|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-212 |
1.13e-69 |
|
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: 211.94 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 4 LNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLF 83
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 84 QEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEP 163
Cdd:cd03225 82 QNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446879615 164 SRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-223 |
1.29e-64 |
|
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: 199.87 E-value: 1.29e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLD 161
Cdd:COG1122 80 VFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 162 EPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-223 |
6.23e-43 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.93 E-value: 6.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLD 161
Cdd:PRK13635 86 VFQNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 162 EPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHD---AAFTrrhfSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13635 166 EATSMLDpRGRREVLETVRQLKEQKGITVLSITHDldeAAQA----DRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-214 |
1.86e-42 |
|
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: 142.40 E-value: 1.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 3 TLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQqamKNLKNRQRAAKVGVL 82
Cdd:cd03226 1 RIENISFSYKKG-TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 83 FQEAENQLFHSTVADEIAFGLKlqkcPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:cd03226 77 MQDVDYQLFTDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446879615 163 PSRDFD-ENWLSVFEsWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03226 153 PTSGLDyKNMERVGE-LIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.70e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 147.36 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTA---GTVMLQQQAMKNLKNRQRAA 77
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPL 157
Cdd:COG1123 84 RIGMVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 158 LLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG1123 164 LIADEPTTALDvTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-214 |
1.03e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.95 E-value: 1.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA--- 77
Cdd:COG2884 1 MIRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVLFQEAenQL-FHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLhSA---QRrmVAVAclEAL 153
Cdd:COG2884 80 RIGVVFQDF--RLlPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHEL-SGgeqQR--VAIA--RAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 154 --SPPLLLLDEPSRDFD-ENwlsvfeSW-----LEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:COG2884 153 vnRPELLLADEPTGNLDpET------SWeimelLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.55e-39 |
|
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: 141.96 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATDC---LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA 77
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 ---KVGVLFQEAENQLFHS-TVADEIAFGLKLQK-CPADEITQRTHAALQCCQL-ADTANSHPLDLHSAQRRMVAVACLE 151
Cdd:COG1123 340 lrrRVQMVFQDPYSSLNPRmTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 152 ALSPPLLLLDEPSrdfdenwlsvfeSWLEKCGQ-------------RGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVN 218
Cdd:COG1123 420 ALEPKLLILDEPT------------SALDVSVQaqilnllrdlqreLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....*
gi 446879615 219 PPDDI 223
Cdd:COG1123 488 PTEEV 492
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-223 |
4.23e-39 |
|
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: 135.64 E-value: 4.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 4 LNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKN----RQraaKV 79
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlweiRK---KV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 GVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLL 159
Cdd:TIGR04520 80 GMVFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIII 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 160 LDEPSRDFD----ENWLSVFESwLEKcgQRGTSVVAISHD---AAFTrrhfSRVVRLEDGLIRNVNPPDDI 223
Cdd:TIGR04520 160 LDEATSMLDpkgrKEVLETIRK-LNK--EEGITVISITHDmeeAVLA----DRVIVMNKGKIVAEGTPREI 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
19-225 |
9.77e-39 |
|
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: 134.00 E-value: 9.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGVLFQEAenQLF-HSTVAD 97
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVGFVFQHY--ALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 98 EIAFGLKLQK----CPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLS 173
Cdd:cd03296 94 NVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 174 VFESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI--HP 225
Cdd:cd03296 174 ELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVydHP 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
7.58e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.32 E-value: 7.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWP--GAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA- 77
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 ---KVGVLFQEAenQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACleAL 153
Cdd:COG1136 84 rrrHIGFVFQFF--NLLpELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR--AL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446879615 154 --SPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRhFSRVVRLEDGLI 214
Cdd:COG1136 160 vnRPKLILADEPTGNLDsKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
1.35e-37 |
|
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: 130.30 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWP--GAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA-- 77
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 --KVGVLFQEAeNQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVAclEAL-- 153
Cdd:cd03255 81 rrHIGFVFQSF-NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA--RALan 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 154 SPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRhFSRVVRLEDGLI 214
Cdd:cd03255 158 DPKIILADEPTGNLDsETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-214 |
2.53e-37 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 129.45 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 6 KISYRWPGAATdCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRA---AKVGVL 82
Cdd:cd03292 5 NVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 83 FQEAEnQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:cd03292 84 FQDFR-LLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446879615 163 PSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-223 |
4.06e-36 |
|
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: 127.47 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:COG1120 1 MLEAENLSVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAENQlFHSTVADEIAFG----LKLQKCPADEITQRTHAALQCCQLADTANsHPLD-LHSAQRRMVAVACLEALSP 155
Cdd:COG1120 79 YVPQEPPAP-FGLTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLAD-RPVDeLSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 156 PLLLLDEPSRDFDENW-LSVFESWLEKCGQRGTSVVAISHD---AAftrRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG1120 157 PLLLLDEPTSHLDLAHqLEVLELLRRLARERGRTVVMVLHDlnlAA---RYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-224 |
2.13e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 125.04 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGVLFQEAenQLF-HSTVADEI 99
Cdd:cd03300 18 GVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR--PVNTVFQNY--ALFpHLTVFENI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPsrdfdenwLSVFESWL 179
Cdd:cd03300 94 AFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP--------LGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446879615 180 EKCGQR---------GTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDIH 224
Cdd:cd03300 166 RKDMQLelkrlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-163 |
6.51e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 126.75 E-value: 6.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPG-AATDclcDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKV 79
Cdd:COG3842 5 ALELENVSKRYGDvTALD---DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR--NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 GVLFQE-AenqLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLhS---AQRrmVAVA-CLeAL 153
Cdd:COG3842 80 GMVFQDyA---LFpHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQL-SggqQQR--VALArAL-AP 152
|
170
....*....|
gi 446879615 154 SPPLLLLDEP 163
Cdd:COG3842 153 EPRVLLLDEP 162
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-163 |
1.27e-34 |
|
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: 120.45 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQeaENQLF-HSTVADEI 99
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQ--DPQLFpRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSA----QRRMVAVACLEALSPPLLLLDEP 163
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGERPGTlsggQRQRVAIARALLTKPKLLLLDEP 148
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-195 |
1.30e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.66 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKIS--YRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAmknlkNRQRAAK 78
Cdd:COG1116 7 ALELRGVSkrFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 79 VGVLFQEAenQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLhS---AQRrmVAVA-CLeAL 153
Cdd:COG1116 82 RGVVFQEP--ALLpWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQL-SggmRQR--VAIArAL-AN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446879615 154 SPPLLLLDEP-------SRDFDENWLsvfeswLEKCGQRGTSVVAISHD 195
Cdd:COG1116 156 DPEVLLMDEPfgaldalTRERLQDEL------LRLWQETGKTVLFVTHD 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
16-224 |
1.94e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 126.22 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 16 TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGVLFQEAenQLF-HST 94
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR--HVNTVFQSY--ALFpHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPsrdfdenwLSV 174
Cdd:PRK09452 103 VFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES--------LSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 175 FESWLEKCGQR---------GTSVVAISHDA--AFTRRhfSRVVRLEDGLIRNVNPPDDIH 224
Cdd:PRK09452 175 LDYKLRKQMQNelkalqrklGITFVFVTHDQeeALTMS--DRIVVMRDGRIEQDGTPREIY 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-195 |
3.17e-34 |
|
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: 121.81 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 8 SYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMknlknRQRAAKVGVLFQEAe 87
Cdd:cd03293 9 TYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDRGYVFQQD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 88 nQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLeALSPPLLLLDEPSR 165
Cdd:cd03293 83 -ALLpWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALArAL-AVDPDVLLLDEPFS 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 446879615 166 DFDE-------NWLsvfeswLEKCGQRGTSVVAISHD 195
Cdd:cd03293 161 ALDAltreqlqEEL------LDIWRETGKTVLLVTHD 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-163 |
3.64e-34 |
|
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: 121.47 E-value: 3.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGaaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGV 81
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLeALSPPLLL 159
Cdd:cd03259 77 VFQDY--ALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALArAL-AREPSLLL 153
|
....
