|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-239 |
9.83e-76 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 228.79 E-value: 9.83e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFVPE 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 162 GLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFncknLEEAFILATEKSQ 239
Cdd:COG1131 161 GLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL----LEDVFLELTGEEA 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
12-232 |
8.70e-65 |
|
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: 201.24 E-value: 8.70e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFVPEIPELDSS 88
Cdd:COG4555 9 KKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvRKEPREARRQIGVLPDERGLYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQI 168
Cdd:COG4555 89 LTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMAR 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 169 ASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFNCKNLEEAFI 232
Cdd:COG4555 169 RLLREILRALKKEgKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEENLEDAFV 233
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-209 |
2.21e-56 |
|
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: 177.59 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFVPE 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdiKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKEILffeaeisgqkkneadltvkkaaticgleevfnkkisKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2540524722 162 GLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:cd03230 125 GLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
12-213 |
1.04e-48 |
|
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: 159.28 E-value: 1.04e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEkNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFVPEIPELDSS 88
Cdd:cd03264 8 KRYGKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvLKQPQKLRRRIGYLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQI 168
Cdd:cd03264 87 FTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2540524722 169 ASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03264 167 IRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
5-218 |
5.35e-47 |
|
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: 154.97 E-value: 5.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFS--ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKA---TAFV 79
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAArqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 160 SAGLDPA---QIASFRKKLKNLSSsmtIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03263 161 TSGLDPAsrrAIWDLILEVRKGRS---IILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-228 |
4.99e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 149.87 E-value: 4.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATAFVPEIPE 84
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYLPEERG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 LDSSLTVKEILFFEAEISGQKKNEADltvKKAATIC---GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FS 160
Cdd:COG4152 82 LYPKMKVGEQLVYLARLKGLSKAEAK---RRADEWLerlGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEpFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 161 aGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFNCKNLE 228
Cdd:COG4152 159 -GLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
12-218 |
2.19e-42 |
|
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: 143.28 E-value: 2.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFVPEIPELDSS 88
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvVREPREVRRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP--- 165
Cdd:cd03265 88 LTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPqtr 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 166 AQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03265 168 AHVWEYIEKLKE-EFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-218 |
2.34e-42 |
|
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: 145.61 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFVPEIPELDSS 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP--- 165
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPrtr 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 166 AQIASFRKKLKnlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:TIGR01188 161 RAIWDYIRALK--EEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
14-231 |
2.02e-41 |
|
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: 141.72 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSL 89
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsrrELARRIAYVPQEPPAPFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 TVKEIL---------FFEAEisgqkkNEADLT-VKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:COG1120 91 TVRELValgryphlgLFGRP------SAEDREaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 160 SAGLDPA-QIASFRkKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVkkfNCKNLEEAF 231
Cdd:COG1120 165 TSHLDLAhQLEVLE-LLRRLARErgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL---TPELLEEVY 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
19-221 |
5.83e-41 |
|
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: 139.78 E-value: 5.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT----EETDEFKKATAFV---PeipelDSSL-- 89
Cdd:COG1122 16 ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkKNLRELRRKVGLVfqnP-----DDQLfa 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 -TVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQI 168
Cdd:COG1122 91 pTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 169 ASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:COG1122 171 RELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-208 |
1.16e-40 |
|
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: 138.37 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFV 79
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlslkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPELD-SSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:cd03225 81 FQNPDDQfFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 159 FSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-213 |
4.67e-40 |
|
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: 137.03 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATAFVPEIPE 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 LDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2540524722 165 PAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03269 161 PVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
9-213 |
1.02e-39 |
|
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: 136.34 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 9 SFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFVPEIPEL 85
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:cd03266 90 YDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2540524722 166 AQIASFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03266 170 MATRALREFIRQLrALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
11-231 |
2.36e-39 |
|
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: 135.60 E-value: 2.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATAFVPEIPELDSSLT 90
Cdd:TIGR03740 7 SKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPPLYENLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 91 VKEILFFEAEISGQKKNEADLTVKkaatICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIAS 170
Cdd:TIGR03740 87 ARENLKVHTTLLGLPDSRIDEVLN----IVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 171 FRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVaacGTEKEIVKKfncKNLEEAF 231
Cdd:TIGR03740 163 LRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVL---GYQGKINKS---ENLEKLF 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-213 |
4.25e-39 |
|
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: 134.57 E-value: 4.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKATAFVPEI 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGvpPERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSA 161
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEpLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 162 gLDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03259 161 -LDAKLREELREELKELQRElgITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
12-207 |
1.70e-38 |
|
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: 132.73 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKAT---AFVpEIPELDSS 88
Cdd:cd03268 8 KTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRrigALI-EAPGFYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEadltVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQI 168
Cdd:cd03268 87 LTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2540524722 169 ASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANG 207
Cdd:cd03268 163 KELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-231 |
1.30e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEfKKATAFVPEIPELDSS--LTV 91
Cdd:COG1121 16 YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-RRRIGYVPQRAEVDWDfpITV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 92 KEI----------LFFeaeISGQKKNEAdltVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:COG1121 95 RDVvlmgrygrrgLFR---RPSRADREA---VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 162 GLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIaNGEVAACGTEKEIvkkFNCKNLEEAF 231
Cdd:COG1121 169 GVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEV---LTPENLSRAY 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-213 |
2.29e-37 |
|
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: 129.96 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCknYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKAtAFVPEIP 83
Cdd:cd03235 1 EVEDLTVS--YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI-GYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 ELDSS--LTVKEI--------LFFEAEISGQKKNEADLTVKKAaticGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:cd03235 78 SIDRDfpISVRDVvlmglyghKGLFRRLSKADKAKVDEALERV----GLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 154 LVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIaNGEVAACG 213
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-208 |
2.30e-36 |
|
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: 125.82 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 6 ELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEetdefkkatafvpeIPEL 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD--------------IAKL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILFfeaeisgqkkneadltvkkaaticgleevfnkkISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:cd00267 67 PLEELRRRIGY---------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2540524722 166 AQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:cd00267 114 ASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-220 |
4.15e-36 |
|
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: 127.62 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-------ETDEFKKATA 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 78 FVPEIPELDSSLTVKE-ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVL 156
Cdd:cd03261 81 MLFQSGALFDSLTVFEnVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 157 DEFSAGLDPAQ-------IASFRKKLKnlsssMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:cd03261 161 DEPTAGLDPIAsgviddlIRSLKKELG-----LTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-213 |
9.54e-36 |
|
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: 126.47 E-value: 9.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 8 ISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD-------EFKKATAFVP 80
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlrkIRRKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 81 EIP--ELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGL---EEVFNKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:cd03257 89 QDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 156 LDEFSAGLDP---AQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03257 169 ADEPTSALDVsvqAQILDLLKKLQE-ELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-213 |
5.91e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 122.93 E-value: 5.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFckNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFV 79
Cdd:cd03214 1 EVENLSV--GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlspkELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPELdssltvkeilffeaeisgqkkneadltvkkaatiCGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:cd03214 79 PQALEL----------------------------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 160 SAGLDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARErgKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-213 |
6.74e-34 |
|
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: 6.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKATAFVPEI 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlpPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 163 LDPAQIASFRKKLKNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLgtTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-218 |
1.45e-33 |
|
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: 120.80 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKATAFVPEI 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 163 LDpaqiASFRKK----LKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03300 161 LD----LKLRKDmqleLKRLQKElgITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
5-221 |
2.30e-33 |
|
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: 120.52 E-value: 2.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSAcKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKATAFVPEI 82
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNlpPEKRDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 163 LDPAQIASFRKKLKNL--SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:cd03299 160 LDVRTKEKLREELKKIrkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-218 |
4.02e-33 |
|
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: 119.46 E-value: 4.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE--FKKAT---AFVPEIPELDSS 88
Cdd:cd03224 10 YGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLppHERARagiGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEADltvkkaaticgLEEVF----------NKKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKAR-----------LERVYelfprlkerrKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 159 FSAGLDPA---QIASFRKKLKnlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03224 159 PSEGLAPKiveEIFEAIRELR--DEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-219 |
8.84e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 120.68 E-value: 8.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATA---FVPEIPELDSS 88
Cdd:PRK13537 15 KRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQrvgVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQI 168
Cdd:PRK13537 95 FTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 169 ASFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:PRK13537 175 HLMWERLRSLlARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-206 |
1.09e-32 |
|
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: 117.96 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 9 SFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETDEFKKATAFVPEIPELDSS 88
Cdd:cd03293 9 TYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-EPVTGPGPDRGYVFQQDALLPW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAgLDpAQ 167
Cdd:cd03293 88 LTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEpFSA-LD-AL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2540524722 168 IasfRKKLKNL------SSSMTIIFSTHHIEEAVSMCNRIYIIAN 206
Cdd:cd03293 166 T---REQLQEElldiwrETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-208 |
3.51e-32 |
|
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: 115.75 E-value: 3.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD------EFKKATAF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledelpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKEILFFeaeisgqkkneadltvkkaaticgleevfnkkisKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 159 FSAGLDPAQIASFRKKLKNL--SSSMTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:cd03229 127 PTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-222 |
4.17e-32 |
|
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: 117.00 E-value: 4.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEetdefkkatafvp 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 81 eIPELD---------------------SSLTVKE-ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFK 138
Cdd:COG1127 69 -ITGLSekelyelrrrigmlfqggalfDSLTVFEnVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 139 QRTSLAKAICKLPKILVLDEFSAGLDP-------AQIASFRKKLKnlsssMTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDPitsavidELIRELRDELG-----LTSVVVTHDLDSAFAIADRVAVLADGKIIA 222
|
250
....*....|....*...
gi 2540524722 212 CGTEKEI-------VKKF 222
Cdd:COG1127 223 EGTPEELlasddpwVRQF 240
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-218 |
4.69e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.82 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDefkkatafVP 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--------LP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 81 eiPE------------LDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAIC 148
Cdd:COG3842 74 --PEkrnvgmvfqdyaLFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 149 KLPKILVLDE-FSAgLDPAQIASFRKKLKNL--SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG3842 152 PEPRVLLLDEpLSA-LDAKLREEMREELRRLqrELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-190 |
5.25e-32 |
|
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: 116.04 E-value: 5.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT---EETDEFKKATAFVPE 81
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKEILFFEAEISGQKKNEADltVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|
gi 2540524722 162 GLDPAQIASFRKKLKN-LSSSMTIIFSTHH 190
Cdd:COG4133 161 ALDAAGVALLAELIAAhLARGGAVLLTTHQ 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
9.83e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 119.02 E-value: 9.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSnEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDefkKAT---- 76
Cdd:COG3839 1 MA-SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD---LPPkdrn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 77 -AFVPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:COG3839 77 iAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 156 LDE-FSAgLDPAQIASFRKKLKNL--SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG3839 157 LDEpLSN-LDAKLRVEMRAEIKRLhrRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
11-220 |
1.66e-31 |
|
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: 115.61 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKATA-----FvpEIP 83
Cdd:cd03219 7 TKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlpPHEIARLgigrtF--QIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 ELDSSLTVKEIL----------FFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:cd03219 85 RLFPELTVLENVmvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 154 LVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:cd03219 165 LLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
35-231 |
1.97e-31 |
|
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: 115.57 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 35 ILGPNGAGKTSVLKAICGLHYQSSG-TVRICG----TEETDEFKKATAFV-PEIPE-LDSSLTVKEILffeaeISG---- 103
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrgGEDVWELRKRIGLVsPALQLrFPRDETVLDVV-----LSGffds 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 104 ----QKKNEADLT-VKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNL 178
Cdd:COG1119 109 iglyREPTDEQRErARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 179 --SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIvkkFNCKNLEEAF 231
Cdd:COG1119 189 aaEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV---LTSENLSEAF 240
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-221 |
2.71e-31 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 121.09 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEipelDSSL---TVKE 93
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqiDPASLRRQIGVVLQ----DVFLfsgTIRE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 -ILFFEAEISgqkkneaDLTVKKAATICGLEEV-------FNKKI----SKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:COG2274 568 nITLGDPDAT-------DEEIIEAARLAGLHDFiealpmgYDTVVgeggSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 162 GLDPAQIASFRKKLKNLSSSMTIIFSTHHiEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:COG2274 641 ALDAETEAIILENLRRLLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
11-209 |
3.08e-31 |
|
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: 114.51 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYG----KFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-------ETDEFKKAT-AF 78
Cdd:cd03255 7 SKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDisklsekELAAFRRRHiGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:cd03255 87 VFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 159 FSAGLDPAQIASFRKKLKNLSSSM--TIIFSTHHiEEAVSMCNRIYIIANGEV 209
Cdd:cd03255 167 PTGNLDSETGKEVMELLRELNKEAgtTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-218 |
3.60e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 115.67 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNY-GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG----TEETDEFKKATAFV 79
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPElDS--SLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLD 157
Cdd:PRK13652 84 FQNPD-DQifSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 158 EFSAGLDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-213 |
8.49e-31 |
|
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: 113.40 E-value: 8.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 7 LISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTeETDEFKKATAFVPEipeld 86
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLGLGGGFNPE----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 ssLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAGlDp 165
Cdd:cd03220 99 --LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEvLAVG-D- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 166 aqiASFRKK----LKNLSS-SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03220 175 ---AAFQEKcqrrLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-158 |
9.50e-31 |
|
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: 111.20 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE----FKKATAFVPEIPELDSSLTVKEILF 96
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDerksLRKEIGYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 97 FEAEISGQKKNEADLTVKKAATICGLEEVFNKKI----SKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-219 |
1.33e-30 |
|
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: 113.02 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE--FKKATA---FVPEIPEL 85
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLpmHKRARLgigYLPQEASI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:cd03218 87 FRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 166 AQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:cd03218 167 IAVQDIQKIIKILKDRgIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
10-218 |
1.93e-30 |
|
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: 112.67 E-value: 1.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 10 FCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD-------EFKKATAFVPEI 82
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkelrKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:cd03258 91 FNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 163 LDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03258 171 LDPETTQSILALLRDINRElgLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-214 |
5.37e-30 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 117.81 E-value: 5.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYaeKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-ET--DEFKKATAFVPEIPELDSSLTVKEILFFE 98
Cdd:TIGR01257 950 NITFY--ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDiETnlDAVRQSLGMCPQHNILFHHLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 AEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNL 178
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*.
gi 2540524722 179 SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGT 214
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-228 |
2.80e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 112.23 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATA---FVPE 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARArigVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:PRK13536 122 FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 162 GLDPAQIASFRKKLKN-LSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK-KFNCKNLE 228
Cdd:PRK13536 202 GLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDeHIGCQVIE 270
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-211 |
7.58e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 109.02 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISF---CKNY----GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETDEFK 73
Cdd:COG1116 1 MSAAAPALELrgvSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-KPVTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 74 KATAFVPEipelDSSL----TVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICK 149
Cdd:COG1116 80 PDRGVVFQ----EPALlpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 150 LPKILVLDE-FSAgLDpAQIasfRKKLKNL------SSSMTIIFSTHHIEEAVSMCNRIYIIAN--GEVAA 211
Cdd:COG1116 156 DPEVLLMDEpFGA-LD-ALT---RERLQDEllrlwqETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-218 |
8.10e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 18 SACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETD-------EFKKATAFVPEIPelDSSL- 89
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKG-EPIKydkksllEVRKTVGIVFQNP--DDQLf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 --TVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQ 167
Cdd:PRK13639 93 apTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 168 IASFRKKLKNLS-SSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK13639 173 ASQIMKLLYDLNkEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-208 |
8.43e-29 |
|
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: 106.70 E-value: 8.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEIPELDSSlTVKEILf 96
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdlDLESLRKNIAYVPQDPFLFSG-TIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 feaeisgqkkneadltvkkaaticgleevfnkkiskLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLK 176
Cdd:cd03228 97 ------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|..
