: 53.79 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 8 RDLSKTYkNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEI-----------FGHNLDTHPSea 76
Cdd:TIGR03719 326 ENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdqSRDALDPNKT-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 kqclgvVPQEFNFGQfektfDILvtQAGYYGIPkkiaeKRAeeYLEKLGLweKRNTQGRM---LSGGMKRRLMIARAMMH 153
Cdd:TIGR03719 403 ------VWEEISGGL-----DII--KLGKREIP-----SRA--YVGRFNF--KGSDQQKKvgqLSGGERNRVHLAKTLKS 460
|
170 180
....*....|....*....|....*...
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTE 181
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEALLN 488
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-217 |
7.91e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTIS-IISSLTKKTSGSVEIFGhnldthpseakqCLGVVPQE---FN-------- 88
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG------------SVAYVPQVswiFNatvrenil 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 89 FG-QFE-----KTFDILVTQAGYYGIPKKIAEKRAEeyleklglwekrntQGRMLSGGMKRRLMIARAMMHEPKLLILDE 162
Cdd:PLN03232 701 FGsDFEserywRAIDVTALQHDLDLLPGRDLTEIGE--------------RGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 163 PTAGVDIELRRSMWEFLTEMNEKGTSIILTT---HYLEEAEmlcrRIAIIDRGVIKED 217
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMD----RIILVSEGMIKEE 820
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
5-170 |
1.11e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 5 LTLRDLSKTYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVeiFghnldthpSEAKQCLGVVP 84
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--F--------RSAKVRMAVFS 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 85 QEFNFGQFEKTFDILVTQAGYYGIPkkiaEKRAEEYLEKLGLWEKRNTQGR-MLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:PLN03073 579 QHHVDGLDLSSNPLLYMMRCFPGVP----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
....*..
gi 491152796 164 TAGVDIE 170
Cdd:PLN03073 655 SNHLDLD 661
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-194 |
1.13e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 3 DALTLRDLSKTYKNG---FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNL--------DT 71
Cdd:PRK10261 11 DVLAVENLNIAFMQEqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 72 HPSEAKQCLGV-------VPQE--------FNFGQfektfDILVTQAGYYGIPKKIAEKRAEEYLEKLGLWEKRNTQGR- 135
Cdd:PRK10261 91 SEQSAAQMRHVrgadmamIFQEpmtslnpvFTVGE-----QIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRy 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 136 --MLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMN-EKGTSIILTTH 194
Cdd:PRK10261 166 phQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITH 227
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-225 |
1.19e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTIS-IISSLTKKTSGSVEIFGHnldthpseakqcLGVVPQ-------------- 85
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT------------VAYVPQvswifnatvrdnil 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 86 ---EFNFGQFEKTFDILVTQAGYYGIP----KKIAEKraeeyleklglwekrntqGRMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:PLN03130 701 fgsPFDPERYERAIDVTALQHDLDLLPggdlTEIGER------------------GVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 159 ILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTT---HYLEEAEmlcrRIAIIDRGVIKEDTSMKDFLN 225
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTnqlHFLSQVD----RIILVHEGMIKEEGTYEELSN 828
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-212 |
1.31e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.81 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 20 ALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTH-PSEA-KQCLGVVPQEFN----FGQFE 93
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnANEAiNHGFALVTEERRstgiYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 94 KTFDILVTQAgyygipkkiaekraEEYLEKLGLWE----KRNTQGRM----------------LSGGMKRRLMIARAMMH 153
Cdd:PRK10982 343 IGFNSLISNI--------------RNYKNKVGLLDnsrmKSDTQWVIdsmrvktpghrtqigsLSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRG 212
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-197 |
1.72e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.18 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 13 TYKNGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKQCLGVVPQEFNfGQF 92
Cdd:cd03290 9 SWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYA-AQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 93 EKTFDILVTQAGYYGIP------KKIAEK---RAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEP 163
Cdd:cd03290 88 PWLLNATVEENITFGSPfnkqryKAVTDAcslQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 491152796 164 TAGVDIELRRSMWE--FLTEMNEKGTSIILTTHYLE 197
Cdd:cd03290 168 FSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-172 |
1.77e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 9 DLSKTYkNGFQalkginLTVPEGEFYA-----LLGPNGAGKSTTISIISSLTKKTSGSVEIfghNLDthpseakqcLGVV 83
Cdd:PRK13409 345 DLTKKL-GDFS------LEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK---------ISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEFnFGQFEKTFDILVTQAG------YYgipkkiaekrAEEYLEKLGLWEKRNTQGRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:PRK13409 406 PQYI-KPDYDGTVEDLLRSITddlgssYY----------KSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170
....*....|....*
gi 491152796 158 LILDEPTAGVDIELR 172
Cdd:PRK13409 475 YLLDEPSAHLDVEQR 489
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-181 |
1.84e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfghnldthpseAKQC-LGVVPQ---EFnFGQFEKTF 96
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGIkLGYFAQhqlEF-LRADESPL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 97 DILVTQAgyygipKKIAEKRAEEYLEKLGLW-EKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSM 175
Cdd:PRK10636 396 QHLARLA------PQELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
....*.