gi 446879615 160 LDEP 163
Cdd:cd03259 154 LDEP 157
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-197 |
1.06e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 119.45 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 16 TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM----KNLKNRQRaaKVGVLFQEAENQLF 91
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysrKGLLERRQ--RVGLVFQDPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 92 HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENW 171
Cdd:TIGR01166 83 AADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|....*.
gi 446879615 172 LSVFESWLEKCGQRGTSVVAISHDAA 197
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTHDVD 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
2.01e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKN-----LKNRQr 75
Cdd:PRK13639 1 ILETRDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkkslLEVRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 76 aaKVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSP 155
Cdd:PRK13639 79 --TVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 156 PLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-225 |
7.08e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 121.41 E-value: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGaaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ-QQAMKNLKNRQRaaKVG 80
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgRDLFTNLPPRER--RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAenQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVAclEALS--PPL 157
Cdd:COG1118 79 FVFQHY--ALFpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALA--RALAvePEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 158 LLLDEP-------SRDFDENWLSVFeswLEKCGqrGTSVVaISHD-------AaftrrhfSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG1118 155 LLLDEPfgaldakVRKELRRWLRRL---HDELG--GTTVF-VTHDqeealelA-------DRVVVMNQGRIEQVGTPDEV 221
|
....
gi 446879615 224 --HP 225
Cdd:COG1118 222 ydRP 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
21-211 |
8.10e-33 |
|
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: 117.58 E-value: 8.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKnRQRAAKVGVLFQEAE--NQLfhsTVADE 98
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGlkPEL---TVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQKCPADEItqRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFESW 178
Cdd:COG4133 96 LRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAEL 173
|
170 180 190
....*....|....*....|....*....|...
gi 446879615 179 LEKCGQRGTSVVAISHDAAFTRrhFSRVVRLED 211
Cdd:COG4133 174 IAAHLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-220 |
9.32e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.45 E-value: 9.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM--KNLKNRQRaaKVGVLFQEAENQLFHSTVA 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLteENVWDIRH--KIGMVFQNPDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD-ENWLSVF 175
Cdd:PRK13650 101 DDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpEGRLELI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446879615 176 ESWLEKCGQRGTSVVAISHD---AAFTrrhfSRVVRLEDGLIRNVNPP 220
Cdd:PRK13650 181 KTIKGIRDDYQMTVISITHDldeVALS----DRVLVMKNGQVESTSTP 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
21-223 |
2.30e-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: 117.39 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA---KVGVLFQEAenQLFHS-TVA 96
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrrRIGMLFQGG--ALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLK-LQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLeALSPPLLLLDEP--------SRD 166
Cdd:COG1127 101 ENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALArAL-ALDPEILLYDEPtagldpitSAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 167 FDEnwlsvfeswL--EKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG1127 180 IDE---------LirELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-223 |
3.54e-32 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 123.02 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQeaENQLFHSTVADEIAFGlklqkcpADEITQrtHAALQCCQLA---DTANSHPLDLHSA-----------QRRMVAV 147
Cdd:COG2274 554 VLQ--DVFLFSGTIRENITLG-------DPDATD--EEIIEAARLAglhDFIEALPMGYDTVvgeggsnlsggQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 148 ACLEALSPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRgtSVVAISHDAAfTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG2274 623 ARALLRNPRILILDEATSALDaETEAIILENLRRLLKGR--TVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-223 |
1.56e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.88 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 16 TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGVLFQEAenQLF-HST 94
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVGFVFQHY--ALFrHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFGLKL----QKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDEN 170
Cdd:PRK10851 91 VFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 171 WLSVFESWLEKCGQ--RGTSVVaISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK10851 171 VRKELRRWLRQLHEelKFTSVF-VTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
21-224 |
7.85e-31 |
|
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: 113.37 E-value: 7.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA---KVGVLFQeaENQLFHS-TVA 96
Cdd:cd03261 18 GVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRMGMLFQ--SGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLK-LQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVF 175
Cdd:cd03261 96 ENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446879615 176 ESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDIH 224
Cdd:cd03261 176 DDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
8.87e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 114.08 E-value: 8.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLL 160
Cdd:PRK13648 87 IVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446879615 161 DEPSRDFDENWLSVFESWLEKCGQ-RGTSVVAISHDAAFTrRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13648 167 DEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEI 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-163 |
1.00e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.56 E-value: 1.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWpgAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVG 80
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQE-AenqLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLeALSPPL 157
Cdd:COG3839 79 MVFQSyA---LYpHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGrAL-VREPKV 154
|
....*.
gi 446879615 158 LLLDEP 163
Cdd:COG3839 155 FLLDEP 160
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-225 |
3.76e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.59 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTP--------TAGTVMLQQQAMKNLKNr 73
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVWDIRE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 74 qraaKVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEAL 153
Cdd:PRK13640 85 ----KVGIVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 154 SPPLLLLDEPSRDFD----ENWLSVFESWLEKcgqRGTSVVAISHDAAfTRRHFSRVVRLEDGLIRNVNPPDDIHP 225
Cdd:PRK13640 161 EPKIIILDESTSMLDpagkEQILKLIRKLKKK---NNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
21-225 |
4.71e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 114.55 E-value: 4.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAakVGVLFQEAenQLF-HSTVADEI 99
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--INMMFQSY--ALFpHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENW-----LSV 174
Cdd:PRK11607 113 AFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmqLEV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446879615 175 FESwLEKCgqrGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI--HP 225
Cdd:PRK11607 193 VDI-LERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIyeHP 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-223 |
5.81e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.42 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRW-PGA--ATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM------KNLKN 72
Cdd:PRK13634 3 ITFQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 73 -RQraaKVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSH-PLDLHSAQRRMVAVACL 150
Cdd:PRK13634 83 lRK---KVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 151 EALSPPLLLLDEPSRDFD----ENWLSVFESwLEKcgQRGTSVVAISH---DAAftrRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDpkgrKEMMEMFYK-LHK--EKGLTTVLVTHsmeDAA---RYADQIVVMHKGTVFLQGTPREI 233
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-223 |
9.37e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 111.75 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRW-PGA--ATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVML---------QQQAMK 68
Cdd:PRK13643 1 MIKFEKVNYTYqPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 69 NLKNrqraaKVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLA-DTANSHPLDLHSAQRRMVAV 147
Cdd:PRK13643 81 PVRK-----KVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 148 ACLEALSPPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-212 |
9.47e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 111.37 E-value: 9.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 7 ISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEA 86
Cdd:PRK13647 10 LHFRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 87 ENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRD 166
Cdd:PRK13647 89 DDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 167 FDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-214 |
1.69e-29 |
|
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: 109.16 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRA--AKVGVLFQEAEnqLF-HSTV 95
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQKVGMVFQQFN--LFpHLTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ADEIAFGL-KLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENW--- 171
Cdd:cd03262 94 LENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELvge 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446879615 172 -LSVfeswLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03262 174 vLDV----MKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-214 |
2.66e-29 |
|
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: 109.21 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKIS--YRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKN---RQR 75
Cdd:cd03258 1 MIELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 76 AAKVGVLFQEAenQLFHS-TVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALS 154
Cdd:cd03258 81 RRRIGMIFQHF--NLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 155 PPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03258 159 PKVLLCDEATSALDpETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-223 |
9.27e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.92 E-value: 9.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAK-V 79
Cdd:PRK13644 1 MIRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 GVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLL 159
Cdd:PRK13644 80 GIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 160 LDEPSRDFD-ENWLSVFESwLEKCGQRGTSVVAISHDaaFTRRHFS-RVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13644 160 FDEVTSMLDpDSGIAVLER-IKKLHEKGKTIVYITHN--LEELHDAdRIIVMDRGKIVLEGEPENV 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-212 |
9.50e-29 |
|
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: 105.79 E-value: 9.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQeaenqlfhstvadeia 100
Cdd:cd00267 17 NVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 101 fglklqkcpadeitqrthaalqccqladtanshpldLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD-ENWLSVFEsWL 179
Cdd:cd00267 81 ------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDpASRERLLE-LL 123
|
170 180 190
....*....|....*....|....*....|...