gi 2540524722 177 NLSSSMTIIFSTHHIeEAVSMCNRIYIIANGE 208
Cdd:cd03228 141 ALAKGKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-218 |
1.25e-28 |
|
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: 107.65 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQ-----SSGTVRICGTEETDE-------- 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLdvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 72 ------FKKATAFvpeipeldsSLTVKEILFFEAEISGQKKNEA-DLTVKKAATICGL-EEVFNK-KISKLSKGFKQRTS 142
Cdd:cd03260 81 rrvgmvFQKPNPF---------PGSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 143 LAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-218 |
1.62e-28 |
|
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: 112.30 E-value: 1.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 15 GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-------ETDEFKKATAFVPEIPE--L 85
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrSLRELRRRVQMVFQDPYssL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILFFEAEISGQ-KKNEADLTVKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGL 163
Cdd:COG1123 356 NPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSAL 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 164 DP---AQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG1123 436 DVsvqAQILNLLRDLQR-ELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-218 |
4.68e-28 |
|
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: 111.15 E-value: 4.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQS---SGTVRICGTEETD----EFKKAT 76
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLElseaLRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 77 AFVPEIPelDSSL---TVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:COG1123 86 GMVFQDP--MTQLnpvTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 154 LVLDEFSAGLDPAQIASFRKKLKNLS--SSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-213 |
5.06e-28 |
|
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: 105.33 E-value: 5.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLH--YQSSGTVRICGTEET-DEFKKATAFVPEIPELDSSLTVKEILFF 97
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLINGRPLDkRSFRKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 EAEISGqkkneadltvkkaaticgleevfnkkiskLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKN 177
Cdd:cd03213 106 AAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 2540524722 178 LSSS-MTIIFSTHHI-EEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03213 157 LADTgRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-218 |
1.24e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.93 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISfcKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRIcgtEETDEF------KK 74
Cdd:COG1118 1 MSIEVRNIS--KRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL---NGRDLFtnlpprER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 75 ATAFVPEIPELDSSLTVKE-ILFFeAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAEnIAFG-LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 154 LVLDE-FSAgLDpaqiASFRKKL-KNLSS-----SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG1118 155 LLLDEpFGA-LD----AKVRKELrRWLRRlhdelGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-221 |
4.45e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 108.71 E-value: 4.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEipelDSSL---TVKE 93
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdlTLESLRRQIGVVPQ----DTFLfsgTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 -ILFFEAEISgqkknEADltVKKAATICGLEEVfnkkISKLSKGF---------------KQRTSLAKAICKLPKILVLD 157
Cdd:COG1132 433 nIRYGRPDAT-----DEE--VEEAAKAAQAHEF----IEALPDGYdtvvgergvnlsggqRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 158 EFSAGLDP---AQIasfRKKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:COG1132 502 EATSALDTeteALI---QEALERLMKGRTTIVIAHRL-STIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-209 |
5.37e-27 |
|
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: 103.95 E-value: 5.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT---EETDEFKKATAFV-PEIPELDSSLTVKEI 94
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwKRRKKFLRRIGVVfGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 95 LFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD-PAQiASFRK 173
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvVAQ-ENIRN 194
|
170 180 190
....*....|....*....|....*....|....*...
gi 2540524722 174 KLK--NLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:cd03267 195 FLKeyNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-218 |
7.86e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.14 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETdefKKAT--------AFVPEIPEL 85
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT---GLPPhriarlgiGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILFFEAEISGQKKNEADLtvkkaaticgLEEVF----------NKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:COG0410 90 FPSLTVEENLLLGAYARRDRAEVRAD----------LERVYelfprlkerrRQRAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-232 |
8.92e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 107.90 E-value: 8.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETDEFKKAT---------AFvpeipE 84
Cdd:NF033858 276 FGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-QPVDAGDIATrrrvgymsqAF-----S 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 LDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:NF033858 350 LYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 165 PAQIASFRKKLKNLS--SSMTIIFSTHHIEEAvSMCNRIYIIANGEVAACGTEKEIVKKFNCKNLEEAFI 232
Cdd:NF033858 430 PVARDMFWRLLIELSreDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVAARGAATLEEAFI 498
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
12-223 |
3.54e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.70 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETdefkkATAFVPEipelds 87
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVsallEL-----GAGFHPE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 sLTVKEILFFEAEISGQKKNEADltvKKAATI---CGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAGl 163
Cdd:COG1134 103 -LTGRENIYLNGRLLGLSRKEID---EKFDEIvefAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEvLAVG- 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 164 DpaqiASFRKK----LKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFN 223
Cdd:COG1134 178 D----AAFQKKclarIRELrESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYE 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-211 |
1.01e-25 |
|
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: 98.27 E-value: 1.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGteetdefkkatafvpeipe 84
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 ldssltvKEILFfeaeisgqkkneadLTVKKAATIcGLEEVFnkkisKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:cd03216 62 -------KEVSF--------------ASPRDARRA-GIAMVY-----QLSVGERQMVEIARALARNARLLILDEPTAALT 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2540524722 165 PAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:cd03216 115 PAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
11-219 |
1.14e-25 |
|
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: 100.43 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE--FKKATA---FVPEIPEL 85
Cdd:TIGR04406 8 IKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmHERARLgigYLPQEASI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILffEAEISGQKKNEADLTVKKAATIcgLEE-----VFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFS 160
Cdd:TIGR04406 88 FRKLTVEENI--MAVLEIRKDLDRAEREERLEAL--LEEfqishLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 161 AGLDPAQIASFRKKLKNLSS-SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:TIGR04406 164 AGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIV 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-218 |
1.26e-25 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 100.11 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISfcKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEF--KKATAF 78
Cdd:cd03296 1 MSIEVRNVS--KRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKEILFFEAEI--SGQKKNEADLT--VKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKIL 154
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVkpRSERPPEAEIRakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 155 VLDEFSAGLDpaqiASFRKKLKNL------SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03296 159 LLDEPFGALD----AKVRKELRRWlrrlhdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-209 |
1.96e-25 |
|
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: 98.87 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFcKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-ETDEFKKATAFVPEi 82
Cdd:cd03226 1 RIENISF-SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPiKAKERRKSIGYVMQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 pELDSSL---TVKEILFFEAEISGQKKNEADlTVKKAATICGLEEvfnKKISKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:cd03226 79 -DVDYQLftdSVREELLLGLKELDAGNEQAE-TVLKDLDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 160 SAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-209 |
5.44e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 97.58 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPEL--DsslTVKEI 94
Cdd:COG4619 17 SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmpppEWRRQVAYVPQEPALwgG---TVRDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 95 LFFEAEISGQKKNEADLtvKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQ------ 167
Cdd:COG4619 94 LPFPFQLRERKFDRERA--LELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvee 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2540524722 168 -IASFRKKlknlsSSMTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:COG4619 172 lLREYLAE-----EGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-213 |
5.71e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 98.11 E-value: 5.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGL---HYQSSGTVRICGTE-ETDEFKKATAFVPEIPELDSSLTVKEILF 96
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPrKPDQFQKCVAYVRQDDILLPGLTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEISGQKKNEADLTVKKAATI----CGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFR 172
Cdd:cd03234 104 YTAILRLPRKSSDAIRKKRVEDVllrdLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2540524722 173 KKLKNLSSSMTIIFSTHHI--EEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03234 184 STLSQLARRNRIVILTIHQprSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-221 |
5.89e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 99.04 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEfkkatAFVPEI----------PelDSS 88
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE-----ENLWEIrkkvgmvfqnP--DNQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 L---TVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:TIGR04520 90 FvgaTVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 166 ---AQIASFRKKLKNlSSSMTIIFSTHHIEEAVsMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:TIGR04520 170 kgrKEVLETIRKLNK-EEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
12-218 |
6.10e-25 |
|
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: 98.41 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYG-KFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKA-------TAFVPEIP 83
Cdd:cd03256 8 KTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlrrqIGMIFQQF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 ELDSSLTVKE-IL--------FFEAEISGQKKNEadltvKKAATIC----GLEEVFNKKISKLSKGFKQRTSLAKAICKL 150
Cdd:cd03256 88 NLIERLSVLEnVLsgrlgrrsTWRSLFGLFPKEE-----KQRALAAlervGLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 151 PKILVLDEFSAGLDPA---QIASFRKKLkNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03256 163 PKLILADEPVASLDPAssrQVMDLLKRI-NREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-222 |
1.13e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.39 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETDEFKKATAFV--------PEIPELDS 87
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpFKRRKEFARRIGVVfgqrsqlwWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 SLTVKEILffeaEISgqkKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD-PA 166
Cdd:COG4586 117 FRLLKAIY----RIP---DAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvVS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 167 QIAsFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKF 222
Cdd:COG4586 190 KEA-IREFLKEYNRErgTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-209 |
2.06e-24 |
|
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: 96.44 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE------ETDEFKKATAF 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKltddkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKE-ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLD 157
Cdd:cd03262 81 VFQQFNLFPHLTVLEnITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 158 EFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
11-218 |
2.44e-24 |
|
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: 97.03 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDefKKATA---------FvpE 81
Cdd:COG0411 11 TKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRiarlgiartF--Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKE-----------ILFFEAEIS--GQKKNEADLTvKKAATI---CGLEEVFNKKISKLSKGFKQRTSLAK 145
Cdd:COG0411 87 NPRLFPELTVLEnvlvaaharlgRGLLAALLRlpRARREEREAR-ERAEELlerVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 146 AICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
19-194 |
2.49e-24 |
|
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: 95.57 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETD-------EFKKATAFVPEIPElDS--SL 89
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG-EPLDysrkgllERRQRVGLVFQDPD-DQlfAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 TVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIA 169
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....*.
gi 2540524722 170 SFRKKLKNLSSS-MTIIFSTHHIEEA 194
Cdd:TIGR01166 165 QMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-209 |
2.56e-24 |
|
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: 96.32 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNY-GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATAF----- 78
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 --VPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVL 156
Cdd:cd03292 81 gvVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 157 DEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAgTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-218 |
3.60e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.87 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDefkkatafVPeiPE 84
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--------VP--AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 ------------LDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPK 152
Cdd:PRK09452 85 nrhvntvfqsyaLFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 153 ILVLDE-FSAgLDpaqiASFRKK----LKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK09452 165 VLLLDEsLSA-LD----YKLRKQmqneLKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-213 |
3.68e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.11 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKfSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE----FKKATAFV 79
Cdd:PRK13647 6 EVEDLHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnekwVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPElDS--SLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLD 157
Cdd:PRK13647 85 FQDPD-DQvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 158 EFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:PRK13647 164 EPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-220 |
4.71e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 4.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFCKNYG---KFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD------E 71
Cdd:PRK13637 1 MSIKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvklsD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 72 FKKATAFVPEIPE--LDSSLTVKEILFFEAEIsGQKKNEADLTVKKAATICGL--EEVFNKKISKLSKGFKQRTSLAKAI 147
Cdd:PRK13637 81 IRKKVGLVFQYPEyqLFEETIEKDIAFGPINL-GLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 148 CKLPKILVLDEFSAGLDP-------AQIASFRKKLKnlsssMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPkgrdeilNKIKELHKEYN-----MTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-213 |
2.82e-23 |
|
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: 93.51 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 31 SITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKK--------ATAFVPEIPELDSSLTVKEILFFEAEis 102
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlppqqrKIGLVFQQYALFPHLNVRENLAFGLK-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 103 GQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAgLDPAQIASFRKKLKNLSSS 181
Cdd:cd03297 102 RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEpFSA-LDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|....
gi 2540524722 182 --MTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03297 181 lnIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-219 |
2.92e-23 |
|
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: 94.63 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKA--------TAFVPEIP 83
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 ELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAg 162
Cdd:cd03294 112 ALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEaFSA- 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 163 LDPAQIASFRKKLKNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:cd03294 191 LDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-218 |
3.32e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 3.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISfcKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKK--ATAF 78
Cdd:PRK10851 1 MSIEIANIK--KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARdrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAAT----ICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKIL 154
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTqlleMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 155 VLDE-FSAgLDpAQI-ASFRKKLKNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK10851 159 LLDEpFGA-LD-AQVrKELRRWLRQLHEELkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-211 |
4.33e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET-DEFKKATAF- 78
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 ---VPEIPELDSSLTVKE--ILFFEaEISGQKKNEADLTvKKAATIC---GLEEVFNKKISKLSKGFKQRTSLAKAICKL 150
Cdd:COG3845 82 igmVHQHFMLVPNLTVAEniVLGLE-PTKGGRLDRKAAR-ARIRELSeryGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 151 PKILVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLRRGKVVG 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-208 |
4.81e-23 |
|
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: 92.53 E-value: 4.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTeetdefkkaTAFVPEIPELDSSlTVKE-ILFfea 99
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS---------IAYVSQEPWIQNG-TIREnILF--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 100 eisGQKKNEADLtvKKAATICGLE------------EVFNKKISkLSKGFKQRTSLAKAICKLPKILVLDE-FSAgLDpA 166
Cdd:cd03250 89 ---GKPFDEERY--EKVIKACALEpdleilpdgdltEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDpLSA-VD-A 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2540524722 167 QIAS------FRKKLKNLSssmTIIFSTHHIeEAVSMCNRIYIIANGE 208
Cdd:cd03250 161 HVGRhifencILGLLLNNK---TRILVTHQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
7.83e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 7.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 2 SNEVELISFCKNYGKFS-ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVrICGTEETD-------EFK 73
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDysrkglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 74 KATAFVPEIPELD-SSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPK 152
Cdd:PRK13636 82 ESVGMVFQDPDNQlFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 153 ILVLDEFSAGLDPAQIASFRKKLKNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-220 |
5.07e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 91.62 E-value: 5.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEETD-EFKKATAFVPEIPelDSSL---TV 91
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlSEETVwDVRRQVGMVFQNP--DNQFvgaTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 92 KEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP---AQI 168
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPrgrREV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 169 ASFRKKLKNlSSSMTIIFSTHHIEEAVSmCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK13635 180 LETVRQLKE-QKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
11-220 |
7.66e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.09 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE--FKKATA---FVPEipel 85
Cdd:COG1137 10 VKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRARLgigYLPQ---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSS----LTVKE----ILffeaEISGQKKNEADltvKKAATIC---GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKIL 154
Cdd:COG1137 86 EASifrkLTVEDnilaVL----ELRKLSKKERE---ERLEELLeefGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 155 VLDE-FsAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:COG1137 159 LLDEpF-AGVDPIAVADIQKIIRHLKERgIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-213 |
2.83e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.86 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNeVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKATAF 78
Cdd:PRK11000 1 MAS-VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvpPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 159 FSAGLDPA-------QIASFRKKLKNlsssmTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:PRK11000 160 PLSNLDAAlrvqmriEISRLHKRLGR-----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-221 |
1.22e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFK--------KATAFVPEIPEldSSL---T 90
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikqirKKVGLVFQFPE--SQLfeeT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 91 VKEILFFEAEISGQKKNEADLTVKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQia 169
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG-- 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 170 sfRKKLKNL-----SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13649 181 --RKELMTLfkklhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-214 |
2.12e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.75 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSLTVKEILF 96
Cdd:PRK13548 19 DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRRAVLPQHSSLSFPFTVEEVVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKL------PKILVLDEFSAGLDPA-QIA 169
Cdd:PRK13548 99 MGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLwepdgpPRWLLLDEPTSALDLAhQHH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2540524722 170 SFRkKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGT 214
Cdd:PRK13548 179 VLR-LARQLAHErgLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
8-214 |
2.54e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 87.85 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 8 ISFCKNYGKFSAckNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT----EETDEF----KKATAFV 79
Cdd:COG4148 5 VDFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFlpphRRRIGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPELDSSLTVKEILFFeaeisGQK---KNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVL 156
Cdd:COG4148 83 FQEARLFPHLSVRGNLLY-----GRKrapRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 157 DEFSAGLDPAqiasfRKK-----LKNLSS--SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGT 214
Cdd:COG4148 158 DEPLAALDLA-----RKAeilpyLERLRDelDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-221 |
5.96e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEetdeFKKAT---------AFVP- 80
Cdd:COG1129 11 SKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP----VRFRSprdaqaagiAIIHq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 81 E---IPELdsslTVKEILFFEAEISG-----QKKneadlTVKKAATIC---GLEEVFNKKISKLSKGFKQRTSLAKAICK 149
Cdd:COG1129 87 ElnlVPNL----SVAENIFLGREPRRgglidWRA-----MRRRARELLarlGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 150 LPKILVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACG-----TEKEIVKK 221
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGpvaelTEDELVRL 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-223 |
6.12e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRI-----CGTEETDEFK---KATAFVPEIPE--LDSSLTV 91
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvSSTSKQKEIKpvrKKVGVVFQFPEsqLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 92 KEILFFEAEIsGQKKNEADLTVKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIAS 170
Cdd:PRK13643 104 KDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 171 FRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFN 223
Cdd:PRK13643 183 MMQLFESIhQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
12-233 |
8.89e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.95 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET-----DEFKKATAFVPEIPELD 86
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 SSLTVKEILFFEAEI-----SGQKKNEADLTVKKAAticgLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:PRK10895 91 RRLSVYDNLMAVLQIrddlsAEQREDRANELMEEFH----IEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 162 GLDPAQIASFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFNCKN--LEEAFIL 233
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLrDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRvyLGEDFRL 241
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-209 |
1.09e-19 |
|
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: 83.03 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET----DEFKKATAFVPEipeldssltvkEILF 96
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwdpNELGDHVGYLPQ-----------DDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEIsgqkkneadltvkkAATIcgleevfnkkiskLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLK 176
Cdd:cd03246 88 FSGSI--------------AENI-------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....