gi 491152796 176 WEFLTE 181
Cdd:PRK10636 470 TEALID 475
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-172 |
2.27e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 15 KNGFqALKGinLTVP-EGEFYALLGPNGAGKSTTISIISSLTKKTSGSV-------EIF----GHNLDTHPSEAK----- 77
Cdd:PRK13409 85 VNGF-KLYG--LPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdEVLkrfrGTELQNYFKKLYngeik 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 78 -----QCLGVVPQEFNfGqfeKTFDILvtqagyygipKKIAEK-RAEEYLEKLGL---WEKRNTQgrmLSGGMKRRLMIA 148
Cdd:PRK13409 162 vvhkpQYVDLIPKVFK-G---KVRELL----------KKVDERgKLDEVVERLGLeniLDRDISE---LSGGELQRVAIA 224
|
170 180
....*....|....*....|....
gi 491152796 149 RAMMHEPKLLILDEPTAGVDIELR 172
Cdd:PRK13409 225 AALLRDADFYFFDEPTSYLDIRQR 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
19-194 |
3.16e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKSTTISIISSltKKTSGSVE-----IFGHNLDthpSEAKQCLGVVPQEfnfgqfe 93
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITggdrlVNGRPLD---SSFQRSIGYVQQQ------- 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 94 ktfDILVTQA---------GYYGIPKKIAEKRAEEYLEK-LGLWEKRN-------TQGRMLSGGMKRRLMIARAMMHEPK 156
Cdd:TIGR00956 845 ---DLHLPTStvreslrfsAYLRQPKSVSKSEKMEYVEEvIKLLEMESyadavvgVPGEGLNVEQRKRLTIGVELVAKPK 921
|
170 180 190
....*....|....*....|....*....|....*....
gi 491152796 157 LLI-LDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:TIGR00956 922 LLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-208 |
4.24e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 48.52 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 31 GEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFghNLDTHPSEAKQCLGVVPqefnfgqfektfdilvtqagyygipk 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--DGEDILEEVLDQLLLII-------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 111 kiaekraeeyleklglwekRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWE------FLTEMNE 184
Cdd:smart00382 54 -------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLLLLKSE 114
|
170 180 190
....*....|....*....|....*....|
gi 491152796 185 KGTSIILTTHYLEE------AEMLCRRIAI 208
Cdd:smart00382 115 KNLTVILTTNDEKDlgpallRRRFDRRIVL 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-168 |
1.98e-06 |
|
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: 47.64 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 2 TDALTLRDLSKTYK---NGFQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTK---KTSGSVEIFGHNLD----T 71
Cdd:cd03233 1 ASTLSWRNISFTTGkgrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEgnvSVEGDIHYNGIPYKefaeK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 72 HPSEAkqcLGVVPQEFNFGQF--EKTFDIlvtqagyygipkkIAEKRAEEYLeklglwekrntqgRMLSGGMKRRLMIAR 149
Cdd:cd03233 81 YPGEI---IYVSEEDVHFPTLtvRETLDF-------------ALRCKGNEFV-------------RGISGGERKRVSIAE 131
|
170
....*....|....*....