gi 446879615 180 EKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:cd00267 124 RELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-217 |
1.65e-28 |
|
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: 106.57 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGaaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGV 81
Cdd:cd03301 1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR--DIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLL 160
Cdd:cd03301 77 VFQNY--ALYpHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 161 DEPSRDFDENWLSVFESWLEKCGQR-GTSVVAISHD--AAFTRRHfsRVVRLEDGLIRNV 217
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDqvEAMTMAD--RIAVMNDGQIQQI 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-168 |
2.49e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.21 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 15 ATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ--QQAMKNLKNRQRAAKVGVLFQEAENQLFH 92
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvDITDKKVKLSDIRKKVGLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 93 STVADEIAFGLKLQKCPADEITQRTHAALQCCQLA--DTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-212 |
4.07e-28 |
|
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: 104.82 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 3 TLNKISYRWPGaaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVL 82
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 83 FQeaenqlfhstvadeiafglklqkcpadeitqrthaALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:cd03214 79 PQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446879615 163 P--SRDFDeNWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:cd03214 124 PtsHLDIA-HQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-162 |
5.23e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 5.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLL 160
Cdd:PRK13632 87 IIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
..
gi 446879615 161 DE 162
Cdd:PRK13632 167 DE 168
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-215 |
6.34e-28 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 105.07 E-value: 6.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKqGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ-------QQAMkNLKNRQRaaKVGVLFQEAenQLF-H 92
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsRKKI-NLPPQQR--KIGLVFQQY--ALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 93 STVADEIAFGLKlqKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWL 172
Cdd:cd03297 90 LNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446879615 173 SVFESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDGLIR 215
Cdd:cd03297 168 LQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-223 |
7.49e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 105.61 E-value: 7.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATDclcdISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVG 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPLR----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER--PVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQeaENQLF-HSTVADEIAFG----LKLqkcpADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLeaLS 154
Cdd:COG3840 75 MLFQ--ENNLFpHLTVAQNIGLGlrpgLKL----TAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALArCL--VR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 155 P-PLLLLDEPsrdF--------DE--NWLSvfeswlEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG3840 147 KrPILLLDEP---FsaldpalrQEmlDLVD------ELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-214 |
1.02e-27 |
|
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: 105.34 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLK---NRQRAAK 78
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 79 VGVLFQE---------AENQL-----FHSTVADeiAFGLklqkCPADEItQRTHAALQCCQLADTANSHPLDLHSAQRRM 144
Cdd:cd03256 80 IGMIFQQfnlierlsvLENVLsgrlgRRSTWRS--LFGL----FPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 145 VAVACLEALSPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDpASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-212 |
1.41e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM----KNLKNRQRA 76
Cdd:PRK13636 5 ILKVEELNYNYSDG-THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 77 akVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPP 156
Cdd:PRK13636 84 --VGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 157 LLLLDEPSRDFDENWLS-VFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSeIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-214 |
2.08e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 109.08 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:COG4988 337 IELEDVSFSYPGGRPA-LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLFHSTVADEIAFGlklqKCPADEitQRTHAALQCCQLADTANSHPLDLHSA-----------QRRMVAVAcl 150
Cdd:COG4988 416 VPQNP--YLFAGTIRENLRLG----RPDASD--EELEAALEAAGLDEFVAALPDGLDTPlgeggrglsggQAQRLALA-- 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 151 EAL--SPPLLLLDEPSRDFD-ENWLSVFESWLEKCgqRGTSVVAISHDAAfTRRHFSRVVRLEDGLI 214
Cdd:COG4988 486 RALlrDAPLLLLDEPTAHLDaETEAEILQALRRLA--KGRTVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-214 |
3.29e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 103.74 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 16 TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA----KVGVLFQeaenqlF 91
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQ------F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 92 HSTVAD-----EIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRD 166
Cdd:PRK11629 96 HHLLPDftaleNVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446879615 167 FDE-NWLSVFESWLEKCGQRGTSVVAISHDAAFTRRhFSRVVRLEDGLI 214
Cdd:PRK11629 176 LDArNADSIFQLLGELNRLQGTAFLVVTHDLQLAKR-MSRQLEMRDGRL 223
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-222 |
4.28e-27 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 104.04 E-value: 4.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:COG4559 1 MLEAENLSVRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAenQL-FHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLhS---AQR----RMVA-VACLE 151
Cdd:COG4559 79 VLPQHS--SLaFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTL-SggeQQRvqlaRVLAqLWEPV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 152 ALSPPLLLLDEPSRDFDENW-LSVFESwLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDD 222
Cdd:COG4559 156 DGGPRWLFLDEPTSALDLAHqHAVLRL-ARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-194 |
6.02e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.44 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRW------PGAAtdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM----KNLK 71
Cdd:PRK13649 3 INLQNVSYTYqagtpfEGRA---LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 72 NRQRAAKVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTA-NSHPLDLHSAQRRMVAVACL 150
Cdd:PRK13649 80 IKQIRKKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446879615 151 EALSPPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-195 |
1.06e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.63 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM--KNLKNRQRaaKVGVLFQEAENQLFHSTVADEI 99
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaENVWNLRR--KIGMVFQNPDNQFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFESWL 179
Cdd:PRK13642 104 AFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170
....*....|....*..