gi 2540524722 177 NLSSS-MTIIFSTHHIeEAVSMCNRIYIIANGEV 209
Cdd:cd03246 141 ALKAAgATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-213 |
1.09e-19 |
|
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: 83.70 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 28 EKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET--DEFKKATAFVPEIPELDSSLTVKEILFFeAEISGQK 105
Cdd:cd03298 22 AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaaPPADRPVSMLFQENNLFAHLTVEQNVGL-GLSPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 106 KNEADL-TVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAqiasFRKKLKNLSSS--- 181
Cdd:cd03298 101 LTAEDRqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPA----LRAEMLDLVLDlha 176
|
170 180 190
....*....|....*....|....*....|....*
gi 2540524722 182 ---MTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03298 177 etkMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-192 |
1.75e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.47 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHY--QSSGTVRIcgteETDEFKKATAFVPEIPELDSSLTVKEILffe 98
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV----PDNQFGREASLIDAIGRKGDFKDAVELL--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 aeisgqkkneadltvkkaaTICGLEEVFN--KKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP--AQIAS--FR 172
Cdd:COG2401 120 -------------------NAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqtAKRVArnLQ 180
|
170 180
....*....|....*....|
gi 2540524722 173 KKLKNLssSMTIIFSTHHIE 192
Cdd:COG2401 181 KLARRA--GITLVVATHHYD 198
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-221 |
2.24e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.47 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGL---HYQSSGTVRICGTEETD----EFKKAT 76
Cdd:PRK13640 7 EFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAktvwDIREKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 77 AFVPEIPelDSSL---TVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:PRK13640 87 GIVFQNP--DNQFvgaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 154 LVLDEFSAGLDPA---QIASFRKKLKNlSSSMTIIFSTHHIEEAvSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13640 165 IILDESTSMLDPAgkeQILKLIRKLKK-KNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-218 |
2.67e-19 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 84.85 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 15 GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET----DEFKKATAFVPEIPE---LDS 87
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRKARRQIGMIFQhfnLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 SLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQ 167
Cdd:PRK11153 96 SRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 168 IASFRKKLKNLSS--SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK11153 176 TRSILELLKDINRelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
13-209 |
3.22e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 13 NYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE-----FKKATAFVPEIPELDS 87
Cdd:PRK11614 14 HYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqtakiMREAVAIVPEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 SLTVKEIL----FFEAEISGQKKNEA--DLTVKkaaticgLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:PRK11614 94 RMTVEENLamggFFAERDQFQERIKWvyELFPR-------LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2540524722 162 GLDPAQIASFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLrEQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-171 |
4.19e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.23 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD-EFKKATAFVPEIPELDSSLTVKEILFFEA 99
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 100 EISGQkkneADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASF 171
Cdd:PRK13539 99 AFLGG----EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-221 |
5.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 83.21 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE-----FKKATAFVPEIPelDSSLT--- 90
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenlwdIRNKAGMVFQNP--DNQIVati 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 91 VKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPA---Q 167
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSgrrE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 168 IASFRKKLkNLSSSMTIIFSTHHIEEAVSmCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13633 183 VVNTIKEL-NKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
14-211 |
8.03e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 81.72 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSacKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE----------FKKATAFvpeip 83
Cdd:COG3840 11 YGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaerpvsmlFQENNLF----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 eldSSLTVkeilffEAEI-----SGQKKNEADLT-VKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAIC-KLPkILVL 156
Cdd:COG3840 84 ---PHLTV------AQNIglglrPGLKLTAEQRAqVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVrKRP-ILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 157 DE-FSAgLDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:COG3840 154 DEpFSA-LDPALRQEMLDLVDELCRErgLTVLMVTHDPEDAARIADRVLLVADGRIAA 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-218 |
1.09e-18 |
|
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: 81.74 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETDEFKKATAFVPEIPELDSSLTVKE--ILFFE 98
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGPDRMVVFQNYSLLPWLTVREniALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 AEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNL 178
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2540524722 179 --SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:TIGR01184 161 weEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
21-231 |
1.18e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 82.09 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETDEFKKAT-----AFVPEIPELDSSLTVKEIL 95
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG-RPLAAWSPWElarrrAVLPQHSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 96 FFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKL-------PKILVLDEFSAGLDPA-Q 167
Cdd:COG4559 97 ALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLwepvdggPRWLFLDEPTSALDLAhQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 168 IASFRkKLKNLSSSMTIIFST-HHIEEAVSMCNRIYIIANGEVAACGTEKEIvkkFNCKNLEEAF 231
Cdd:COG4559 177 HAVLR-LARQLARRGGGVVAVlHDLNLAAQYADRILLLHQGRLVAQGTPEEV---LTDELLERVY 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
21-223 |
2.06e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 81.70 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE----FKKATAFVPEIPelDSSL---TVKE 93
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdIRHKIGMVFQNP--DNQFvgaTVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRK 173
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 174 KLKNLSSS--MTIIFSTHHIEEaVSMCNRIYIIANGEVAACGTEKEIVKKFN 223
Cdd:PRK13650 182 TIKGIRDDyqMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
34-213 |
2.61e-18 |
|
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: 80.33 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 34 GILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEIPELDSSlTVKE-ILFFEAEISgqkkne 108
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDirqlDPADLRRNIGYVPQDVTLFYG-TLRDnITLGAPLAD------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 109 aDLTVKKAATICGLEEVFNK-------KISK----LSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKN 177
Cdd:cd03245 107 -DERILRAAELAGVTDFVNKhpngldlQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQ 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 2540524722 178 LSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03245 186 LLGDKTLIIITHRP-SLLDLVDRIIVMDSGRIVADG 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-219 |
2.64e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 80.91 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD------EFKKATAF 78
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvderLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKE-ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLD 157
Cdd:PRK09493 82 VFQQFYLFPHLTALEnVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 158 EFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-218 |
4.58e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.44 E-value: 4.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSL 89
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlssrQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 TVKEI--------LFFEAEISGQKKNeadlTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:PRK11231 92 TVRELvaygrspwLSLWGRLSAEDNA----RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 162 GLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-218 |
5.09e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.27 E-value: 5.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGL-----HYQSSGTVRICG----TEETD- 70
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrniySPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 71 -EFKKATAFVPEIPELDSSLTVKEILFFEAEISG--QKKNEADLTV----KKAATICGLEEVFNKKISKLSKGFKQRTSL 143
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVewalKKAALWDEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 144 AKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
21-221 |
7.19e-18 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 79.58 E-value: 7.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEipelDSSLTVKEILF 96
Cdd:cd03253 18 KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevTLDSLRRAIGVVPQ----DTVLFNDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 feaEISGQKKNEADLTVKKAATICGLEEV---FNKKIS--------KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:cd03253 94 ---NIRYGRPDATDEEVIEAAKAAQIHDKimrFPDGYDtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 166 AQIASFRKKLKNLSSSMTIIFSTHHIEEAVSmCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:cd03253 171 HTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
19-221 |
1.10e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.06 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFK--------KATAFVPEIPEldSSL- 89
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklkplrKKVGIVFQFPE--HQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 --TV-KEILF----FeaeisGQKKNEADLTVKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:PRK13634 100 eeTVeKDICFgpmnF-----GVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 162 GLDPaqiaSFRKKLKNLSSS------MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13634 175 GLDP----KGRKEMMEMFYKlhkekgLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-220 |
1.10e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.65 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE-FKKATAFVPEI 82
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 ---PelDSS---LTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVL 156
Cdd:PRK13632 89 fqnP--DNQfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 157 DEFSAGLDP---AQIASFRKKLKNlSSSMTIIFSTHHIEEAVsMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK13632 167 DESTSMLDPkgkREIKKIMVDLRK-TRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILN 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-223 |
1.16e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.53 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNE--VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEF--KKAT 76
Cdd:PRK11432 1 MTQKnfVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 77 AFVPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVL 156
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 157 DEFSAGLDPAQIASFRKKLKNLSSSMTI--IFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFN 223
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
9-218 |
1.45e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.12 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 9 SFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD-------EFKKATAFVPE 81
Cdd:COG1135 10 TFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserelrAARRKIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:COG1135 90 HFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 162 GLDP---AQI----ASFRKKLkNLsssmTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG1135 170 ALDPettRSIldllKDINREL-GL----TIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
34-222 |
1.50e-17 |
|
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: 81.60 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 34 GILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE---ETDEFKKATAFVPEIPELDSSLTVKEILFFEAEISGQKKNEAD 110
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiltNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIE 2048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 111 LTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQiasfRKKLKNLSSSM-----TII 185
Cdd:TIGR01257 2049 KVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA----RRMLWNTIVSIiregrAVV 2124
|
170 180 190
....*....|....*....|....*....|....*..
gi 2540524722 186 FSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKF 222
Cdd:TIGR01257 2125 LTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKF 2161
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
4-221 |
1.55e-17 |
|
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: 78.42 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKfSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFV 79
Cdd:cd03254 4 EFENVNFSYDEKK-PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisrkSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPELDSSlTVKE-ILFFEAEISGQKKNEADLTVKKAATIC----GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKIL 154
Cdd:cd03254 83 LQDTFLFSG-TIMEnIRLGRPNATDEEVIEAAKEAGAHDFIMklpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 155 VLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHH---IEEAvsmcNRIYIIANGEVAACGTEKEIVKK 221
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRlstIKNA----DKILVLDDGKIIEEGTHDELLAK 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
5-227 |
1.60e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKfSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD-----EFKKATAFV 79
Cdd:PRK13644 4 LENVSYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsklqGIRKLVGIV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPELD-SSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:PRK13644 83 FQNPETQfVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 159 FSAGLDPAQIASFRKKLKNL-SSSMTIIFSTHHIEEaVSMCNRIYIIANGEVAACGTEKEIVKKFNCKNL 227
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-209 |
2.08e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.79 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 8 ISF---CKNY-GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETDEFKKAtafvpEIP 83
Cdd:COG2884 2 IRFenvSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG-QDLSRLKRR-----EIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 EL---------D----SSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKL 150
Cdd:COG2884 76 YLrrrigvvfqDfrllPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 151 PKILVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-219 |
2.95e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 79.69 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-------ETDEFK-KATAFVPEIPELDSSLTVK 92
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakisdaELREVRrKKIAMVFQSFALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 93 EILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFR 172
Cdd:PRK10070 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2540524722 173 KKLKNLSS--SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:PRK10070 205 DELVKLQAkhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-225 |
3.69e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.49 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKATAFVPEI 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvpPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 163 LDpaqiasfrKKLKNLSS----------SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFNCK 225
Cdd:PRK11607 180 LD--------KKLRDRMQlevvdilervGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-218 |
4.13e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.65 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGL-----HYQSSGTVRICGTE----ETDEFKKATAFVPEIPE 84
Cdd:PRK14247 13 FGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDifkmDVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 LDSSLTVKEILFFEAEISGQKKNEADLT--VKKAATICGL-EEVFNK---KISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLVKSKKELQerVRWALEKAQLwDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 159 FSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-218 |
4.61e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 4.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGL------HYQSSGTVRICGTE----ETDEFKKATAFVPEIPELDSSLT 90
Cdd:PRK14246 27 KDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDifqiDAIKLRKEVGMVFQQPNPFPHLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 91 VKEILFFEAEISGQK-KNEADLTVKKAATICGL-EEVF---NKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:PRK14246 107 IYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYdrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDI 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 166 AQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK14246 187 VNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-231 |
7.23e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 18 SACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKA-TAFVPEIPELDSSLTVkeiLF 96
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNlVAYVPQSEEVDWSFPV---LV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEISGQ---------KKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD--- 164
Cdd:PRK15056 98 EDVVMMGRyghmgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDvkt 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 165 PAQIASFRKKLKNLSSSMTIifSTHHIEEAVSMCNRIYIIaNGEVAACG-TEkeivKKFNCKNLEEAF 231
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLV--STHNLGSVTEFCDYTVMV-KGTVLASGpTE----TTFTAENLELAF 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-222 |
1.09e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.55 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 10 FCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLH---YQSSGTVRICGTE-ETDEFKKATAFVPEIPEL 85
Cdd:TIGR00955 31 FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPiDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILFFEAEI------SGQKKNEA------DLTVKKAA-TICGLEEvfnkKISKLSKGFKQRTSLAKAICKLPK 152
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLrmprrvTKKEKRERvdevlqALGLRKCAnTRIGVPG----RVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 153 ILVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHH-IEEAVSMCNRIYIIANGEVAACGTEKEIVKKF 222
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQAVPFF 258
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-231 |
1.72e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.57 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 23 INFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG--TEETD--EFKKATAFVPEIPELDSSLTVKEILffe 98
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddVEALSarAASRRVASVPQDTSLSFEFDVRQVV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 aEIsGQ--------KKNEADLT-VKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD-PAQI 168
Cdd:PRK09536 99 -EM-GRtphrsrfdTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 169 ASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVkkfNCKNLEEAF 231
Cdd:PRK09536 177 RTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL---TADTLRAAF 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
14-232 |
1.86e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.86 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKAT-----AFVPE------I 82
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvcpriAYMPQglgknlY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PEldssLTVKE-ILFFeAEISGQKKNE-----ADLTvkkAATicGLEEVFNKKISKLSKGFKQRTSLAkaiCKL---PKI 153
Cdd:NF033858 91 PT----LSVFEnLDFF-GRLFGQDAAErrrriDELL---RAT--GLAPFADRPAGKLSGGMKQKLGLC---CALihdPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 154 LVLDEFSAGLDP---AQ----IASFRKKlknlSSSMTIIFSTHHIEEA------VSMcnriyiiANGEVAACGTEKEIVK 220
Cdd:NF033858 158 LILDEPTTGVDPlsrRQfwelIDRIRAE----RPGMSVLVATAYMEEAerfdwlVAM-------DAGRVLATGTPAELLA 226
|
250
....*....|..