gi 491152796 150 AMMHEPKLLILDEPTAGVD 168
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLD 150
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
137-194 |
2.00e-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: 48.54 E-value: 2.00e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 137 LSGGMKR---RLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:pfam13304 237 LSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-214 |
3.98e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.86 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 19 QALKGINLTVPEGEFYALLGPNGAGKS-TTISIIS-SLTKKTSGSVEIFGHNLDTH-PSEA------------KQcLGVV 83
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGrSYGRNISGTVFKDGKEVDVStVSDAidaglayvtedrKG-YGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 84 PQEfnfgqfektfDIL--VTQAGYYGIPKK-----IAEKR-AEEYLEKL-----GLWEKRNTqgrmLSGGMKRRLMIARA 150
Cdd:NF040905 353 LID----------DIKrnITLANLGKVSRRgvideNEEIKvAEEYRKKMniktpSVFQKVGN----LSGGNQQKVVLSKW 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491152796 151 MMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLEEAEMLCRRIAIIDRGVI 214
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-168 |
5.17e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 18 FQALKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHnLDTHPSE--AKQCLGVV----PQEFNFGQ 91
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVIT-YDGITPEeiKKHYRGDVvynaETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 92 FeKTFDILVTQAG-------YYGIPKKI-AEKRAEEYLEKLGLWEKRNTQ-G----RMLSGGMKRRLMIARAMMHEPKLL 158
Cdd:TIGR00956 153 L-TVGETLDFAARcktpqnrPDGVSREEyAKHIADVYMATYGLSHTRNTKvGndfvRGVSGGERKRVSIAEASLGGAKIQ 231
|
170
....*....|
gi 491152796 159 ILDEPTAGVD 168
Cdd:TIGR00956 232 CWDNATRGLD 241
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
30-215 |
5.53e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 30 EGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIfghnldthpsEAKQCLGVVPQ-EFNFGQF----------EKTFDI 98
Cdd:PRK15064 26 GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL----------DPNERLGKLRQdQFAFEEFtvldtvimghTELWEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 99 LVTQAGYYGIPKK---------------------IAEKRAEEYLEKLGLWEKRNtQGRM--LSGGMKRRLMIARAMMHEP 155
Cdd:PRK15064 96 KQERDRIYALPEMseedgmkvadlevkfaemdgyTAEARAGELLLGVGIPEEQH-YGLMseVAPGWKLRVLLAQALFSNP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491152796 156 KLLILDEPTAGVDIELRRSMWEFLTEMNekGTSIILT--THYLeeaEMLCRRIAIIDRGVIK 215
Cdd:PRK15064 175 DILLLDEPTNNLDINTIRWLEDVLNERN--STMIIIShdRHFL---NSVCTHMADLDYGELR 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-169 |
5.21e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 21 LKGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHP-SEAKQCLGVVPQ---------EFNFG 90
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKVLGIIPQapvlfsgtvRFNLD 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 91 QFEKTFDilvtqagyygipkkiaekrAE--EYLEKLGLWE--KRNTQ---------GRMLSGGMKRRLMIARAMMHEPKL 157
Cdd:PLN03130 1335 PFNEHND-------------------ADlwESLERAHLKDviRRNSLgldaevseaGENFSVGQRQLLSLARALLRRSKI 1395
|
170
....*....|..
gi 491152796 158 LILDEPTAGVDI 169
Cdd:PLN03130 1396 LVLDEATAAVDV 1407
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
113-169 |
7.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 7.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 113 AEKRAEEYLEKLGLW-EKRNTQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDI 169
Cdd:PLN03073 320 AEARAASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
38-194 |
1.73e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 38 GPNGAGKSTTISIISSLTKKTSGsvEIFGHNLDTHpSEAKQCLGVVPQEFNFGQFEKTFDILVTQAGYYG----IPKKIA 113
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSG--NIYYKNCNIN-NIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNsaetLYAAIH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 114 EKRAEEYLEKlglwekrntQGRMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTT 193
Cdd:PRK13541 110 YFKLHDLLDE---------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSS 180
|
.
gi 491152796 194 H 194
Cdd:PRK13541 181 H 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-181 |
1.76e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 9 DLSKTYknGFQAL-KGINLTVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEI-----------FGHNLDthPSEA 76
Cdd:PRK11819 329 NLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdqSRDALD--PNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 77 kqclgvVPQEFNFGQfektfDILvtQAGYYGIPkkiaeKRAeeYLEKLGLweKRNTQGR---MLSGGMKRRLMIARAMMH 153
Cdd:PRK11819 405 ------VWEEISGGL-----DII--KVGNREIP-----SRA--YVGRFNF--KGGDQQKkvgVLSGGERNRLHLAKTLKQ 462
|
170 180
....*....|....*....|....*...