gi 446879615 180 EKCGQR-GTSVVAISHD 195
Cdd:PRK13642 184 HEIKEKyQLTVLSITHD 200
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
2.56e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 101.70 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRqraakVG 80
Cdd:COG1121 6 AIELENLTVSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAE-NQLFHSTVADEIAFGL----KLQKCPADEITQRTHAALQCCQLADTANsHPLDLHSA-QRRMVAVA-CLeAL 153
Cdd:COG1121 79 YVPQRAEvDWDFPITVRDVVLMGRygrrGLFRRPSRADREAVDEALERVGLEDLAD-RPIGELSGgQQQRVLLArAL-AQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 154 SPPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRnVNPPDDI 223
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVA-HGPPEEV 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-219 |
6.05e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 6.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 6 KISYRW-PGAA--TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVML------QQQAMKNLKNRQRa 76
Cdd:PRK13641 7 NVDYIYsPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitPETGNKNLKKLRK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 77 aKVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLA-DTANSHPLDLHSAQRRMVAVACLEALSP 155
Cdd:PRK13641 86 -KVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 156 PLLLLDEPSRDFD-ENWLSVFESWLEKcgQR-GTSVVAISHDAAFTRRHFSRVVRLEDG-LIRNVNP 219
Cdd:PRK13641 165 EILCLDEPAAGLDpEGRKEMMQLFKDY--QKaGHTVILVTHNMDDVAEYADDVLVLEHGkLIKHASP 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-214 |
8.06e-26 |
|
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: 99.97 E-value: 8.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQeaENQLFHSTVADEIAFGLKLqkcpADEitQRTHAALQCCQLADTANSHP--LD---------LHSAQRRMVAVACL 150
Cdd:cd03245 83 VPQ--DVTLFYGTLRDNITLGAPL----ADD--ERILRAAELAGVTDFVNKHPngLDlqigergrgLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 151 EALSPPLLLLDEPSRDFDEN----WLSVFESWLekcgqRGTSVVAISHDAAFTRRhFSRVVRLEDGLI 214
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNseerLKERLRQLL-----GDKTLIIITHRPSLLDL-VDRIIVMDSGRI 216
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-212 |
8.45e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 99.95 E-value: 8.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRA---AKVGVLFQEaENQLFHSTVADE 98
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMIFQD-HHLLMDRTVYDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD----ENWLSV 174
Cdd:PRK10908 100 VAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalsEGILRL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 446879615 175 FESWlekcGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK10908 180 FEEF----NRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-212 |
2.08e-25 |
|
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: 97.45 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLFHSTVADEIafglklqkcpadeitqrthaalqccqladtanshpldLHSAQRRMVAVAclEAL--SPPLLL 159
Cdd:cd03228 81 VPQDP--FLFSGTIRENI-------------------------------------LSGGQRQRIAIA--RALlrDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446879615 160 LDEPSRDFD-ENWLSVFESWLEKCGQRgtSVVAISHDAAfTRRHFSRVVRLEDG 212
Cdd:cd03228 120 LDEATSALDpETEALILEALRALAKGK--TVIVIAHRLS-TIRDADRIIVLDDG 170
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
19-223 |
2.97e-25 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 98.60 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKnlKNRQRA-AKVGVLFQEAEnqLF-HSTVA 96
Cdd:COG1131 16 LDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVrRRIGYVPQEPA--LYpDLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACleALS--PPLLLLDEPSRDFDENWLSV 174
Cdd:COG1131 92 ENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLAL--ALLhdPELLILDEPTSGLDPEARRE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446879615 175 FESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG1131 170 LWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-223 |
3.20e-25 |
|
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: 98.78 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaAKVG 80
Cdd:COG4555 1 MIEVENLSKKYGKVPA--LKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQeaENQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLL 159
Cdd:COG4555 78 VLPD--ERGLYdRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446879615 160 LDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-223 |
3.78e-25 |
|
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: 98.41 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLL-----TPTAGTVMLQQQAMKNLKNRQRA--AKVGVLFQEAenQLFHS 93
Cdd:cd03260 18 DISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElrRRVGMVFQKP--NPFPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEIAFGLKLQKC-PADEITQRTHAALQCCQLADTAN--SHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDEN 170
Cdd:cd03260 96 SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446879615 171 WLSVFESWLEKCGQRgTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:cd03260 176 STAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-163 |
5.75e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.15 E-value: 5.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKIS--YRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQ-RAA 77
Cdd:COG1135 1 MIELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 --KVGVLFQEAeNqLFHS-TVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLeAL 153
Cdd:COG1135 81 rrKIGMIFQHF-N-LLSSrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIArAL-AN 157
|
170
....*....|
gi 446879615 154 SPPLLLLDEP 163
Cdd:COG1135 158 NPKVLLCDEA 167
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-223 |
6.52e-25 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 98.48 E-value: 6.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQ----RAAKVGVLFQEAenQLF-HSTV 95
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelRRKKISMVFQSF--ALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEP--------SRDF 167
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAfsaldpliRREM 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 168 DENWLSvfeswLEKcgQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:cd03294 200 QDELLR-----LQA--ELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
21-214 |
6.67e-25 |
|
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: 97.58 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQ---RAAKVGVLFQEAenqlFHS---- 93
Cdd:cd03257 23 DVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiRRKEIQMVFQDP----MSSlnpr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 -TVADEIAFGLKLQKCPADEITQRTHAALQCCQL---ADTANSHPLDLhS---AQRRMVAVAcLeALSPPLLLLDEPSRD 166
Cdd:cd03257 99 mTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHEL-SggqRQRVAIARA-L-ALNPKLLIADEPTSA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446879615 167 FD----ENWLSVFeswLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03257 176 LDvsvqAQILDLL---KKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-222 |
7.30e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 7.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAeNQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLEALS----- 154
Cdd:PRK13548 80 VLPQHS-SLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVLAQLWepdgp 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 155 PPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDD 222
Cdd:PRK13548 159 PRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-223 |
9.04e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.70 E-value: 9.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQ----QAMKNLKNRQRAAKVGVLFQEAENQLFHST 94
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQFPESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFGLKLQKCPADEITQRTHAALQccQLA---DTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDEN- 170
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVKNYAHRLLM--DLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQs 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 171 ---WLSVFESWLEKcgqRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13646 181 krqVMRLLKSLQTD---ENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-162 |
2.27e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKIS--YRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQ-RAA 77
Cdd:PRK11153 1 MIELKNISkvFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 --KVGVLFQEAeNQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSP 155
Cdd:PRK11153 81 rrQIGMIFQHF-NLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
....*..
gi 446879615 156 PLLLLDE 162
Cdd:PRK11153 160 KVLLCDE 166
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-194 |
2.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.47 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRW----PGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKN---- 72
Cdd:PRK13633 4 MIKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 73 RQRAakvGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEA 152
Cdd:PRK13633 84 RNKA---GMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446879615 153 LSPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:PRK13633 161 MRPECIIFDEPTAMLDpSGRREVVNTIKELNKKYGITIILITH 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-214 |
2.67e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 95.96 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAAT--DCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA- 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 ---KVGVLFQEaenqlFH----STVADEIAFGLKLQkcPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACL 150
Cdd:COG4181 88 rarHVGFVFQS-----FQllptLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 151 EALSPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRhFSRVVRLEDGLI 214
Cdd:COG4181 161 FATEPAILFADEPTGNLDaATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRL 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-214 |
3.52e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.80 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATDclcdISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAakVG 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQeaENQLF-HSTVADEIAFG----LKL---QKCPADEITQRThaalqccQLADTANSHPLDLHSAQRRMVAVACLEA 152
Cdd:PRK10771 75 MLFQ--ENNLFsHLTVAQNIGLGlnpgLKLnaaQREKLHAIARQM-------GIEDLLARLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 153 LSPPLLLLDEPSRDFD----ENWLSVFEswlEKCGQRGTSVVAISH---DAAftrRHFSRVVRLEDGLI 214
Cdd:PRK10771 146 REQPILLLDEPFSALDpalrQEMLTLVS---QVCQERQLTLLMVSHsleDAA---RIAPRSLVVADGRI 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-214 |
4.80e-24 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 94.87 E-value: 4.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDclcdISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAakVGV 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMH----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQeaENQLF-HSTVADEIAFGL--KLQKCPADEitQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLL 158