gi 2540524722 221 KFNCKNLEEAFI 232
Cdd:NF033858 227 RTGADTLEAAFI 238
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
14-218 |
2.51e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.58 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGL-----HYQSSGTVRICG------TEETDEFKKATAFVPEI 82
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGhniyspRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PElDSSLTVKEILFFEAEISGQK-KNEADLTVK---KAATIcgLEEVFNKKISK---LSKGFKQRTSLAKAICKLPKILV 155
Cdd:PRK14239 95 PN-PFPMSIYENVVYGLRLKGIKdKQVLDEAVEkslKGASI--WDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-214 |
4.23e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 74.45 E-value: 4.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSlTVKEILF 96
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiglhDLRSRISIIPQDPVLFSG-TIRSNLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEISgqkkneaDLTVKKAATICGLEEVFNKKISKL-----------SKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:cd03244 100 PFGEYS-------DEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEATASVDP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2540524722 166 AQIASFRKKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGT 214
Cdd:cd03244 173 ETDALIQKTIREAFKDCTVLTIAHRL-DTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
19-221 |
4.42e-16 |
|
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: 76.73 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEIPELDSSlTVKE- 93
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlrdlDEDDLRRRIAVVPQRPHLFDT-TLREn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ILFFEAEISgqkknEADLtvKKAATICGLEEVFNKKI-----------SKLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:COG4987 429 LRLARPDAT-----DEEL--WAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 163 LDPAQIASFRKKLKNLSSSMTIIFSTHHiEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:COG4987 502 LDAATEQALLADLLEALAGRTVLLITHR-LAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-190 |
6.78e-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: 73.16 E-value: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT---EETDEFKKATAFVPEIPELDSSLTVKEILFFE 98
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 AEISGqkknEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLK-N 177
Cdd:TIGR01189 98 AAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRaH 173
|
170
....*....|...
gi 2540524722 178 LSSSMTIIFSTHH 190
Cdd:TIGR01189 174 LARGGIVLLTTHQ 186
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-214 |
1.51e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFckNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG-----TEETDE---- 71
Cdd:PRK11124 1 MSIQLNGINC--FYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfSKTPSDkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 72 -FKKATAFVPEIPELDSSLTVKEILfFEA--EISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAIC 148
Cdd:PRK11124 79 eLRRNVGMVFQQYNLWPHLTVQQNL-IEApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 149 KLPKILVLDEFSAGLDP---AQIASFRKKLKNlsSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGT 214
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPeitAQIVSIIRELAE--TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-223 |
1.53e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNS-ITgILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD--EFKKA-------------TAfvpei 82
Cdd:COG1101 21 ALDGLNLTIEEGDfVT-VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlpEYKRAkyigrvfqdpmmgTA----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 peldSSLTVKEILFFeAEISGQK--------KNEADLTVKKAATI-CGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:COG1101 95 ----PSMTIEENLAL-AYRRGKRrglrrgltKKRRELFRELLATLgLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 154 LVLDEFSAGLDP---AQIASFRKKL---KNLSSSMTiifsTHHIEEAVSMCNRIYIIANGEVA--ACGTEKE------IV 219
Cdd:COG1101 170 LLLDEHTAALDPktaALVLELTEKIveeNNLTTLMV----THNMEQALDYGNRLIMMHEGRIIldVSGEEKKkltvedLL 245
|
....
gi 2540524722 220 KKFN 223
Cdd:COG1101 246 ELFE 249
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-220 |
1.60e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 73.97 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 17 FSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEfKKATAFVPEIPELDSSLT------ 90
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNK-KKTKEKEKVLEKLVIQKTrfkkik 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 91 -VKEI------LF-------FEAEIS----------GQKKNEADLTVKKAATICGLEEVFNKKIS-KLSKGFKQRTSLAK 145
Cdd:PRK13651 99 kIKEIrrrvgvVFqfaeyqlFEQTIEkdiifgpvsmGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRRVALAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 146 AICKLPKILVLDEFSAGLDPAQIASFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
11-231 |
4.17e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.04 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEIPELD 86
Cdd:COG4604 8 SKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvattPSRELAKRLAILRQENHIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 SSLTVKEILFFeaeisGQ------KKNEADLT-VKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:COG4604 88 SRLTVRELVAF-----GRfpyskgRLTAEDREiIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 160 SAGLDPAQIASFRKKLKNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKfncKNLEEAF 231
Cdd:COG4604 163 LNNLDMKHSVQMMKLLRRLADELgkTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITP---EVLSDIY 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-210 |
4.49e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 71.29 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKF--SACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATA 77
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDistiPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 78 FVPEIPELDSSlTVKEILFFEAEISGQKKNEAdLTVKKAAticgleevfnkkiSKLSKGFKQRTSLAKAICKLPKILVLD 157
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLDPFDEYSDEEIYGA-LRVSEGG-------------LNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 158 EFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVA 210
Cdd:cd03369 151 EATASIDYATDALIQKTIREEFTNSTILTIAHRL-RTIIDYDKILVMDAGEVK 202
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-213 |
6.16e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 6.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETdEFKKATA------F 78
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-RLTPAKAhqlgiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKE-ILFfeaEISGQKKNEADLTVKKAATICGLE--------EVFNKKISKLSKGFkQRTSlakaick 149
Cdd:PRK15439 91 VPQEPLLFPNLSVKEnILF---GLPKRQASMQKMKQLLAALGCQLDldssagslEVADRQIVEILRGL-MRDS------- 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 150 lpKILVLDEFSAGLDPAQIASFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:PRK15439 160 --RILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSG 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-209 |
1.35e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 71.28 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFckNYGKFSACKNIN---FYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE----FKKAT 76
Cdd:PRK13642 6 EVENLVF--KYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvwnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 77 AFVPEIPELD-SSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:PRK13642 84 GMVFQNPDNQfVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSmCNRIYIIANGEV 209
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-207 |
1.70e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.50 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE-FKKATAFVPE--IPELDs 87
Cdd:PRK11248 8 YADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgAERGVVFQNEglLPWRN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 sltVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpaq 167
Cdd:PRK11248 87 ---VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD--- 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2540524722 168 iASFRKKLKNL------SSSMTIIFSTHHIEEAVSMCNRIYIIANG 207
Cdd:PRK11248 161 -AFTREQMQTLllklwqETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-218 |
2.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.42 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 16 KFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVrICG----------TEETDEFKKATAFVPEIPE- 84
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGdyaipanlkkIKEVKRLRKEIGLVFQFPEy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 -LDSSLTVKEILFFEAEIsGQKKNEADLTVKKAATICGLEEVFNKKIS-KLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:PRK13645 102 qLFQETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 163 LDPAQIASFRKKLKNLSSSMT--IIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
21-209 |
2.82e-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: 70.27 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYqSSGTVRICG----TEETDEFKKATAFVPEipeldssltvkEILF 96
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswnSVPLQKWRKAFGVIPQ-----------KVFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEIS------GQKKNEADLTVKKAATICGLEEVFNKKIS--------KLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:cd03289 89 FSGTFRknldpyGKWSDEEIWKVAEEVGLKSVIEQFPGQLDfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2540524722 163 LDPAQIASFRKKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEV 209
Cdd:cd03289 169 LDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-221 |
3.49e-14 |
|
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: 69.44 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG----TEETDEFKKATAFVPEIPELDSSLTVKEILF 96
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaLADPAWLRRQVGVVLQENVLFNRSIRDNIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEISGQKKNEADLTVKKAATICGLEEVFNKKI----SKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFR 172
Cdd:cd03252 99 ADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIM 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2540524722 173 KKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:cd03252 179 RNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-220 |
3.60e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.24 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG---TEET-----DEFKKATAFVPEIPEldSSL---T 90
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETgnknlKKLRKKVSLVFQFPE--AQLfenT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 91 VKEILFFEAEISGQKKNEADLTVKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIA 169
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 170 SFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK13641 183 EMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
14-218 |
3.95e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 69.68 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLH-----YQSSGTVRICGTE----ETDE----------FKK 74
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlipgARVEGEILLDGEDiydpDVDVvelrrrvgmvFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 75 ATAFvpeiPeldssLTVKEILFFEAEISGQK-KNEADLTVKKAATICGL-EEV---FNKKISKLSKGFKQRTSLAKAICK 149
Cdd:COG1117 101 PNPF----P-----KSIYDNVAYGLRLHGIKsKSELDEIVEESLRKAALwDEVkdrLKKSALGLSGGQQQRLCIARALAV 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 150 LPKILVLDEFSAGLDPaqIASFR--KKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:COG1117 172 EPEVLLMDEPTSALDP--ISTAKieELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQI 240
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-209 |
4.33e-14 |
|
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: 68.44 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLH---YQSSGTVRICGtEETDEFKKA----TAFVPEIPE 84
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNG-IPYKEFAEKypgeIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 LDSSLTVKEILFFEAEISGqkkneadltvkkaaticgleevfNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:cd03233 94 HFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2540524722 165 PAQIASFRKKLKNLS--SSMTIIFSTHHI-EEAVSMCNRIYIIANGEV 209
Cdd:cd03233 151 SSTALEILKCIRTMAdvLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQ 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
35-190 |
4.91e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 68.29 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 35 ILGPNGAGKTSVLKAICGLHYQSSGTVRICGT---EETDEFKKATAFVPEIPELDSSLTVKEILFFEAEISGqkkneaDL 111
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpldFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHS------DE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 112 TVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLK-NLSSSMTIIFSTHH 190
Cdd:cd03231 105 QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAgHCARGGMVVLTTHQ 184
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-229 |
5.21e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGtEETDEFKK---------ATAFV-PE----IPELD 86
Cdd:PRK13638 18 KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRgllalrqqvATVFQdPEqqifYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 S--SLTVKEILFFEAEISGQkkneadltVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:PRK13638 97 SdiAFSLRNLGVPEAEITRR--------VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 165 PA---QIASFRKKLknLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIvkkFNCKNLEE 229
Cdd:PRK13638 169 PAgrtQMIAIIRRI--VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV---FACTEAME 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-218 |
5.26e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.88 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRI-----------------CGTEETDEFK- 73
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelitnPYSKKIKNFKe 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 74 --KATAFVPEIPE--LDSSLTVKEILFFEAEIsGQKKNEADLTVKKAATICGLEEVF-NKKISKLSKGFKQRTSLAKAIC 148
Cdd:PRK13631 114 lrRRVSMVFQFPEyqLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSYlERSPFGLSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 149 KLPKILVLDEFSAGLDPA-QIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKgEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-221 |
5.56e-14 |
|
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: 68.80 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEIPELDSSlTVKEilf 96
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdyTLASLRRQIGLVSQDVFLFND-TVAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 feaEISGQKKNEADLTVKKAAT-------ICGLEEVFNKKI----SKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:cd03251 95 ---NIAYGRPGATREEVEEAARaanahefIMELPEGYDTVIgergVKLSGGQRQRIAIARALLKDPPILILDEATSALDT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 166 AQIASFRKKLKNLSSSMTIIFSTHH---IEEAvsmcNRIYIIANGEVAACGTEKEIVKK 221
Cdd:cd03251 172 ESERLVQAALERLMKNRTTFVIAHRlstIENA----DRIVVLEDGKIVERGTHEELLAQ 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-211 |
6.00e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 6.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET-----DEFKKATAFVPE-------IPELD-- 86
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprDAIRAGIAYVPEdrkgeglVLDLSir 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 -----SSLTVKEILFFeaeISGQKKNEA------DLTVKkAATIcgleevfNKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:COG1129 349 enitlASLDRLSRGGL---LDRRRERALaeeyikRLRIK-TPSP-------EQPVGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:COG1129 418 LDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-210 |
6.54e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 24 NFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE----------FKKATAFvpeipeldSSLTVke 93
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsrrpvsmlFQENNLF--------SHLTV-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ilffEAEIS-----GQKKNEAD-LTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAgLDPA 166
Cdd:PRK10771 89 ----AQNIGlglnpGLKLNAAQrEKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEpFSA-LDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2540524722 167 qiasFRKKLKNLSSS------MTIIFSTHHIEEAVSMCNRIYIIANGEVA 210
Cdd:PRK10771 164 ----LRQEMLTLVSQvcqerqLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-164 |
8.53e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVricgtEETDEFKkaTAFVP 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----KRNGKLR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 81 EIPELDSS--LTVKEILFFEAeisgqkkneadlTVKKAATICGLEEV-----FNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:PRK09544 74 QKLYLDTTlpLTVNRFLRLRP------------GTKKEDILPALKRVqaghlIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 2540524722 154 LVLDEFSAGLD 164
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-219 |
1.43e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPEIPELDSSL 89
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHiqhyASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 TVKEIL----FFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:PRK10253 97 TVQELVargrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 166 AQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:PRK10253 177 SHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-231 |
1.70e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.56 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 23 INFYAEKNSITGILGPNGAGKTSVLKAICGLhYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSLTVKEILFFe 98
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDwsaaELARHRAYLSQQQSPPFAMPVFQYLAL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 aeisGQKKNEADLTVKKA-ATIC---GLEEVFNKKISKLSKGFKQRTSLAKAICKL-------PKILVLDEFSAGLDPAQ 167
Cdd:COG4138 93 ----HQPAGASSEAVEQLlAQLAealGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVwptinpeGQLLLLDEPMNSLDVAQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 168 IASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKfncKNLEEAF 231
Cdd:COG4138 169 QAALDRLLRELCQQgITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTP---ENLSEVF 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-208 |
2.14e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.70 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLH---------YQSSGTVRICGTEETDEfkKATAFVPEI 82
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgeiYWSGSPLKASNIRDTER--AGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEAEIS--GQKKNEADLTVKKAATicgLEEV------FNKKISKLSKGFKQRTSLAKAICKLPKIL 154
Cdd:TIGR02633 87 LTLVPELSVAENIFLGNEITlpGGRMAYNAMYLRAKNL---LRELqldadnVTRPVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 155 VLDEFSAGLDPAQIASFRKKLKNLSS-SMTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-220 |
2.83e-13 |
|
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: 68.61 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKfSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFV 79
Cdd:TIGR01193 475 VINDVSYSYGYGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDidrhTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPELDSSLTVKEILFfeaeisGQKKNEADLTVKKAATIC-----------GLEEVFNKKISKLSKGFKQRTSLAKAIC 148
Cdd:TIGR01193 554 PQEPYIFSGSILENLLL------GAKENVSQDEIWAACEIAeikddienmplGYQTELSEEGSSISGGQKQRIALARALL 627
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 149 KLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSmTIIFSTHHIEEAvSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:TIGR01193 628 TDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDELLD 697
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-189 |
3.40e-13 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.73 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQS--SGTVRICGTEETDEFKKATAFVPEIPELDSSLTVKEILFFE 98
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTVREALRFS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 AEISGqkkneadltvkkaaticgleevfnkkiskLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNL 178
Cdd:cd03232 104 ALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170
....*....|..