gi 491152796 154 EPKLLILDEPTAGVDIELRRSMWEFLTE 181
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
137-212 |
2.95e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.77 E-value: 2.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491152796 137 LSGGMKRRLMIARAMMHEPK--LLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTHYLeeaEMLCRRIAIIDRG 212
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNL---DVLSSADWIIDFG 162
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-170 |
3.17e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.08 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 27 TVPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGH------NLDThPSEAKQCLG-VVPQEFNFGQFEKTFDIL 99
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvNQET-PALPQPALEyVIDGDREYRQLEAQLHDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 100 VTQ------AGYYGIPKKIA----EKRAEEYLEKLGLWEKRNTQG-RMLSGGMKRRLMIARAMMHEPKLLILDEPTAGVD 168
Cdd:PRK10636 102 NERndghaiATIHGKLDAIDawtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
..
gi 491152796 169 IE 170
Cdd:PRK10636 182 LD 183
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
16-194 |
3.57e-04 |
|
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: 41.91 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 16 NGFQALKGINLTVPEGeFYALLGPNGAGKSTTISIISSLTKKTSG---SVEIFGHNLDTHP------------------- 73
Cdd:COG3593 9 KNFRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrkfDEEDFYLGDDPDLpeieieltfgsllsrllrl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 74 ---SEAKQCLGVVPQEFNfGQFEKTFDILVTQAGYYGIPK--------KIAEKRAEEYLEKLGLWEKRNTQGRM--LSGG 140
Cdd:COG3593 88 llkEEDKEELEEALEELN-EELKEALKALNELLSEYLKELldgldlelELSLDELEDLLKSLSLRIEDGKELPLdrLGSG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491152796 141 MKRRLMIA--RAMMH-----EPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGTSIILTTH 194
Cdd:COG3593 167 FQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
28-210 |
5.11e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 37.17 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 28 VPEGEFYALLGPNGAGKSTTISIISSLTKKTSGSVEIFGHNLDTHPSEAKqclgvvpqefnfgqfektfdilvtqagyyg 107
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID------------------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 108 ipkkiaekraeeyleklglwekrntqgrmLSGGMKRRLMIARAMMHEPKLLILDEPTAGVDIELRRSMWEFLTEMNEKGT 187
Cdd:cd03222 72 -----------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
170 180
....*....|....*....|....
gi 491152796 188 -SIILTTHYLEEAEMLCRRIAIID 210
Cdd:cd03222 123 kTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
107-197 |
6.26e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.72 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 107 GIPKKIAEKRAEEYLEKLGLWEKRNTQG-----RMLSGGMKRRLMIARAMM---HEPKLLILDEPTAGVDIELRRSMWE- 177
Cdd:COG1106 168 GIEDIEVEEEEIEDLVERKLIFKHKGGNvplplSEESDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLRKLLKl 247
|
90 100
....*....|....*....|
gi 491152796 178 FLTEMNEKGTSIILTTHYLE 197
Cdd:COG1106 248 FLDLANKNNAQLIFTTHSTE 267
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
11-194 |
8.46e-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: 36.82 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 11 SKTYKNGFQALKGINLTVpegefyallGPNGAGKSTTISIIS-SLTKKTSGSVEIFGHnlDTHPSEAKQCLGVVpqEFNF 89
Cdd:cd03240 11 SFHERSEIEFFSPLTLIV---------GQNGAGKTTIIEALKyALTGELPPNSKGGAH--DPKLIREGEVRAQV--KLAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491152796 90 GQFEKTfDILVTQagYYGIPKKIAEKRAEEYLEKLGLWEKRntqgrmLSGGMKR------RLMIARAMMHEPKLLILDEP 163
Cdd:cd03240 78 ENANGK-KYTITR--SLAILENVIFCHQGESNWPLLDMRGR------CSGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190
....*....|....*....|....*....|...
gi 491152796 164 TAGVDIE-LRRSMWEFLTEMNEKGTS-IILTTH 194
Cdd:cd03240 149 TTNLDEEnIEESLAEIIEERKSQKNFqLIVITH 181
|
|
| |