Cdd:cd03298 75 LFQ--ENNLFaHLTVEQNVGLGLspGLKLTAEDR--QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 159 LLDEPSRDFD----ENWLSVFeswLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03298 151 LLDEPFAALDpalrAEMLDLV---LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
6.94e-24 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.97 E-value: 6.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAAtDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:TIGR02868 335 LELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLFHSTVADEIAFGLKlqKCPADEITqrthAALQCCQLADTANSHPLDLHS-----------AQRRMVAVACL 150
Cdd:TIGR02868 414 CAQDA--HLFDTTVRENLRLARP--DATDEELW----AALERVGLADWLRALPDGLDTvlgeggarlsgGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 151 EALSPPLLLLDEPSRDFD-ENWLSVFESWLEkcGQRGTSVVAISHD 195
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDaETADELLEDLLA--ALSGRTVVLITHH 529
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
21-168 |
1.38e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 96.64 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAakVGVLFQEAenQLF-HSTVADEI 99
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQSY--ALYpHLSVAENM 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK11000 97 SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-212 |
1.63e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.66 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAEnqLFHSTVADEIafglklqkcpadeitqrthaalqccqladtanshpldLHSAQRRMVAVAclEAL--SPPLLL 159
Cdd:cd03246 81 LPQDDE--LFSGSIAENI-------------------------------------LSGGQRQRLGLA--RALygNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 160 LDEPSRDFD---ENWLSVFESWLEKcgqRGTSVVAISHDAAFTRRhFSRVVRLEDG 212
Cdd:cd03246 120 LDEPNSHLDvegERALNQAIAALKA---AGATRIVIAHRPETLAS-ADRILVLEDG 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-214 |
2.19e-23 |
|
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: 93.37 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRqraakVGVLFQEAE-NQLFHSTVADEI 99
Cdd:cd03235 17 DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQRRSiDRDFPISVRDVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 100 AFGLKLQKCPADEIT----QRTHAALQCCQLADTANsHPLD-LHSAQRRMVAVA-CLeALSPPLLLLDEPSRDFDENWLS 173
Cdd:cd03235 92 LMGLYGHKGLFRRLSkadkAKVDEALERVGLSELAD-RQIGeLSGGQQQRVLLArAL-VQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446879615 174 VFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03235 170 DIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-212 |
2.61e-23 |
|
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: 92.25 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAatDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVML--QQQAMKNLKNRQRAAKV 79
Cdd:cd03229 1 LELKNVSKRYGQK--TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgEDLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 GVLFQEAenQLF-HSTVADEIAFGLKlqkcpadeitqrthaalqccqladtanshpldlhSAQRRMVAVACLEALSPPLL 158
Cdd:cd03229 79 GMVFQDF--ALFpHLTVLENIALGLS----------------------------------GGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 159 LLDEPSRDFDENWLSVFESWLEK-CGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
19-214 |
2.96e-23 |
|
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: 91.69 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaAKVGVLFQEAenQLFhstvade 98
Cdd:cd03230 16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLPEEP--SLY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 iafglklqkcpaDEITQRTHaalqccqladtanshpLDLHSAQRRMVAVACleALS--PPLLLLDEPSRDFDENWLSVFE 176
Cdd:cd03230 86 ------------ENLTVREN----------------LKLSGGMKQRLALAQ--ALLhdPELLILDEPTSGLDPESRREFW 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 446879615 177 SWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:cd03230 136 ELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-223 |
2.98e-23 |
|
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: 93.27 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAK-VGVLFQEAenQLFHS-TVADE 98
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIP--RLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQK----------CPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEP----- 163
Cdd:cd03219 96 VMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPaagln 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446879615 164 ---SRDFDEnwlsvfesWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:cd03219 176 peeTEELAE--------LIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-195 |
3.37e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNlknrqRAAKVG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPA--LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-----PGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEaENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLL 160
Cdd:PRK11248 74 VVFQN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 446879615 161 DEPSRDFDENWLSVFESWLEKCGQR-GTSVVAISHD 195
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHD 188
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-214 |
3.57e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.77 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTV-----------------------MLQQQAMKNLKN--- 72
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvleklVIQKTRFKKIKKike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 73 -RQRaakVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRthaALQCCQLADTANSH----PLDLHSAQRRMVAV 147
Cdd:PRK13651 103 iRRR---VGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKR---AAKYIELVGLDESYlqrsPFELSGGQKRRVAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 148 ACLEALSPPLLLLDEPSRDFD----ENWLSVFeswlEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDpqgvKEILEIF----DNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-223 |
4.94e-23 |
|
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: 92.78 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGVLFQEaeNQLF-HSTVAD 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYVPQN--YALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 98 EIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFES 177
Cdd:cd03299 91 NIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446879615 178 WLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:cd03299 171 ELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-223 |
1.74e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 91.69 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWpgAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAK-- 78
Cdd:PRK09493 1 MIEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 79 VGVLFQEAenQLF-HSTVADEIAFG-LKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPP 156
Cdd:PRK09493 79 AGMVFQQF--YLFpHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 157 LLLLDEPSRDFD----ENWLSVFESWLEKcgqrGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK09493 157 LMLFDEPTSALDpelrHEVLKVMQDLAEE----GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-163 |
6.49e-22 |
|
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: 90.48 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKvGVL--FQEAenQLFHS-TVAD 97
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARL-GIArtFQNP--RLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 98 ---------------EIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:COG0411 99 nvlvaaharlgrgllAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
.
gi 446879615 163 P 163
Cdd:COG0411 179 P 179
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-212 |
6.55e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 4 LNKISYRWPGaaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMlqqqamknlknRQRAAKVGVLF 83
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS-----------IPKGLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 84 QEAEnqLF-HSTVADEIAFGLK------------LQKCPADEITQRTHAALQcCQLAD----TANSH----------PLD 136
Cdd:COG0488 68 QEPP--LDdDLTVLDTVLDGDAelraleaeleelEAKLAEPDEDLERLAELQ-EEFEAlggwEAEARaeeilsglgfPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 137 LHSA--------QRRMVAVACLeALSPP-LLLLDEPSRDFDEN---WLsvfESWLEKcgQRGTsVVAISHDaaftrRHF- 203
Cdd:COG0488 145 DLDRpvselsggWRRRVALARA-LLSEPdLLLLDEPTNHLDLEsieWL---EEFLKN--YPGT-VLVVSHD-----RYFl 212
|
250
....*....|...
gi 446879615 204 ----SRVVRLEDG 212
Cdd:COG0488 213 drvaTRILELDRG 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
21-163 |
8.32e-22 |
|
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: 89.52 E-value: 8.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAK-VGVLFQEAenQLFHS-TVADE 98
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEA--SIFRKlTVEEN 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 99 IAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEP 163
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-223 |
9.91e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.02 E-value: 9.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQ----RAAKVGVLFQEAEnQLFHSTVA 96
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQSFA-LMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFE 176
Cdd:PRK10070 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446879615 177 SWLEKC-GQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK10070 205 DELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-195 |
1.61e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.68 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKN-----RQR 75
Cdd:PRK13638 1 MLATSDLWFRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgllalRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 76 AAKVgvlFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQlADTANSHPLD-LHSAQRRMVAVACLEALS 154
Cdd:PRK13638 79 VATV---FQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446879615 155 PPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHD 195
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-223 |
1.96e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.99 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWpgAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:COG4604 1 MIEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQeaENQlFHS--TVADEIAFG--------LKlqkcPADEitQRTHAALQCCQLADTANSHpLD-LHSAQRRMVAVAC 149
Cdd:COG4604 79 ILRQ--ENH-INSrlTVRELVAFGrfpyskgrLT----AEDR--EIIDEAIAYLDLEDLADRY-LDeLSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 150 LEALSPPLLLLDEPSrdfdeNWLSVFES-----WLEK-CGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG4604 149 VLAQDTDYVLLDEPL-----NNLDMKHSvqmmkLLRRlADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-225 |
3.32e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 88.13 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATdCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQL--ADTANSHPLDLHSAQRRMVAVACLEALSPPLL 158