gi 2540524722 179 SSS-MTIIFSTH 189
Cdd:cd03232 155 ADSgQAILCTIH 166
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-164 |
3.97e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET----DEFKKATAFVPEIPELDSSlTVKEILFF 97
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlkpEIYRQQVSYCAQTPTLFGD-TVYDNLIF 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 98 EAEISGQKKNEADLtVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:PRK10247 104 PWQIRNQQPDPAIF-LDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-209 |
4.14e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.96 E-value: 4.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 1 MSNEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGL---------HYQSSGTVRICGTEETDE 71
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagsHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 72 FKKA---TAFVPEIPELDSSLTVKEILFFEA------------EISGQKKNEAdltvKKAATICGLEEVFNKKISKLSKG 136
Cdd:PRK09984 81 IRKSranTGYIFQQFNLVNRLSVLENVLIGAlgstpfwrtcfsWFTREQKQRA----LQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 137 FKQRTSLAKAICKLPKILVLDEFSAGLDP--AQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPesARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-220 |
7.18e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.18 E-value: 7.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 20 CKNINFYAEKNSITGILGPNGAGKTSVLKAICG-LHYQssGTVRICGTEETD----EFKKATAFVPEIPELDSSlTVKE- 93
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGfLPYQ--GSLKINGIELREldpeSWRKHLSWVGQNPQLPHG-TLRDn 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ILFFEAEISGQKKNEAdltVKKA-------ATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpA 166
Cdd:PRK11174 443 VLLGNPDASDEQLQQA---LENAwvseflpLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD-A 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 167 QiaSFRK---KLKNLSSSMTIIFSTHHIEEaVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK11174 519 H--SEQLvmqALNAASRRQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
12-208 |
8.69e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGL--HYQSSGTVRICGTE-------ETDE-----FKKATA 77
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEElqasnirDTERagiaiIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 78 FVPEipeldssLTVKEILFFEAEISGQKKNEADLTVKKAATIcgLEEV-----FNKKISKLSKGFKQRTSLAKAICKLPK 152
Cdd:PRK13549 93 LVKE-------LSVLENIFLGNEITPGGIMDYDAMYLRAQKL--LAQLkldinPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 153 ILVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAHgIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
14-218 |
9.60e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.78 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE---------------ETDE----FKK 74
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpghqiarmgvvRTFQhvrlFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 75 ATA----FVPEIPELDSSL---TVKEILFFEAEisgqkkNEAdltVKKAAT---ICGLEEVFNKKISKLSKGFKQRTSLA 144
Cdd:PRK11300 95 MTVienlLVAQHQQLKTGLfsgLLKTPAFRRAE------SEA---LDRAATwleRVGLLEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 145 KAICKLPKILVLDEFSAGLDPAQ-------IASFRKKLKnlsssMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKE 217
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKEtkeldelIAELRNEHN-----VTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
.
gi 2540524722 218 I 218
Cdd:PRK11300 241 I 241
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-218 |
9.61e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKnyGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT-------EETDEFKKAT 76
Cdd:PRK11831 9 DMRGVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGEnipamsrSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 77 AFVPEIPELDSSLTVKEILFFEAEISGQKKNEA-DLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNLSSS--MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
14-194 |
9.98e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.57 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 14 YGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLH-----YQSSGTVRICGTEETD------EFKKATAFVPEI 82
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLYApdvdpvEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PElDSSLTVKEILFFEAEISGQKKNEADL---TVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:PRK14243 100 PN-PFPKSIYDNIAYGARINGYKGDMDELverSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|....*
gi 2540524722 160 SAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEA 194
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQA 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-224 |
2.03e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 66.28 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT--EETDE--FKKATAFVPEIPELDSSLTVKEILF 96
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplVQYDHhyLHRQVALVGQEPVLFSGSVRENIAY 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 feaeisGQKKNEAD--LTVKKAAT----ICGLEEVFNKKI----SKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpA 166
Cdd:TIGR00958 578 ------GLTDTPDEeiMAAAKAANahdfIMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALD-A 650
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 167 QIASFRKKLKNlSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIVKKFNC 224
Cdd:TIGR00958 651 ECEQLLQESRS-RASRTVLLIAHRL-STVERADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-231 |
2.09e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 32 ITGILGPNGAGKTSVLKAICG-LHYQS-SGTVRICGTEETDEFKKATAFVPEIPELDSSLTVKEILFFEA------EISG 103
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSllrlpkSLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 104 QKKNEADLTV--KKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSS 181
Cdd:PLN03211 176 QEKILVAESVisELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 182 -MTIIFSTHHIEEAV-SMCNRIYIIANGEVAACGTEKEIVKKFNCKNLEEAF 231
Cdd:PLN03211 256 gKTIVTSMHQPSSRVyQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSF 307
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
35-190 |
2.26e-12 |
|
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: 62.94 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 35 ILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEEtdefkkaTAFVPEIPELdSSLTVKEILFFEAEisgqkkneadltvk 114
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGED-------LLFLPQRPYL-PLGTLREQLIYPWD-------------- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 115 kaaticgleevfnkkiSKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLssSMTIIFSTHH 190
Cdd:cd03223 90 ----------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
35-190 |
2.56e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 35 ILGPNGAGKTSVLKAICGLHYQSSGTVRICGT---EETDEFKKATAFVPEIPELDSSLTVKEILFFEAEISGQKKNEADL 111
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDAGEVLWQGEpirRQRDEYHQDLLYLGHQPGIKTELTALENLRFYQRLHGPGDDEALW 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 112 TVKKAATICGLEEVfnkKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAgLDPAQIASFRKKL-KNLSSSMTIIFSTH 189
Cdd:PRK13538 112 EALAQVGLAGFEDV---PVRQLSAGQQRRVALARLWLTRAPLWILDEpFTA-IDKQGVARLEALLaQHAEQGGMVILTTH 187
|
.
gi 2540524722 190 H 190
Cdd:PRK13538 188 Q 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-209 |
2.66e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.09 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 18 SACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLhYQSSGTVRICGTE----ETDEFKKATAFVPEipeldssltvkE 93
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSwnsvTLQTWRKAFGVIPQ-----------K 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ILFFEAEIsgqKKN------EADLTVKKAATICGLEEVFNKKISK-----------LSKGFKQRTSLAKAICKLPKILVL 156
Cdd:TIGR01271 1301 VFIFSGTF---RKNldpyeqWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 157 DEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEV 209
Cdd:TIGR01271 1378 DEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSV 1429
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-218 |
3.11e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 3 NEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-----ETDE------ 71
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrDKDGqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 72 ------FKKATAFVPEIPELDSSLTVKE-ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKI-SKLSKGFKQRTSL 143
Cdd:PRK10619 84 knqlrlLRTRLTMVFQHFNLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 144 AKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-221 |
3.56e-12 |
|
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: 63.71 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSlTVKEilf 96
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlnlrWLRSQIGLVSQEPVLFDG-TIAE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 feaEISGQKKNEADLTVKKAATIC-----------GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP 165
Cdd:cd03249 96 ---NIRYGKPDATDEEVEEAAKKAnihdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2540524722 166 AQIASFRKKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:cd03249 173 ESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-218 |
4.07e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATA------F 78
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlgigiI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDsSLTVKEILFF----EAEISGQKKNEADLTVKKAATI---CGLEEVFNKKISKLSKGFKQRTSLAKAICKLP 151
Cdd:PRK09700 86 YQELSVID-ELTVLENLYIgrhlTKKVCGVNIIDWREMRVRAAMMllrVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 152 KILVLDEFSAGLDPAQIASFRKKLKNLSSSMT-IIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-193 |
4.79e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.90 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 29 KNSITGILGPNGAGKTSVLKAICGLHyQSSGTVRICGTEE------------TDEFKKATAFVPEIPELdSSLTVKEILF 96
Cdd:PRK14258 32 QSKVTAIIGPSGCGKSTFLKCLNRMN-ELESEVRVEGRVEffnqniyerrvnLNRLRRQVSMVHPKPNL-FPMSVYDNVA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEISG-QKKNEADLTVKKAATICGLEEVFNKKISK----LSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASF 171
Cdd:PRK14258 110 YGVKIVGwRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKV 189
|
170 180
....*....|....*....|....
gi 2540524722 172 RKKLKN--LSSSMTIIFSTHHIEE 193
Cdd:PRK14258 190 ESLIQSlrLRSELTMVIVSHNLHQ 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-190 |
7.94e-12 |
|
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: 64.30 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG----TEETDEFKKATAFVPEIPELDSSlTVKE-IL 95
Cdd:TIGR02868 352 DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvsSLDQDEVRRRVSVCAQDAHLFDT-TVREnLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 96 FFEAEISGQKKNEADLTVKKAATICGLEEVFNKKI----SKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASF 171
Cdd:TIGR02868 431 LARPDATDEELWAALERVGLADWLRALPDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
170
....*....|....*....
gi 2540524722 172 RKKLKNLSSSMTIIFSTHH 190
Cdd:TIGR02868 511 LEDLLAALSGRTVVLITHH 529
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
32-220 |
8.40e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 8.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 32 ITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE----ETDEFKKATAFVPE-IPELDSsLTVKEILffeaEIS---- 102
Cdd:PRK10575 39 VTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswSSKAFARKVAYLPQqLPAAEG-MTVRELV----AIGrypw 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 103 ----GQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNL 178
Cdd:PRK10575 114 hgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2540524722 179 SS--SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK10575 194 SQerGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-209 |
1.10e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.93 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRIcGTeeTDEFkkatAFVP-EIPELDSSLTVKEILffeA 99
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE--TVKI----GYFDqHQEELDPDKTVLDEL---R 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 100 EISgqkkneADLTVKKAATICGL-----EEVFnKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKK 174
Cdd:COG0488 402 DGA------PGGTEQEVRGYLGRflfsgDDAF-KPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
170 180 190
....*....|....*....|....*....|....*..
gi 2540524722 175 LKNLSSsmTIIFSTH--HIEEAVsmCNRIYIIANGEV 209
Cdd:COG0488 475 LDDFPG--TVLLVSHdrYFLDRV--ATRILEFEDGGV 507
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
15-219 |
1.20e-11 |
|
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: 63.67 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 15 GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRI-CGTEETDEFKK-------ATAFV------- 79
Cdd:TIGR03269 295 GVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPgpdgrgrAKRYIgilhqey 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 ---PEIPELDSsLTVKEILFFEAEISGQKK----NEADLTVKKAaticglEEVFNKKISKLSKGFKQRTSLAKAICKLPK 152
Cdd:TIGR03269 375 dlyPHRTVLDN-LTEAIGLELPDELARMKAvitlKMVGFDEEKA------EEILDKYPDELSEGERHRVALAQVLIKEPR 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 153 ILVLDEFSAGLDPAQIASFRKKLKNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:TIGR03269 448 IVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-168 |
1.22e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 37 GPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD-EFKKATAFVPEIPELDSSLTVKEILFFEAEISGQKkneADLTVKK 115
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRR---AKQMPGS 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 116 AATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQI 168
Cdd:PRK13543 121 ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI 173
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-218 |
1.26e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 62.81 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 31 SITGILGPNGAGKTSVLKAICGLH-----YQSSGTVRICGT-----EETDEFKKATAFVPEIPELDSSLTVKEILffeAE 100
Cdd:PRK14271 48 AVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRsifnyRDVLEFRRRVGMLFQRPNPFPMSIMDNVL---AG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 101 ISGQK---KNEADLTVKKAATICGLEEVFNKKIS----KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRK 173
Cdd:PRK14271 125 VRAHKlvpRKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2540524722 174 KLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK14271 205 FIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-158 |
1.57e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEEtdefkkaTAFVPEIPELDSSLTVKEILF---- 96
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR-------IGYLPQEPPLDDDLTVLDTVLdgda 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 ---------FEAEISGQKKNE-----ADLTVK-----------KAATIC-GL---EEVFNKKISKLSKGFKQRTSLAKAI 147
Cdd:COG0488 88 elraleaelEELEAKLAEPDEdlerlAELQEEfealggweaeaRAEEILsGLgfpEEDLDRPVSELSGGWRRRVALARAL 167
|
170
....*....|.
gi 2540524722 148 CKLPKILVLDE 158
Cdd:COG0488 168 LSEPDLLLLDE 178
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-221 |
2.12e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTV----RICGTEETDEFKKATAFVPEIPE---LDSslTVKE 93
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnQAITDDNFEKLRKHIGIVFQNPDnqfVGS--IVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRK 173
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2540524722 174 KLKNLSSS--MTIIFSTHHIEEAVSmCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13648 184 LVRKVKSEhnITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-225 |
3.02e-11 |
|
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: 60.62 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLH-YQ-SSGTVRICGTE----ETDEFKKATAFV-PEIPeldssltvke 93
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkYEvTEGEILFKGEDitdlPPEERARLGIFLaFQYP---------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ilffeAEISGqkkneadltVKKAATICGLEEVFnkkisklSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpaqIASFR- 172
Cdd:cd03217 87 -----PEIPG---------VKNADFLRYVNEGF-------SGGEKKRNEILQLLLLEPDLAILDEPDSGLD---IDALRl 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 173 -----KKLKNLSSSMTIIfsTHH--IEEAVSMcNRIYIIANGEVAACGTeKEIVKKFNCK 225
Cdd:cd03217 143 vaeviNKLREEGKSVLII--THYqrLLDYIKP-DRVHVLYDGRIVKSGD-KELALEIEKK 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-220 |
3.07e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-----ETDEFKKATAFVPE-------------- 81
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDisprsPLDAVKKGMAYITEsrrdngffpnfsia 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 -----IPEL-DSSLTVKEILFFEAEISGQKKNEADLTVKKAATIcgleevfNKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:PRK09700 360 qnmaiSRSLkDGGYKGAMGLFHEVDEQRTAENQRELLALKCHSV-------NQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAAC------GTEKEIVK 220
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQIltnrddMSEEEIMA 504
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-213 |
1.15e-10 |
|
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: 58.48 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET---DEFKKATAFVPEIPELdssltvkeilfF 97
Cdd:cd03247 19 KNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSdleKALSSLISVLNQRPYL-----------F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 eaeisgqkkneadltvkkAATIcgleevFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP---AQIAS-FRK 173
Cdd:cd03247 88 ------------------DTTL------RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPiteRQLLSlIFE 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2540524722 174 KLKNlsssMTIIFSTHHIeEAVSMCNRIYIIANGEVAACG 213
Cdd:cd03247 144 VLKD----KTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-176 |
1.21e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 16 KFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQS----SGTVRICGTEETDEFKKATAFVPEIPELD---SS 88
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvEGVITYDGITPEEIKKHYRGDVVYNAETDvhfPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEILFFEAEISG------------QKKNEADLTvkkaATICGLEEVFNKK-----ISKLSKGFKQRTSLAKAICKLP 151
Cdd:TIGR00956 153 LTVGETLDFAARCKTpqnrpdgvsreeYAKHIADVY----MATYGLSHTRNTKvgndfVRGVSGGERKRVSIAEASLGGA 228
|
170 180
....*....|....*....|....*
gi 2540524722 152 KILVLDEFSAGLDPAQIASFRKKLK 176
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALK 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
12-209 |
2.02e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGtvricgteetdEFKKATAFVPEIPElDSSLtv 91
Cdd:PRK11247 20 KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-----------ELLAGTAPLAEARE-DTRL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 92 keiLFFEAEI--------------SGQKKNEAdltvKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLD 157
Cdd:PRK11247 86 ---MFQDARLlpwkkvidnvglglKGQWRDAA----LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 158 EFSAGLDpaqiASFRKKLKNLSSSM------TIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:PRK11247 159 EPLGALD----ALTRIEMQDLIESLwqqhgfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-229 |
2.39e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGL-HYQ-SSGTVRICG---TE-ETDEFKKATAFV-----PEIPELdssl 89
Cdd:COG0396 17 KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpKYEvTSGSILLDGediLElSPDERARAGIFLafqypVEIPGV---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 90 TVKEilFFEAEISGQKKNEADL-----TVKKAATICGLEEVF-----NkkiSKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:COG0396 93 SVSN--FLRTALNARRGEELSAreflkLLKEKMKELGLDEDFldryvN---EGFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 160 SAGLDpaqIASFR------KKLKNLSSSMTIIfsTHH--IEEAVSmCNRIYIIANGEVAACGTeKEIVKKfncknLEE 229
Cdd:COG0396 168 DSGLD---IDALRivaegvNKLRSPDRGILII--THYqrILDYIK-PDFVHVLVDGRIVKSGG-KELALE-----LEE 233
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-222 |
2.82e-10 |
|
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: 59.43 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGL--HYQSSGT----VRICgteETDEFKKATAF 78
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRiiyhVALC---EKCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPE-IPELDSSLTVKEILFF---EAEISGQKKN------------------------------EADLTVKKAATIcgLEE 124
Cdd:TIGR03269 78 VGEpCPVCGGTLEPEEVDFWnlsDKLRRRIRKRiaimlqrtfalygddtvldnvlealeeigyEGKEAVGRAVDL--IEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 125 V-FNKKIS----KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNL--SSSMTIIFSTHHIEEAVSM 197
Cdd:TIGR03269 156 VqLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|....*
gi 2540524722 198 CNRIYIIANGEVAACGTEKEIVKKF 222
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-207 |
3.52e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETdeFKKATA--------------FVPEipe 84
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAalaagvaiiyqelhLVPE--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 ldssLTVKEILFFeaeisGQKKNEADL----TVKKAATIC----GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVL 156
Cdd:PRK11288 94 ----MTVAENLYL-----GQLPHKGGIvnrrLLNYEAREQlehlGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 157 DEFSAGLDPAQIASFRKKLKNLSSSMT-IIFSTHHIEEAVSMCNRIYIIANG 207
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRvILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-209 |
3.71e-10 |
|
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: 57.87 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDE----FKKATAFVPEIPELDSSLTVKEILF 96
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYehkyLHSKVSLVGQEPVLFARSLQDNIAY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 FEAEISGQKKNEADLTVKKAATICGLEEVFN----KKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFR 172
Cdd:cd03248 111 GLQSCSFECVKEAAQKAHAHSFISELASGYDtevgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQ 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 2540524722 173 KKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEV 209
Cdd:cd03248 191 QALYDWPERRTVLVIAHRL-STVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-221 |
4.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.25 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 16 KFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFK--------KATAFVPEIPE--L 85
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpvrKRIGMVFQFPEsqL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 86 DSSLTVKEILFfeaeisGQKKNEADL-TVKKAATICGLEEVFNKKISKLSK-----GFKQRTSLAKAICKLPKILVLDEF 159
Cdd:PRK13646 99 FEDTVEREIIF------GPKNFKMNLdEVKNYAHRLLMDLGFSRDVMSQSPfqmsgGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 160 SAGLDPA---QIASFRKKLKnLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13646 173 TAGLDPQskrQVMRLLKSLQ-TDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-221 |
5.45e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.22 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 23 INFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSLTVKEILFFe 98
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfgltDLRRVLSIIPQSPVLFSGTVRFNIDPF- 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 aeisgQKKNEADL-------TVKKAA--TICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIA 169
Cdd:PLN03232 1334 -----SEHNDADLwealeraHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 170 SFRKKLKNLSSSMTIIFSTHHIEEAVSmCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-164 |
6.58e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.41 E-value: 6.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEE---TDEFKKAtafvpeipeLDS 87
Cdd:TIGR03719 329 TKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKlayVDQSRDA---------LDP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 SLTVKEilffeaEISGQkkneADLTVKKAATI-----CGLeevFN-------KKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:TIGR03719 400 NKTVWE------EISGG----LDIIKLGKREIpsrayVGR---FNfkgsdqqKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*....