Cdd:cd03295 80 VIQQI--GLFpHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 159 LLDEPSRDFDENWLSVFESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI--HP 225
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrSP 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
21-215 |
3.57e-21 |
|
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: 87.59 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlknrQRAAKVGVLFqeAENQLFHS--TVADE 98
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-------------TVRGRVSSLL--GLGGGFNPelTGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEpsrdfdenWLSVF-ES 177
Cdd:cd03220 105 IYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE--------VLAVGdAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446879615 178 WLEKCGQR-------GTSVVAISHDAAFTRRHFSRVVRLEDGLIR 215
Cdd:cd03220 177 FQEKCQRRlrellkqGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
15-214 |
8.96e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.99 E-value: 8.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 15 ATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMkNLKN-------RQRAAKVGVLFQEAe 87
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKtpsdkaiRELRRNVGMVFQQY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 88 NQLFHSTVADE-IAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRD 166
Cdd:PRK11124 92 NLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446879615 167 FDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-223 |
1.38e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlknrQRAAKVGVLFqeaenQL---FHS-- 93
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-------------EVNGRVSALL-----ELgagFHPel 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANsHPLDLHSAQRRM-VAVACLEALSPPLLLLDEpsrdfdenWL 172
Cdd:COG1134 104 TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFID-QPVKTYSSGMRArLAFAVATAVDPDILLVDE--------VL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 173 SV----FeswLEKCGQR-------GTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:COG1134 175 AVgdaaF---QKKCLARirelresGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
21-168 |
1.53e-20 |
|
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: 86.02 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaAKVGVLFQeaENQLFHS-TVADEI 99
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGYCPQ--FDALFDElTVREHL 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACleAL--SPPLLLLDEPSRDFD 168
Cdd:cd03263 97 RFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAI--ALigGPSVLLLDEPTSGLD 165
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-168 |
4.95e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 85.62 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 32 LALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAENQLFHSTVADEIAFGLKLQKCPAD 111
Cdd:PRK13652 33 IAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFSPTVEQDIAFGPINLGLDEE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 112 EITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK13652 113 TVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-223 |
6.07e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWpgAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQeaenQLFHS---TVADEIAFG----LKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEAL 153
Cdd:PRK11231 80 LLPQ----HHLTPegiTVRELVAYGrspwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 154 SPPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
21-170 |
7.79e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 86.31 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGVLFQEAenQLF-HSTVADEI 99
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR--DICMVFQSY--ALFpHMSLGENV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDEN 170
Cdd:PRK11432 100 GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
22-214 |
1.56e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 84.03 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTV------------MLQQQAMKnlknRQRAAKVGVLFQEAeNQ 89
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarsLSQQKGLI----RQLRQHVGFVFQNF-NL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 90 LFHSTVADEIAFG-LKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK11264 97 FPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 169 ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK11264 177 PELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-223 |
2.21e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.29 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAAT---DCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQA----MKNLKNRQ 74
Cdd:PRK13645 7 IILDNVSYTYAKKTPfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 75 RAAK-VGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLA-DTANSHPLDLHSAQRRMVAVACLEA 152
Cdd:PRK13645 87 RLRKeIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 153 LSPPLLLLDEPSRDFD----ENWLSVFESWLEKCGQRgtsVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKR---IIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-215 |
4.70e-19 |
|
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: 82.10 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKvGVLFQEAENQLFHS-TVADEI 99
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA-GIGYVPEGRRIFPElTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 100 AFGLKLQKCPADEIT------------QRTHaalqccQLADTanshpldLHSAQRRMVAVAclEAL--SPPLLLLDEPSR 165
Cdd:cd03224 97 LLGAYARRRAKRKARlervyelfprlkERRK------QLAGT-------LSGGEQQMLAIA--RALmsRPKLLLLDEPSE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 166 DfdenwLS------VFESwLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIR 215
Cdd:cd03224 162 G-----LApkiveeIFEA-IRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
19-214 |
6.58e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 82.43 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA---KVGVLFQEAENQLF-HST 94
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDSISAVNpRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFGLK-LQKCPADEITQRTHAALQCCQLADT-ANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWL 172
Cdd:PRK10419 108 VREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQ 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446879615 173 SVFESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK10419 188 AGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-223 |
1.03e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.74 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 14 AATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAENQlFHS 93
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLS-FEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEIAFGLKLQKC------PADE-ITQRTHAALQCCQLADTANShplDLHSAQRRMVAVACLEALSPPLLLLDEPSRD 166
Cdd:PRK09536 93 DVRQVVEMGRTPHRSrfdtwtETDRaAVERAMERTGVAQFADRPVT---SLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 167 FDEN-WLSVFESwLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK09536 170 LDINhQVRTLEL-VRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
22-194 |
1.46e-18 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 80.23 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMknlkNRQRAAkvgvlFQEAENQLFHstvadeiAF 101
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDS-----IARGLLYLGH-------AP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 102 GLKLQKCPADEIT--QRTHAALQCCQLADTANSHPLD------LHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLS 173
Cdd:cd03231 83 GIKTTLSVLENLRfwHADHSDEQVEEALARVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 446879615 174 VFESWLEKCGQRGTSVVAISH 194
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-214 |
1.59e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 81.26 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWpgAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaakvgV 81
Cdd:PRK11247 13 LLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-----L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAEnQLFHSTVADEIAFGLKLQKCPAdeitqrTHAALQCCQLADTANSHPLDLHSAQRRMVAVAclEAL--SPPLLL 159
Cdd:PRK11247 86 MFQDAR-LLPWKKVIDNVGLGLKGQWRDA------ALQALAAVGLADRANEWPAALSGGQKQRVALA--RALihRPGLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 160 LDEPSRDFDEnwLSVFES-------WLekcgQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK11247 157 LDEPLGALDA--LTRIEMqdlieslWQ----QHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
22-223 |
2.00e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.17 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG-------------VLFQEAeN 88
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVAdknqlrllrtrltMVFQHF-N 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 89 QLFHSTVADEIAFG----LKLQKCPADEitqRTHAALQCCQLADTANS-HPLDLHSAQRRMVAVACLEALSPPLLLLDEP 163
Cdd:PRK10619 103 LWSHMTVLENVMEApiqvLGLSKQEARE---RAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 164 SRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
22-194 |
2.27e-18 |
|
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: 79.71 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMknlkNRQRAakvgvLFQEAENQLFHS-------T 94
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRD-----EPHENILYLGHLpglkpelS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFglklqKCPADEITQRT-HAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLS 173
Cdd:TIGR01189 90 ALENLHF-----WAAIHGGAQRTiEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 446879615 174 VFESWLEKCGQRGTSVVAISH 194
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-163 |
2.79e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGvlfqeaenqlfHS------- 93
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG-----------HRnamkpal 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEIAFGLKLQKCPADEItqrtHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEP 163
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-214 |
2.84e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 80.21 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 6 KISYRWPG-AATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQ 84
Cdd:cd03248 16 NVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 85 EAenQLFHSTVADEIAFGlkLQKCPADEITqrthaalqccQLADTANSHPL-----------------DLHSAQRRMVAV 147
Cdd:cd03248 96 EP--VLFARSLQDNIAYG--LQSCSFECVK----------EAAQKAHAHSFiselasgydtevgekgsQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 148 ACLEALSPPLLLLDEPSRDFDENWLSVFESWLEKCGQRgTSVVAISHDAAfTRRHFSRVVRLEDGLI 214
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-164 |
3.35e-18 |
|
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: 79.54 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGaaTDCLCDISLQLKQGEWlALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaAKVGV 81
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEaenqlF----HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPL 157
Cdd:cd03264 77 LPQE-----FgvypNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
|
....*..