gi 2540524722 156 LDEFSAGLD 164
Cdd:TIGR03719 467 LDEPTNDLD 475
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
21-218 |
8.68e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 57.07 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRIcGTEETD-------------EFKKATAFVPEIPELDS 87
Cdd:PRK11264 20 HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDtarslsqqkglirQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 SLTVKE-ILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPA 166
Cdd:PRK11264 99 HRTVLEnIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 167 QIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK11264 179 LVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-228 |
8.99e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 57.82 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 3 NEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAgktSVLKAICGLHYQSSGTVR-------ICGTEETDEfKKA 75
Cdd:NF000106 12 NAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---A**RGALPAHV*GPDAGRrpwrf*tWCANRRALR-RTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 76 TAFVPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILV 155
Cdd:NF000106 88 G*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFNCKNLE 228
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
31-195 |
9.24e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.42 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 31 SITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATAFVPEIPELDSSLTVKEILFFEAEISgqkkNEAD 110
Cdd:PRK13541 27 AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIY----NSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 111 lTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQiasfRKKLKNL----SSSMTIIF 186
Cdd:PRK13541 103 -TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN----RDLLNNLivmkANSGGIVL 177
|
....*....
gi 2540524722 187 STHHIEEAV 195
Cdd:PRK13541 178 LSSHLESSI 186
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
12-218 |
1.47e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.16 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNY-GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG----TEETDEFKKATAF-----VPE 81
Cdd:PRK11650 11 KSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnELEPADRDIAMVFqnyalYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 ipeldssLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:PRK11650 91 -------MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 162 GLDPAQIASFRKKLKNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK11650 164 NLDAKLRVQMRLEIQRLHRRLktTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-229 |
1.80e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRIcgteetdefKKATAFVPEIPELDSSLTVKEILFFE 98
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI---------KGSAALIAISSGLNGQLTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 AEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAGLDPAQIASFRKKLKN 177
Cdd:PRK13545 110 GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEaLSVGDQTFTKKCLDKMNEF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 178 LSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV-------KKFNCKNLEE 229
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVdhydeflKKYNQMSVEE 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
35-209 |
1.83e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 35 ILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET--DEFKKA------TAFVPEIPELDSSLTVKEILFFEAEISGQKK 106
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAklrakhVGFVFQSFMLIPTLNALENVELPALLRGESS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 107 NEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPA---QIASFRKKLkNLSSSMT 183
Cdd:PRK10584 121 RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQtgdKIADLLFSL-NREHGTT 199
|
170 180
....*....|....*....|....*.
gi 2540524722 184 IIFSTHHIEEAvSMCNRIYIIANGEV 209
Cdd:PRK10584 200 LILVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-218 |
2.39e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 8 ISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVR-------------ICGTEETDEFKK 74
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 75 -------ATAFVPEIPELDSSLTVKEILFFEAEI-SGQKKNEADLTVKKA---ATICGLEEVFNKKISKLSKGFKQRTSL 143
Cdd:PRK10261 100 hvrgadmAMIFQEPMTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMldqVRIPEAQTILSRYPHQLSGGMRQRVMI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 144 AKAICKLPKILVLDEFSAGLD---PAQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK10261 180 AMALSCRPAVLIADEPTTALDvtiQAQILQLIKVLQK-EMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-221 |
2.50e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 15 GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEipelDSSLT 90
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvtraSLRRNIAVVFQ----DAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 91 VKEIlffEAEISGQKKNEADLTVKKAATIC-----------GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEF 159
Cdd:PRK13657 422 NRSI---EDNIRVGRPDATDEEMRAAAERAqahdfierkpdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 160 SAGLDPAQIASFRKKLKNLSSSMT--II---FSThhIEEAvsmcNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMKGRTtfIIahrLST--VRNA----DRILVFDNGRVVESGSFDELVAR 559
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-167 |
3.79e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.49 E-value: 3.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 29 KNSITGILGPNGAGKTSVLKAICGLHYQSSGtvricgteETDEFKKATAFVPEIPELDSSLTVKEILFFEAEISG---QK 105
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEG--------DIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDFYthpYF 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 106 KNEAdltvkkaATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQ 167
Cdd:cd03237 96 KTEI-------AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQ 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-189 |
4.46e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.10 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNIN---FYAEKnsiTGILGPNGAGKTSVLKAICGLHYQSSGTVRIcgteeTDEFKkaTAFVPEIPELDSSLTVKEILF- 96
Cdd:TIGR03719 22 KDISlsfFPGAK---IGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----QPGIK--VGYLPQEPQLDPTKTVRENVEe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 -----------FEaEIS---GQKKNEADLTVKKAATI------CGLEEVFNK---------------KISKLSKGFKQRT 141
Cdd:TIGR03719 92 gvaeikdaldrFN-EISakyAEPDADFDKLAAEQAELqeiidaADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2540524722 142 SLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSsmTIIFSTH 189
Cdd:TIGR03719 171 ALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-190 |
5.15e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGT---EETDEFKKATAFVPEIPELDSSLTVKEILFF 97
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikKDLCTYQKQLCFVGHRSGINPYLTLRENCLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 EAEISgqkknEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKN 177
Cdd:PRK13540 98 DIHFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|...
gi 2540524722 178 LSSSMTIIFSTHH 190
Cdd:PRK13540 173 HRAKGGAVLLTSH 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-164 |
5.53e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.82 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNY--GKFSA--CKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATA--------F 78
Cdd:PRK11629 12 CKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqklgF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:PRK11629 92 IYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
....*.
gi 2540524722 159 FSAGLD 164
Cdd:PRK11629 172 PTGNLD 177
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-208 |
8.31e-09 |
|
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: 52.84 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVricgteetdefkkatafvpeipE 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------T 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 85 LDSSLTvkeILFFEaeisgqkkneadltvkkaaticgleevfnkkisKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:cd03221 59 WGSTVK---IGYFE---------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2540524722 165 PAQIASFRKKLKNLSSsmTIIFSTH--HIEEAVsmCNRIYIIANGE 208
Cdd:cd03221 103 LESIEALEEALKEYPG--TVILVSHdrYFLDQV--ATKIIELEDGK 144
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
123-208 |
1.73e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 123 EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSS---MTIIFSthHIEEAVSMCN 199
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenrITIIIA--HRLSTIRYAN 647
|
....*....
gi 2540524722 200 RIYIIANGE 208
Cdd:PTZ00265 648 TIFVLSNRE 656
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
30-213 |
2.47e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 30 NSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKAtaFVPeiPEL--------DSSL----TVKEILFF 97
Cdd:PRK11144 24 QGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGI--CLP--PEKrrigyvfqDARLfphyKVRGNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 eaeisGQKKNEADLtVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD-PaqiasfRKK-- 174
Cdd:PRK11144 100 -----GMAKSMVAQ-FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlP------RKRel 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2540524722 175 ---LKNLSSSMT--IIFSTHHIEEAVSMCNRIYIIANGEVAACG 213
Cdd:PRK11144 168 lpyLERLAREINipILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-218 |
2.88e-08 |
|
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: 53.76 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTeetdefkkaTAFVPEIPELDSSlTVKEILFFeae 100
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---------ISFSPQTSWIMPG-TIKDNIIF--- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 101 isGQKKNEADLT-VKKAatiCGLEEVFNKKISK-----------LSKGFKQRTSLAKAICKLPKILVLDEFSAGLD-PAQ 167
Cdd:TIGR01271 510 --GLSYDEYRYTsVIKA---CQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDvVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 168 IASFRKKLKNLSSSMTIIFSTHHIEEaVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:TIGR01271 585 KEIFESCLCKLMSNKTRILVTSKLEH-LKKADKILLLHEGVCYFYGTFSEL 634
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
35-190 |
5.88e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.50 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 35 ILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETdefkkatAFVPE---IPELdsslTVKEILFF---EAEISgqkkne 108
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARV-------LFLPQrpyLPLG----TLREALLYpatAEAFS------ 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 109 aDLTVKKAATICGLEEVFNK--------KIskLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSS 180
Cdd:COG4178 457 -DAELREALEAVGLGHLAERldeeadwdQV--LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP 533
|
170
....*....|
gi 2540524722 181 SMTIIFSTHH 190
Cdd:COG4178 534 GTTVISVGHR 543
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-211 |
7.02e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGL-HYQSSGTVRICGTEET-----DEFKKATAFVPE-------IPELD-- 86
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKirnpqQAIAQGIAMVPEdrkrdgiVPVMGvg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 --------SSLTVKEILFFEAEISGQKKNEADLTVKKAATICgleevfnkKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:PRK13549 360 knitlaalDRFTGGSRIDDAAELKTILESIQRLKVKTASPEL--------AIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 159 FSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQQgVAIIVISSELPEVLGLSDRVLVMHEGKLKG 485
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-219 |
7.41e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET----DEFKKATAFVP 80
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTklqlDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 81 EIPELDSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISK----LSKGFKQRTSLAKAICKLPKILVL 156
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILIL 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540524722 157 DE-FSA--GLDPAQIasfrkkLKNLSS---SMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:PRK10789 476 DDaLSAvdGRTEHQI------LHNLRQwgeGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-164 |
8.05e-08 |
|
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: 52.48 E-value: 8.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 28 EKNSITGILGPNGAGKTSVLKAICGL------HYQSSGTV-----RICGTEETDEFKKATA----------FVPEIPELd 86
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGElkpnlgDYDEEPSWdevlkRFRGTELQDYFKKLANgeikvahkpqYVDLIPKV- 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 87 SSLTVKEILffeaeisgqKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:COG1245 176 FKGTVRELL---------EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-207 |
8.91e-08 |
|
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: 51.28 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGlHYQ-SSGTVRICGTEETDEFKKATA----------------F--- 78
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLpDSGSILVRHDGGWVDLAQASPreilalrrrtigyvsqFlrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 79 VPEIPELDsslTVKEILFfEAeisGQKKNEADLTVKKAATICGLEEvfnkkisKL--------SKGFKQRTSLAKAICKL 150
Cdd:COG4778 105 IPRVSALD---VVAEPLL-ER---GVDREEARARARELLARLNLPE-------RLwdlppatfSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 151 PKILVLDEFSAGLDPAQIASFR---KKLKNLSSSMTIIFstHHIE--EAVsmCNRIYIIANG 207
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVeliEEAKARGTAIIGIF--HDEEvrEAV--ADRVVDVTPF 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-210 |
1.27e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEET-----DEFKKATAFVPEIPE-----LDS--- 87
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINalstaQRLARGLVYLPEDRQssglyLDApla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 ----SLTVKEILFFEAEisgqKKNEADLTVKKAATICGLEEVfNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGL 163
Cdd:PRK15439 360 wnvcALTHNRRGFWIKP----ARENAVLERYRRALNIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2540524722 164 DPAQIASFRKKLKNLSS-SMTIIFSTHHIEEAVSMCNRIYIIANGEVA 210
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-164 |
1.29e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 2 SNEVELIS---FCKNYGKFSackninFYAE-----KNSITGILGPNGAGKTSVLKAICGLHYQSSGTVricgteetdEFK 73
Cdd:COG1245 336 KEEETLVEypdLTKSYGGFS------LEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---------DED 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 74 KATAFVPEIPELDSSLTVKEIL-----------FFEAEIsgqkkneadltVKKaatiCGLEEVFNKKISKLSKGFKQRTS 142
Cdd:COG1245 401 LKISYKPQYISPDYDGTVEEFLrsantddfgssYYKTEI-----------IKP----LGLEKLLDKNVKDLSGGELQRVA 465
|
170 180
....*....|....*....|..
gi 2540524722 143 LAKAICKLPKILVLDEFSAGLD 164
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLD 487
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-220 |
1.52e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICG-LHYQSSGTVRICGTeetdefkkaTAFVPEIPELDSSLTVKEILF---F 97
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS---------VAYVPQVSWIFNATVRENILFgsdF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 EAEISGQK------KNEADLTVKKAATICGLEEVfnkkisKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpAQIAS- 170
Cdd:PLN03232 706 ESERYWRAidvtalQHDLDLLPGRDLTEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD-AHVAHq 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 171 -FRKKLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PLN03232 779 vFDSCMKDELKGKTRVLVTNQL-HFLPLMDRIILVSEGMIKEEGTFAELSK 828
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-220 |
1.59e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 51.66 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICG-LHYQSSGTVRICGTeetdefkkaTAFVPEIPELDSSlTVKEILFFEAE 100
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT---------VAYVPQVSWIFNA-TVRDNILFGSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 101 ISGQKKNEA-DLTV--KKAATICG--LEEVFNKKISkLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpAQIAS--FRK 173
Cdd:PLN03130 705 FDPERYERAiDVTAlqHDLDLLPGgdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALD-AHVGRqvFDK 782
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2540524722 174 KLKNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PLN03130 783 CIKDELRGKTRVLVTNQL-HFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-231 |
1.95e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.32 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 32 ITGILGPNGAGKTSVLKAICGLhYQSSGTVRICGTEETD----EFKKATAF----------VPEIPELDSSLTvkeilff 97
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAwsaaELARHRAYlsqqqtppfaMPVFQYLTLHQP------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 eaeiSGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKL-PKI------LVLDEFSAGLDPAQIAS 170
Cdd:PRK03695 96 ----DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVwPDInpagqlLLLDEPMNSLDVAQQAA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 171 FRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKFnckNLEEAF 231
Cdd:PRK03695 172 LDRLLSELCQQgIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPE---NLAQVF 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-164 |
1.96e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISfcKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRIcGteET------DEFKKAta 77
Cdd:PRK11819 326 EAENLS--KSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G--ETvklayvDQSRDA-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 78 fvpeipeLDSSLTVKEilffeaEISGqkknEAD-LTVKKAaticgleEV--------FN-------KKISKLSKGFKQRT 141
Cdd:PRK11819 399 -------LDPNKTVWE------EISG----GLDiIKVGNR-------EIpsrayvgrFNfkggdqqKKVGVLSGGERNRL 454
|
170 180
....*....|....*....|...