gi 446879615 158 LLLDEPS 164
Cdd:cd03264 152 LIVDEPT 158
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
5.29e-18 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 81.95 E-value: 5.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:TIGR02857 322 LEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLFHSTVADEIAFGLKLQkcPADEITQrthaALQCCQLADTANSHPLDLHS-----------AQRRMVAVACL 150
Cdd:TIGR02857 401 VPQHP--FLFAGTIAENIRLARPDA--SDAEIRE----ALERAGLDEFVAALPQGLDTpigeggaglsgGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 151 EALSPPLLLLDEPSRDFDENWLSVFESWLEKCGQrGTSVVAISHDAAFTRRhFSRVVRL 209
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-214 |
5.40e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 81.75 E-value: 5.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:COG1132 340 IEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLFHSTVADEIAFGlklqKCPADEitQRTHAALQCCQLADTANSHPLDLHSA-----------QRRMVAVAcl 150
Cdd:COG1132 419 VPQDT--FLFSGTIRENIRYG----RPDATD--EEVEEAAKAAQAHEFIEALPDGYDTVvgergvnlsggQRQRIAIA-- 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 151 EAL--SPPLLLLDEPSRDFD-ENWLSVFESwLEKcGQRGTSVVAISHdaaftR----RHFSRVVRLEDGLI 214
Cdd:COG1132 489 RALlkDPPILILDEATSALDtETEALIQEA-LER-LMKGRTTIVIAH-----RlstiRNADRILVLDDGRI 552
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-196 |
9.07e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRwpGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:PRK10247 7 LLQLQNVGYL--AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAenQLFHSTVADEIAFGLKLQKCPADEitQRTHAALQCCQLADTANSHPL-DLHSAQRRMVA-VACLEALsPPLL 158
Cdd:PRK10247 85 YCAQTP--TLFGDTVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNIaELSGGEKQRISlIRNLQFM-PKVL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 446879615 159 LLDEPSRDFDE-NWLSVFESWLEKCGQRGTSVVAISHDA 196
Cdd:PRK10247 160 LLDEITSALDEsNKHNVNEIIHRYVREQNIAVLWVTHDK 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-163 |
2.41e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.76 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAK-VGVLFQEAenqlfhS-----T 94
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGYLPQEA------SifrklT 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA-CLeALSPPLLLLDEP 163
Cdd:COG1137 95 VEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIArAL-ATNPKFILLDEP 163
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-212 |
2.59e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.96 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLtPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAEnQLFHSTVADE 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQS-PPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKlQKCPADEITQRTHAALQCCQLADTAnSHPLDLHSA---QR-RMVAVaCLE---ALSPP--LLLLDEPSRDFDE 169
Cdd:COG4138 90 LALHQP-AGASSEAVEQLLAQLAEALGLEDKL-SRPLTQLSGgewQRvRLAAV-LLQvwpTINPEgqLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446879615 170 NWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:COG4138 167 AQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-194 |
4.27e-17 |
|
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: 75.16 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMkNLKNRQRAAKVGVlfqeaenqlfhSTVade 98
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-SFASPRDARRAGI-----------AMV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 iafglklqkcpadeitqrthaalqccqladtansHPLDLhsAQRRMVAVAclEALS--PPLLLLDEP----SRDFDENWL 172
Cdd:cd03216 81 ----------------------------------YQLSV--GERQMVEIA--RALArnARLLILDEPtaalTPAEVERLF 122
|
170 180
....*....|....*....|..
gi 446879615 173 SVfeswLEKCGQRGTSVVAISH 194
Cdd:cd03216 123 KV----IRRLRAQGVAVIFISH 140
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-214 |
6.23e-17 |
|
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: 76.50 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLFHSTVADEIAFGlklqkcpADEITQ-RTHAALQCCQLADTANSHPLDLHS-----------AQRRMVAVAc 149
Cdd:cd03251 81 VSQDV--FLFNDTVAENIAYG-------RPGATReEVEEAARAANAHEFIMELPEGYDTvigergvklsgGQRQRIAIA- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 150 lEAL--SPPLLLLDEPSRDFD-ENWLSVFESwLEKCGQRGTSVVaISHDAAfTRRHFSRVVRLEDGLI 214
Cdd:cd03251 151 -RALlkDPPILILDEATSALDtESERLVQAA-LERLMKNRTTFV-IAHRLS-TIENADRIVVLEDGKI 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-194 |
6.97e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ------------------QQAMKNLKNRQRaaKVGVL 82
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknnhelitnpySKKIKNFKELRR--RVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 83 FQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADT-ANSHPLDLHSAQRRMVAVACLEALSPPLLLLD 161
Cdd:PRK13631 122 FQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFD 201
|
170 180 190
....*....|....*....|....*....|...
gi 446879615 162 EPSRDFDENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:PRK13631 202 EPTAGLDPKGEHEMMQLILDAKANNKTVFVITH 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-209 |
1.02e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlkNRQRAAKVGVLFQEAE-NQLFHSTVAD 97
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEvPDSLPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 98 EIAFGLKLQKCPADEITQRTHA----ALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLS 173
Cdd:NF040873 77 LVAMGRWARRGLWRRLTRDDRAavddALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 446879615 174 VFESWLEKCGQRGTSVVAISHDAAFTRRHFsRVVRL 209
Cdd:NF040873 157 RIIALLAEEHARGATVVVVTHDLELVRRAD-PCVLL 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-163 |
1.70e-16 |
|
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: 77.06 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVML------QQQAMKNLKNRQRAakVGVLFQEAenQLF-HS 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqDSARGIFLPPHRRR--IGYVFQEA--RLFpHL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 94 TVADEIAFGLKlqKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACleAL--SPPLLLLDEP 163
Cdd:COG4148 93 SVRGNLLYGRK--RAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGR--ALlsSPRLLLMDEP 160
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-214 |
1.99e-16 |
|
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: 75.22 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGV 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEaeNQLFHSTVADEIAF---GLKLQKCPADEITQRTHAALqcCQLADTANS----HPLDLHSAQRRMVAVACLEALS 154
Cdd:cd03252 81 VLQE--NVLFNRSIRDNIALadpGMSMERVIEAAKLAGAHDFI--SELPEGYDTivgeQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 155 PPLLLLDEPSRDFDENWLSVFESWLEK-CGQRgtSVVAISHDAAfTRRHFSRVVRLEDGLI 214
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDiCAGR--TVIIIAHRLS-TVKNADRIIVMEKGRI 214
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-194 |
4.14e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.21 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPG--AatdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQ-RAA 77
Cdd:COG1129 4 LLEMRGISKSFGGvkA----LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVLFQeaENQLF-HSTVADEIAFGLKLQKCPA---DEITQRTHAALQccQLadtanSHPLDLHS-------AQRRMVA 146
Cdd:COG1129 80 GIAIIHQ--ELNLVpNLSVAENIFLGREPRRGGLidwRAMRRRARELLA--RL-----GLDIDPDTpvgdlsvAQQQLVE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446879615 147 VAclEALS--PPLLLLDEP--SRDFDE-NWLsvFEsWLEKCGQRGTSVVAISH 194
Cdd:COG1129 151 IA--RALSrdARVLILDEPtaSLTEREvERL--FR-IIRRLKAQGVAIIYISH 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-223 |
4.59e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 74.64 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAENQlFHSTVADEIA 100
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTP-GDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 101 FG--------LKLQKCPADEITqrthAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD-ENW 171
Cdd:PRK10253 104 RGryphqplfTRWRKEDEEAVT----KAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDiSHQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446879615 172 LSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-201 |
5.07e-16 |
|
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: 74.29 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqQAMKNLKNRQR---AAKVGVLFQEAENQLFHSTVAD 97
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV----RVAGLVPWKRRkkfLRRIGVVFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 98 EIAFGLKLQKCPADEITQRTH---AALQCCQLADTanshPLDLHSAQRRMVA-VACLEALSPPLLLLDEPSRDFDEN-WL 172
Cdd:cd03267 115 SFYLLAAIYDLPPARFKKRLDelsELLDLEELLDT----PVRQLSLGQRMRAeIAAALLHEPEILFLDEPTIGLDVVaQE 190
|
170 180 190
....*....|....*....|....*....|...