gi 2540524722 142 SLAKAICKLPKILVLDEFSAGLD 164
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-201 |
2.00e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 3 NEVELISFCKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVR--------ICGTEETDEFkk 74
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanigYYAQDHAYDF-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 75 atafvpeipelDSSLTVKEILffeaeisGQKKNEAD--LTVKkaATICGL---EEVFNKKISKLSKGFKQRTSLAKAICK 149
Cdd:PRK15064 396 -----------ENDLTLFDWM-------SQWRQEGDdeQAVR--GTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 150 LPKILVLDEFSAGLDPAQIASFRKKLKNLSSsmTIIFSTHHIEEAVSMCNRI 201
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHDREFVSSLATRI 505
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-211 |
2.80e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEetdefkkataFVPEIPE--LDSSLtvkeilffe 98
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE----------VVTRSPQdgLANGI--------- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 99 AEISGQKKNEA---DLTVKKAATICGLEE----------------------VFNKK-------ISKLSKGFKQRTSLAKA 146
Cdd:PRK10762 330 VYISEDRKRDGlvlGMSVKENMSLTALRYfsraggslkhadeqqavsdfirLFNIKtpsmeqaIGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 147 ICKLPKILVLDEFSAGLDPAQ-------IASFRKKlknlssSMTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAkkeiyqlINQFKAE------GLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
34-221 |
2.84e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 34 GILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKATAFVPEIPELDSSlTVKEIL--FFEaeisgqkKN 107
Cdd:PLN03130 1269 GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmDLRKVLGIIPQAPVLFSG-TVRFNLdpFNE-------HN 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 108 EADL-----------TVKKAATicGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLK 176
Cdd:PLN03130 1341 DADLweslerahlkdVIRRNSL--GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2540524722 177 NLSSSMTIIFSTHHIEEAVSmCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PLN03130 1419 EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
21-220 |
3.50e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 3.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQS--SGTVRICGTEETD----------EFKKATAFVPEIPELDSS 88
Cdd:PRK13547 18 RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLNgeplaaidapRLARLRAVLPQAAQPAFA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKEIL----FFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKL---------PKILV 155
Cdd:PRK13547 98 FSAREIVllgrYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQLwpphdaaqpPRYLL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 156 LDEFSAGLDPAQIASFRKKLKNLSS--SMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVK 220
Cdd:PRK13547 178 LDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
15-191 |
5.36e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 15 GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-------ETDEFKKATAFVPEIPELDS 87
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlknrEVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 88 SLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQ 167
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180
....*....|....*....|....*
gi 2540524722 168 IASFRKKLKNLSS-SMTIIFSTHHI 191
Cdd:PRK10908 173 SEGILRLFEEFNRvGVTVLMATHDI 197
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-221 |
5.89e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 2 SNEVELISFCKNY--GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETD----EFKKA 75
Cdd:TIGR00957 1282 RGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiglhDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 76 TAFVPEIPELDS-SLTVKEILFfeaeisGQKKNE--------ADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKA 146
Cdd:TIGR00957 1362 ITIIPQDPVLFSgSLRMNLDPF------SQYSDEevwwalelAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 147 ICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMcNRIYIIANGEVAACGTEKEIVKK 221
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-211 |
1.21e-06 |
|
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: 48.67 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGLHY-QSSGTVRICGTE-----ETDEFKKATAFVPE-------IPELD-- 86
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPvdirnPAQAIRAGIAMVPEdrkrhgiVPILGvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 --------SSLTVKEILFFEAEISGQKKNEADLTVKKAATICgleevfnkKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:TIGR02633 358 knitlsvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFL--------PIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 159 FSAGLDPAQIASFRKKLKNLSSS-MTIIFSTHHIEEAVSMCNRIYIIANGEVAA 211
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-164 |
1.36e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVricgteetdeFKKATAFVP-----EIPELDssLTVKEIL 95
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV----------FRSAKVRMAvfsqhHVDGLD--LSSNPLL 593
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 96 FFEAEISG--QKKNEADLTVKKAATICGLEEVFNkkiskLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:PLN03073 594 YMMRCFPGvpEQKLRAHLGSFGVTGNLALQPMYT-----LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-158 |
1.38e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNIN---FYAEKnsItGILGPNGAGKTSVLKAICGLHYQSSGTVRIcgteeTDEFKkaTAFVPEIPELDSSLTVKEILF- 96
Cdd:PRK11819 24 KDISlsfFPGAK--I-GVLGLNGAGKSTLLRIMAGVDKEFEGEARP-----APGIK--VGYLPQEPQLDPEKTVRENVEe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 97 -----------FEaEISGQKKNEADLTVKKAATICGLEEVF------------------------NKKISKLSKGFKQRT 141
Cdd:PRK11819 94 gvaevkaaldrFN-EIYAAYAEPDADFDALAAEQGELQEIIdaadawdldsqleiamdalrcppwDAKVTKLSGGERRRV 172
|
170 180
....*....|....*....|.
gi 2540524722 142 slakAICKL----PKILVLDE 158
Cdd:PRK11819 173 ----ALCRLllekPDMLLLDE 189
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-190 |
1.39e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGlH--YQ-SSGTVRICGT----EETDEFKKATAFVP-----EIPELDSS 88
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HpaYKiLEGDILFKGEsildLEPEERAHLGIFLAfqypiEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 89 LTVKeiLFFEAEISGQKKNEAD----LTV-KKAATICGLEEVF-NKKISK-LSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:CHL00131 103 DFLR--LAYNSKRKFQGLPELDplefLEIiNEKLKLVGMDPSFlSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDS 180
|
170 180 190
....*....|....*....|....*....|..
gi 2540524722 162 GLDP---AQIASFRKKLKNLSSSMTIIfsTHH 190
Cdd:CHL00131 181 GLDIdalKIIAEGINKLMTSENSIILI--THY 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
5-164 |
1.70e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 5 VELISFCKNYGKFSAckNINF-YAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVricgteetdEFKKATAFVPEIP 83
Cdd:PRK13409 341 VEYPDLTKKLGDFSL--EVEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---------DPELKISYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 ELDSSLTVKEIL----------FFEAEIsgqkkneadltVKKaatiCGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKI 153
Cdd:PRK13409 410 KPDYDGTVEDLLrsitddlgssYYKSEI-----------IKP----LQLERLLDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170
....*....|.
gi 2540524722 154 LVLDEFSAGLD 164
Cdd:PRK13409 475 YLLDEPSAHLD 485
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-221 |
2.73e-06 |
|
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: 48.02 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 23 INFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRIcgteetdefKKATAFVPEIPELDSSLTVKEILFfeaeis 102
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM---------KGSVAYVPQQAWIQNDSLRENILF------ 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 103 GQKKNEA--DLTVKKAATICGLE--------EVFNKKISkLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpAQIAS-- 170
Cdd:TIGR00957 722 GKALNEKyyQQVLEACALLPDLEilpsgdrtEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVD-AHVGKhi 799
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 171 FRKKL--KNLSSSMTIIFSTHHIeEAVSMCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:TIGR00957 800 FEHVIgpEGVLKNKTRILVTHGI-SYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-164 |
2.74e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 28 EKNSITGILGPNGAGKTSVLKAICGL------HYQSSGTV-----RICGTEETDEFKKATA----------FVPEIPELD 86
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGElipnlgDYEEEPSWdevlkRFRGTELQNYFKKLYNgeikvvhkpqYVDLIPKVF 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 87 SSlTVKEILffeaeisgQKKNEADLtVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:PRK13409 177 KG-KVRELL--------KKVDERGK-LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-211 |
3.33e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKATA--------FVPEIPELDSSLTVK 92
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrrehfgFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 93 EILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFR 172
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2540524722 173 KKLKNL-SSSMTIIFSTHHIEEAvSMCNRIYIIANGEVAA 211
Cdd:PRK10535 185 AILHQLrDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIVR 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-218 |
4.41e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.39 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTeetdefkkaTAFVPEIPELDSSlTVKEILFFeae 100
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR---------ISFSSQFSWIMPG-TIKENIIF--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 101 isGQKKNEAD-LTVKKAatiCGLEEVFNKKISK-----------LSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPA-Q 167
Cdd:cd03291 121 --GVSYDEYRyKSVVKA---CQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFtE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 168 IASFRKKLKNLSSSMTIIFSTHHIEEaVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:cd03291 196 KEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-190 |
4.70e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAIcglhYQSSGTVRICGTEETdEFKKATAFVpeipeldssltvkeilffeae 100
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----LYASGKARLISFLPK-FSRNKLIFI--------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 101 isGQKKNEADLtvkkaaticGLEEV-FNKKISKLSKGFKQRTSLAKAICKLPK--ILVLDEFSAGLDPAQIASFRKKLKN 177
Cdd:cd03238 66 --DQLQFLIDV---------GLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG 134
|
170
....*....|....
gi 2540524722 178 L-SSSMTIIFSTHH 190
Cdd:cd03238 135 LiDLGNTVILIEHN 148
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
131-209 |
4.88e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.01 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 131 SKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD---PAQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANG 207
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLQQ-KHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
..
gi 2540524722 208 EV 209
Cdd:PRK15134 503 EV 504
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-222 |
6.67e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 7 LISFCKNyGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKAtafvpeipeLD 86
Cdd:PRK13546 28 LIPKHKN-KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAG---------LS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 87 SSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE-FSAGLDP 165
Cdd:PRK13546 98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEaLSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 166 AQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIVKKF 222
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
34-209 |
7.84e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.83 E-value: 7.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 34 GILGPNGAGKTSVLKAICGLHYQSSGTVRICGT-------EETDEFKKATAFVPE--IPELDSSLTVKEILffeAE---- 100
Cdd:PRK10419 42 ALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplaklnrAQRKAFRRDIQMVFQdsISAVNPRKTVREII---REplrh 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 101 ISGQKKNEADLTVKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD---PAQIASFRKKLK 176
Cdd:PRK10419 119 LLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQ 198
|
170 180 190
....*....|....*....|....*....|...
gi 2540524722 177 NlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEV 209
Cdd:PRK10419 199 Q-QFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-218 |
8.43e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 8.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 35 ILGPNGAGKTSVLKAICGLHYQSSGTvRICGTEET-------------DEFKKATAFVPEIPELDSSLTVKEILFFEAei 101
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGE-RQSQFSHItrlsfeqlqklvsDEWQRNNTDMLSPGEDDTGRTTAEIIQDEV-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 102 sgqKKNEAdltVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSS 181
Cdd:PRK10938 111 ---KDPAR---CEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 2540524722 182 -MTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK10938 185 gITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-164 |
1.19e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRIcgteetdefKKATAFVPEIPELDSSLTVKEILFFEAE 100
Cdd:PTZ00243 677 RDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA---------ERSIAYVPQQAWIMNATVRGNILFFDEE 747
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 101 isgqkkNEADLtvKKAATIC-----------GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD 164
Cdd:PTZ00243 748 ------DAARL--ADAVRVSqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-219 |
1.37e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.17 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 19 ACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRI------CGTEETDEFKKATAFVPEIPELDSSLTVK 92
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhFGDYSYRSQRIRMIFQDPSTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 93 EILFF----EAEISGQKKNEA-DLTVKKAATicgLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDpaq 167
Cdd:PRK15112 108 QILDFplrlNTDLEPEQREKQiIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD--- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2540524722 168 iASFRKKLKNL------SSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEIV 219
Cdd:PRK15112 182 -MSMRSQLINLmlelqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-202 |
3.45e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 43.22 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 3 NEVELISFcKNYGKFsacKNINFyaeKNSITGILGPNGAGKTSVLKAIC-GLHYQSSGTVRicGTEETDEFKKATAFVPE 81
Cdd:cd03278 2 KKLELKGF-KSFADK---TTIPF---PPGLTAIVGPNGSGKSNIIDAIRwVLGEQSAKSLR--GEKMSDVIFAGSETRKP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKEILFFEAeISGQKKneadltvkkaaticgLEEVFN---KKISK---LSKGFKQRTSLAK--AICKL--- 150
Cdd:cd03278 73 ANFAEVTLTFDNSDGRYS-IISQGD---------------VSEIIEapgKKVQRlslLSGGEKALTALALlfAIFRVrps 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2540524722 151 PkILVLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHiEEAVSMCNRIY 202
Cdd:cd03278 137 P-FCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHR-KGTMEAADRLY 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-201 |
3.66e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 29 KNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEfkkatafvpeipELDSSLTVKEILFFEAEISGQKKne 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILE------------EVLDQLLLIIVGGKKASGSGELR-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 109 adltvkkaaticgleevfnkkisklskgFKQRTSLAKAicKLPKILVLDEFSAGLDPAQIASFR-------KKLKNLSSS 181
Cdd:smart00382 67 ----------------------------LRLALALARK--LKPDVLILDEITSLLDAEQEALLLlleelrlLLLLKSEKN 116
|
170 180
....*....|....*....|
gi 2540524722 182 MTIIFSTHHIEEAVSMCNRI 201
Cdd:smart00382 117 LTVILTTNDEKDLGPALLRR 136
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
34-218 |
3.83e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 43.93 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 34 GILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKA---------TAFVPEIPELDSSLTVKEIL-----FFEA 99
Cdd:PRK15079 51 GVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwravrsdiqMIFQDPLASLNPRMTIGEIIaeplrTYHP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 100 EISGQKKNEadlTVKKAATICGL-EEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD---PAQIASFrkkL 175
Cdd:PRK15079 131 KLSRQEVKD---RVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDvsiQAQVVNL---L 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2540524722 176 KNLSSSM--TIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK15079 205 QQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
11-208 |
3.85e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 11 CKNYGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEEtdEFKKA-------TAFVPEIP 83
Cdd:PRK10982 5 SKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFKSSkealengISMVHQEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 84 ELDSSLTVKEILFF-----EAEISGQKKNEADltVKKAATICGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDE 158
Cdd:PRK10982 83 NLVLQRSVMDNMWLgryptKGMFVDQDKMYRD--TKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 159 FSAGLDPAQIAS-FR--KKLKNlsSSMTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:PRK10982 161 PTSSLTEKEVNHlFTiiRKLKE--RGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-197 |
4.03e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICG---LHYQSSGTVRICGTEETDEFKKATAFVPE----IPEldssLTVKE 93
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLDSSFQRSIGYVQQqdlhLPT----STVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ILFFEA------EISGQKKNEadlTVKKAATICGLEEVFNKKISKLSKGF----KQRTSLAKAICKLPKILV-LDEFSAG 162
Cdd:TIGR00956 856 SLRFSAylrqpkSVSKSEKME---YVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190
....*....|....*....|....*....|....*
gi 2540524722 163 LDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSM 197
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTIHQPSAILF 967
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
12-51 |
4.39e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 4.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACKNINFyaeKNSITGILGPNGAGKTSVLKAIC 51
Cdd:COG0419 8 ENFRSYRDTETIDF---DDGLNLIVGPNGAGKSTILEAIR 44
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
132-220 |
5.19e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.58 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 132 KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD---PAQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiQAQIIELLLELQQ-KENMALVLITHDLALVAEAAHKIIVMYAGQ 231
|
90
....*....|..
gi 2540524722 209 VAACGTEKEIVK 220
Cdd:PRK11022 232 VVETGKAHDIFR 243
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
23-208 |
5.35e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 23 INFYAEKnsITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKAT--AFVPEI-PELD--SSLTVKEILFF 97
Cdd:PRK10762 25 LNVYPGR--VMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSqeAGIGIIhQELNliPQLTIAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 EAEISGQ------KK--NEADLTVKKaatiCGLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIA 169
Cdd:PRK10762 103 GREFVNRfgridwKKmyAEADKLLAR----LNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2540524722 170 SFRKKLKNL-SSSMTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:PRK10762 179 SLFRVIRELkSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-222 |
7.07e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 8 ISFCKNyGKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQS---SGTVRICGtEETDEF--KKATAFVPEI 82
Cdd:PLN03140 170 INLAKK-TKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG-YRLNEFvpRKTSAYISQN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 83 PELDSSLTVKEILFFEA-------------EISGQKKN-------EADLTVKKAAT-------------------ICGLE 123
Cdd:PLN03140 248 DVHVGVMTVKETLDFSArcqgvgtrydllsELARREKDagifpeaEVDLFMKATAMegvksslitdytlkilgldICKDT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 124 EVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPA---QIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNR 200
Cdd:PLN03140 328 IVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSttyQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDD 407
|
250 260
....*....|....*....|..
gi 2540524722 201 IYIIANGEVAACGTEKEIVKKF 222
Cdd:PLN03140 408 IILLSEGQIVYQGPRDHILEFF 429
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-221 |
7.09e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 127 NKKISKLSKGFKQRTSLAKAI-CKLPKIL-VLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSMCNRIYII 204
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLgAELIGITyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDI 550
|
90 100
....*....|....*....|...
gi 2540524722 205 A------NGEVAACGTEKEIVKK 221
Cdd:PRK00635 551 GpgagifGGEVLFNGSPREFLAK 573
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
132-217 |
7.78e-05 |
|
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: 43.27 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 132 KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSMT--II---FSThhIEEAvsmcNRIYIIAN 206
Cdd:COG5265 494 KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTtlVIahrLST--IVDA----DEILVLEA 567
|
90
....*....|.
gi 2540524722 207 GEVAACGTEKE 217
Cdd:COG5265 568 GRIVERGTHAE 578
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
15-218 |
1.26e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 42.40 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 15 GKFSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQS---SGTVRICGTE----ETDEFKKATA------FVPE 81
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREilnlPEKELNKLRAeqismiFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 IPELDSSLTVKEILffeAEI----SGQKKNEA-DLTVKKaaticgLEEV----FNKKIS----KLSKGFKQRTSLAKAIC 148
Cdd:PRK09473 107 MTSLNPYMRVGEQL---MEVlmlhKGMSKAEAfEESVRM------LDAVkmpeARKRMKmyphEFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 149 KLPKILVLDEFSAGLD---PAQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANGEVAACGTEKEI 218
Cdd:PRK09473 178 CRPKLLIADEPTTALDvtvQAQIMTLLNELKR-EFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
133-219 |
1.34e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 133 LSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNL--SSSMTIIFSTHHIeEAVSMCNRIYIIANGE-- 208
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRI-ASIKRSDKIVVFNNPDrt 1437
|
90
....*....|....
gi 2540524722 209 ---VAACGTEKEIV 219
Cdd:PTZ00265 1438 gsfVQAHGTHEELL 1451
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
130-189 |
1.37e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 1.37e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 130 ISKLSKGFKQRTSLAKAI---CKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSMT-IIFSTH 189
Cdd:pfam13304 234 AFELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-164 |
1.51e-04 |
|
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: 41.55 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 22 NINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEFKKAT--------AFVPEIPELDSSlTVKE 93
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnrysvAYAAQKPWLLNA-TVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 ILFFEAEISGQKkneadltVKKAATICGLE------------EVFNKKISkLSKGFKQRTSLAKAICKLPKILVLDEFSA 161
Cdd:cd03290 98 NITFGSPFNKQR-------YKAVTDACSLQpdidllpfgdqtEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
...
gi 2540524722 162 GLD 164
Cdd:cd03290 170 ALD 172
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-204 |
1.77e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 26 YAEKNSITG-------ILGPNGAGKTSVLKAIC-GLHYQSSGTVRicgteetDEFKKATAFVPEIpeldssltvkeilff 97
Cdd:cd03227 10 YFVPNDVTFgegsltiITGPNGSGKSTILDAIGlALGGAQSATRR-------RSGVKAGCIVAAV--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 98 eaeisgqkkneadltvkkAATICGLeevfnkkISKLSKGFKQRTSLAKAI----CKLPKILVLDEFSAGLDP--AQIASF 171
Cdd:cd03227 68 ------------------SAELIFT-------RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPrdGQALAE 122
|
170 180 190
....*....|....*....|....*....|...
gi 2540524722 172 RKKLKNLSSSMTIIFSthHIEEAVSMCNRIYII 204
Cdd:cd03227 123 AILEHLVKGAQVIVIT--HLPELAELADKLIHI 153
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
32-207 |
1.79e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 32 ITGILGPNGAGKTSVLKAICGLHYQSSGtvricGTEETDEFKKATAFVPEIPELDSSLTVKEILFFEAEISGQKKN-EAD 110
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDAL-----VIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRyRYG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 111 LTVKKAAticgLEEVFNKKISKLSKGFKQRTSLAKAICKLPkILVLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHH 190
Cdd:pfam13304 76 LDLERED----VEEKLSSKPTLLEKRLLLREDSEEREPKFP-PEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISP 150
|
170
....*....|....*..
gi 2540524722 191 IEEAVSMCNRIYIIANG 207
Cdd:pfam13304 151 LSFLLLLDEGLLLEDWA 167
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-221 |
2.70e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 41.73 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 18 SACKNINFYAEKNSITGILGPNGAGKTSVLKAICgLHYQ-SSGTVRICGTEETD----EFKKATAFVPEIPELDSSlTVK 92
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWDpQQGEILLNGQPIADyseaALRQAISVVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 93 EILFFEAEisgqKKNEADLTVkkAATICGLEEVFNKKIS----------KLSKGFKQRTSLAKAICKLPKILVLDEFSAG 162
Cdd:PRK11160 432 DNLLLAAP----NASDEALIE--VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 163 LDPA---QIasfrkkLKNLSSSM---TIIFSTHHIEEAVSMcNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK11160 506 LDAEterQI------LELLAEHAqnkTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
12-189 |
2.96e-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: 41.14 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSACkNINFyaeKNSITGILGPNGAGKTSVLKAICGLhYQSSGTVRIcgteETDEFKKATAFVPEIPELDssLTV 91
Cdd:COG3593 9 KNFRSIKDL-SIEL---SDDLTVLVGENNSGKSSILEALRLL-LGPSSSRKF----DEEDFYLGDDPDLPEIEIE--LTF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 92 KEIL--FFEAEISGQKKNE-----ADLTVKKAATICGLEEVFNKK----------------------------------- 129
Cdd:COG3593 78 GSLLsrLLRLLLKEEDKEEleealEELNEELKEALKALNELLSEYlkelldgldlelelsldeledllkslslriedgke 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 130 --ISKLSKGFKQRTSLA--KAICKL-----PKILVLDEFSAGLDPAQIASFRKKLKNLSS-SMTIIFSTH 189
Cdd:COG3593 158 lpLDRLGSGFQRLILLAllSALAELkrapaNPILLIEEPEAHLHPQAQRRLLKLLKELSEkPNQVIITTH 227
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-221 |
3.34e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 41.24 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 4 EVELISFCKNYGKfSACKNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICG----TEETDEFKKATAFV 79
Cdd:PRK10790 342 DIDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGrplsSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 80 PEIPEL--DSsltvkeilFFE-----AEISGQKKNEADLTVKKAATICGLEEVFNKKI----SKLSKGFKQRTSLAKAIC 148
Cdd:PRK10790 421 QQDPVVlaDT--------FLAnvtlgRDISEEQVWQALETVQLAELARSLPDGLYTPLgeqgNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540524722 149 KLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHHIEEAVSmCNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
12-51 |
4.12e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 40.33 E-value: 4.12e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2540524722 12 KNYGKFSACKNINFYA-EKNSITGILGPNGAGKTSVLKAIC 51
Cdd:cd03279 9 KNFGPFREEQVIDFTGlDNNGLFLICGPTGAGKSTILDAIT 49
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
21-206 |
4.58e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.90 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSI------TGILGPNGAGKTSVLKAIcglhyqssgtvRICGTEETDEFKKATAFVPE-IPELDSSLTVKe 93
Cdd:cd03240 7 RNIRSFHERSEIeffsplTLIVGQNGAGKTTIIEAL-----------KYALTGELPPNSKGGAHDPKlIREGEVRAQVK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 94 iLFFEAEISGQKKNEADLTVKKAATICGLEEvFNK----KISKLSKGFKQ------RTSLAKAIC-KLPkILVLDEFSAG 162
Cdd:cd03240 75 -LAFENANGKKYTITRSLAILENVIFCHQGE-SNWplldMRGRCSGGEKVlasliiRLALAETFGsNCG-ILALDEPTTN 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2540524722 163 LDP-------AQIASFRKKLKNlsssMTIIFSTHHiEEAVSMCNRIYIIAN 206
Cdd:cd03240 152 LDEenieeslAEIIEERKSQKN----FQLIVITHD-EELVDAADHIYRVEK 197
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-221 |
4.87e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.73 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 23 INFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTEETDEfkKATAFVPEIpeldsSLTVKEILFFEAEIS 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE--QPEDYRKLF-----SAVFTDFHLFDQLLG 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 103 GQKKNEADLTVKKAATICGLE---EVFNKKIS--KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKN 177
Cdd:PRK10522 415 PEGKPANPALVEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLP 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2540524722 178 LSSSMTI-IFSTHHIEEAVSMCNRIYIIANGEVAAC-GTEKEIVKK 221
Cdd:PRK10522 495 LLQEMGKtIFAISHDDHYFIHADRLLEMRNGQLSELtGEERDAASR 540
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
127-201 |
6.61e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 6.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2540524722 127 NKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSmtIIFSTHHIEEAVSMCNRI 201
Cdd:PRK11147 151 DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS--IIFISHDRSFIRNMATRI 223
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
12-50 |
7.46e-04 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.98 E-value: 7.46e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2540524722 12 KNYGKFSACKnINFYAEKNsITGILGPNGAGKTSVLKAI 50
Cdd:COG3950 9 ENFRGFEDLE-IDFDNPPR-LTVLVGENGSGKTTLLEAI 45
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
132-209 |
1.05e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.69 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 132 KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLD---PAQIASFRKKLKNlSSSMTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDvsvQAQILQLLRELQQ-ELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
.
gi 2540524722 209 V 209
Cdd:PRK15134 235 C 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-189 |
1.09e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.83 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 32 ITGILGPNGAGKTSVLKAICGLHYQS--SGTVRICG-TEETDEFKKATAFVPEIPELDSSLTVKEILFFEA------EIS 102
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAflrlpkEVS 987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 103 gqkKNEADLTVKKAATICGLEEVFNK-----KISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKN 177
Cdd:PLN03140 988 ---KEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
|
170
....*....|...
gi 2540524722 178 -LSSSMTIIFSTH 189
Cdd:PLN03140 1065 tVDTGRTVVCTIH 1077
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
5-51 |
1.20e-03 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 38.73 E-value: 1.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2540524722 5 VELISF-CKNYGKFSACKNINFyaeknsitgILGPNGAGKTSVLKAIC 51
Cdd:cd03276 4 ITLKNFmCHRHLQIEFGPRVNF---------IVGNNGSGKSAILTALT 42
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
121-221 |
2.12e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 38.85 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 121 GLEEVFNKKISKLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDPAQIASFRKKLKNLSSSMTIIFSTHH---IEEAvsm 197
Cdd:PRK11176 469 GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRlstIEKA--- 545
|
90 100
....*....|....*....|....
gi 2540524722 198 cNRIYIIANGEVAACGTEKEIVKK 221
Cdd:PRK11176 546 -DEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-210 |
2.17e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.94 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 21 KNINFYAEKNSITGILGPNGAGKTSVLKAICGLHYQSSGTVRICGTE-----ETDEFKKATAFVPE-------------- 81
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKinnhnANEAINHGFALVTEerrstgiyayldig 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 82 ----IPELDSSLTVKEILffeaeisGQKKNEAD-------LTVKKAAticgleevFNKKISKLSKGFKQRTSLAKAICKL 150
Cdd:PRK10982 345 fnslISNIRNYKNKVGLL-------DNSRMKSDtqwvidsMRVKTPG--------HRTQIGSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2540524722 151 PKILVLDEFSAGLDPAQ-------IASFRKKLKNlsssmtIIFSTHHIEEAVSMCNRIYIIANGEVA 210
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAkfeiyqlIAELAKKDKG------IIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
7-97 |
2.72e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.10 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 7 LISF-CKNYGKFSACKNINFYAEKNS---ITGILGPNGAGKTSVLKAIcglhYQSSGTVRIcGTEETDEFKKATAFVPEI 82
Cdd:COG1106 2 LISFsIENFRSFKDELTLSMVASGLRllrVNLIYGANASGKSNLLEAL----YFLRNLVLN-SSQPGDKLVEPFLLDSES 76
|
90
....*....|....*
gi 2540524722 83 PELDSSLtvkEILFF 97
Cdd:COG1106 77 KNEPSEF---EILFL 88
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
12-139 |
2.85e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 12 KNYGKFSAcKNINFyaeKNSITGILGPNGAGKTSVLKAIC-GLHYQSSGTVRICGTEETD-----EFKKATAFVPEIPEL 85
Cdd:pfam13476 4 ENFRSFRD-QTIDF---SKGLTLITGPNGSGKTTILDAIKlALYGKTSRLKRKSGGGFVKgdiriGLEGKGKAYVEITFE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2540524722 86 DSSLTVKEILFFEAEISGQKKNEADLTVKKAATICGLEEVFNKKISKLSKGFKQ 139
Cdd:pfam13476 80 NNDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPL 133
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
127-221 |
3.02e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 127 NKKISKLSKGFKQRTSLAKAI-CKLPKIL-VLDEFSAGL---DPAQIASFRKKLKNLSSSMTIIfstHHIEEAVSMCNRI 201
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLhqrDNRRLINTLKRLRDLGNTLIVV---EHDEDTIRAADYV 559
|
90 100
....*....|....*....|....*.
gi 2540524722 202 YIIA------NGEVAACGTEKEIVKK 221
Cdd:TIGR00630 560 IDIGpgagehGGEVVASGTPEEILAN 585
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
23-51 |
3.09e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 38.63 E-value: 3.09e-03
10 20 30
....*....|....*....|....*....|..
gi 2540524722 23 INFYAE---KNSITGILGPNGAGKTSVLKAIC 51
Cdd:PRK10246 20 IDFTAEpfaSNGLFAITGPTGAGKTTLLDAIC 51
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
132-219 |
7.56e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 37.09 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540524722 132 KLSKGFKQRTSLAKAICKLPKILVLDEFSAGLDP---AQIASFRKKLkNLSSSMTIIFSTHHIEEAVSMCNRIYIIANGE 208
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPttqAQIFRLLTRL-NQNNNTTILLISHDLQMLSQWADKINVLYCGQ 236
|
90
....*....|.
gi 2540524722 209 VAACGTEKEIV 219
Cdd:PRK15093 237 TVETAPSKELV 247
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
32-50 |
8.02e-03 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 36.67 E-value: 8.02e-03
|
| |