gi 446879615 173 SVFESWLEKCGQRGTSVVAISHD----AAFTRR 201
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYmkdiEALARR 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
21-216 |
5.36e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQqqamKNLknrqraaKVGVLFQEAENqlFHS--TVADE 98
Cdd:COG0488 333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETV-------KIGYFDQHQEE--LDPdkTVLDE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGlklqkcpADEITQRTHAALqccqLA------DTANSHPLDLHSAQRRMVAVACLeALSPP-LLLLDEPSRDFD--- 168
Cdd:COG0488 400 LRDG-------APGGTEQEVRGY----LGrflfsgDDAFKPVGVLSGGEKARLALAKL-LLSPPnVLLLDEPTNHLDiet 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446879615 169 ----ENWLSVFEswlekcgqrGTsVVAISHDAAFTRRHFSRVVRLEDGLIRN 216
Cdd:COG0488 468 lealEEALDDFP---------GT-VLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-223 |
5.83e-16 |
|
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: 75.99 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ------QQAMKNLKNRQRAAK-VGVLFQEAEnqLF-HS 93
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvDMTKPGPDGRGRAKRyIGILHQEYD--LYpHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEI--AFGLKLqkcpADEITQRThaALQCCQLA--------DTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEP 163
Cdd:TIGR03269 381 TVLDNLteAIGLEL----PDELARMK--AVITLKMVgfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 164 SRDFDE-NWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:TIGR03269 455 TGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-214 |
8.16e-16 |
|
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: 72.35 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNrQRAAKVGV 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAenQLFHSTVADEIafGLKLQkcpadeitqrthaalqccqladtanshpldlhSAQRRMVAVACLEALSPPLLLLD 161
Cdd:cd03247 80 LNQRP--YLFDTTLRNNL--GRRFS--------------------------------GGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 162 EPSRDFD---EN-WLSVFESWLEkcgqrGTSVVAISHDAAfTRRHFSRVVRLEDGLI 214
Cdd:cd03247 124 EPTVGLDpitERqLLSLIFEVLK-----DKTLIWITHHLT-GIEHMDKILFLENGKI 174
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-212 |
9.33e-16 |
|
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: 73.27 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ-QQAMKNLKNRQraakvgVLFQEAeNQLFHSTVAD 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEgKQITEPGPDRM------VVFQNY-SLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 98 EIAFGLK--LQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDE-NWLSV 174
Cdd:TIGR01184 74 NIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAlTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 446879615 175 FESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-210 |
1.42e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.14 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMknlkNRQRAAkvgvlfqeaenqlFHSTV----- 95
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDE-------------YHQDLlylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ---------ADE-IAFGLKLQKCPADEitqRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSR 165
Cdd:PRK13538 82 qpgikteltALEnLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446879615 166 DFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLE 210
Cdd:PRK13538 159 AIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLRLG 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-164 |
1.43e-15 |
|
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: 72.71 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKvGVLFQEAENQLFHS-TVADEI 99
Cdd:COG0410 21 GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARL-GIGYVPEGRRIFPSlTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 100 AFGLKLQKCPA------DEI-------TQRTHaalqccQLADTanshpldLHSAQRRMVAVACleAL--SPPLLLLDEPS 164
Cdd:COG0410 100 LLGAYARRDRAevradlERVyelfprlKERRR------QRAGT-------LSGGEQQMLAIGR--ALmsRPKLLLLDEPS 164
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-212 |
2.31e-15 |
|
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: 70.17 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGaaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQqamknlknrqrAAKVGV 81
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQeaenqlfhstvadeiafglklqkcpadeitqrthaalqccqladtanshpldLHSAQRRMVAVACLEALSPPLLLLD 161
Cdd:cd03221 68 FEQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446879615 162 EPSRDFDENWLSVFESWLEKcgQRGTsVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:cd03221 96 EPTNHLDLESIEALEEALKE--YPGT-VILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-203 |
5.18e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.05 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 3 TLNKISYRWPGAATdCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQqamknlknrqrAAKVGVL 82
Cdd:TIGR03719 6 TMNRVSKVVPPKKE-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP-----------GIKVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 83 FQEAenQLFHS-TVADEIAFGLKLQKC--------------PADEITQ--RTHAALQccQLADTANSHPLD--------- 136
Cdd:TIGR03719 74 PQEP--QLDPTkTVRENVEEGVAEIKDaldrfneisakyaePDADFDKlaAEQAELQ--EIIDAADAWDLDsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 137 ------------LHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENwlSVfeSWLEKCGQR--GTsVVAISHDaaftrRH 202
Cdd:TIGR03719 150 lrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE--SV--AWLERHLQEypGT-VVAVTHD-----RY 219
|
.
gi 446879615 203 F 203
Cdd:TIGR03719 220 F 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-214 |
5.97e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 5.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQrAAKVGVLFQEAENQLFHS-TVADEIA 100
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGIYLVPQEPLLFPNlSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 101 FGLKLQKCPADEITQRThAALQcCQLADTANSHPLDLhsAQRRMVAVacLEAL--SPPLLLLDEPSRDFDENWLSVFESW 178
Cdd:PRK15439 109 FGLPKRQASMQKMKQLL-AALG-CQLDLDSSAGSLEV--ADRQIVEI--LRGLmrDSRILILDEPTASLTPAETERLFSR 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 446879615 179 LEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK15439 183 IRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
1.08e-14 |
|
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: 70.09 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKIS--YRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLqqQAMKNLKNRQRA-A 77
Cdd:cd03266 1 MITADALTkrFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVVKEPAEArR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVLFqeAENQLFHS-TVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVAclEAL--S 154
Cdd:cd03266 79 RLGFVS--DSTGLYDRlTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIA--RALvhD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 155 PPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIR 215
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-225 |
1.37e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.02 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 6 KISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKS-TLLRVMaGLLTPTA----GTVMLQQQAMKNLKNRQ----RA 76
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAahpsGSILFDGQDLLGLSERElrriRG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 77 AKVGVLFQE---AENQLFhsTVADEIAFGLKL-QKCPADEITQRTHAALQCCQLADTA---NSHPLDLhSA---QRRMVA 146
Cdd:COG4172 92 NRIAMIFQEpmtSLNPLH--TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQL-SGgqrQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 147 VACleALSPPLLLLDEPS---------------RDfdenwlsvfeswLEKcgQRGTSVVAISHDAAFTRRHFSRVVRLED 211
Cdd:COG4172 169 MAL--ANEPDLLIADEPTtaldvtvqaqildllKD------------LQR--ELGMALLLITHDLGVVRRFADRVAVMRQ 232
|
250
....*....|....*....
gi 446879615 212 GLIRNVNPPDDI-----HP 225
Cdd:COG4172 233 GEIVEQGPTAELfaapqHP 251
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-84 |
3.41e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.34 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRW-PGAATD--CLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA 77
Cdd:COG1101 1 MLELKNLSKTFnPGTVNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
....*..
gi 446879615 78 KVGVLFQ 84
Cdd:COG1101 81 YIGRVFQ 87
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-194 |
4.46e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 4.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPG-AATDclcDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKnLKN-RQ-RAA 77
Cdd:COG3845 5 ALELRGITKRFGGvVAND---DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRSpRDaIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVLFQEAenQLFHS-TVADEIAFGLKlqkcPADEITQRTHAALQccQLADTANSHPLDLH--------SA---QRrmv 145
Cdd:COG3845 81 GIGMVHQHF--MLVPNlTVAENIVLGLE----PTKGGRLDRKAARA--RIRELSERYGLDVDpdakvedlSVgeqQR--- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 146 aVACLEALS--PPLLLLDEPSrdfdenwlSV---------FESwLEKCGQRGTSVVAISH 194
Cdd:COG3845 150 -VEILKALYrgARILILDEPT--------AVltpqeadelFEI-LRRLAAEGKSIIFITH 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-212 |
4.77e-14 |
|
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: 68.96 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVM------LQQQAMKNLKNRqraakVGVLFQEAENQLFHST 94
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWELRKR-----IGLVSPALQLRFPRDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEI----AFG-LKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVAclEAL--SPPLLLLDEPSRDF 167
Cdd:COG1119 96 TVLDVvlsgFFDsIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA--RALvkDPELLILDEPTAGL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 168 DENWLSVFESWLEK-CGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:COG1119 174 DLGARELLLALLDKlAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-194 |
7.17e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAenQLFHSTVADE 98
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEP--VLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGlkLQKCPADEITQrthAALQCC---------QLADT-ANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:TIGR00958 575 IAYG--LTDTPDEEIMA---AAKAANahdfimefpNGYDTeVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|....*.
gi 446879615 169 ENWLSVFESWLEkcgQRGTSVVAISH 194
Cdd:TIGR00958 650 AECEQLLQESRS---RASRTVLLIAH 672
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-163 |
8.07e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.10 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAaTDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRA-AKV 79
Cdd:PRK11650 3 GLKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDiAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 gvlFQeaeN-QLF-HSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVAclEAL--SP 155
Cdd:PRK11650 82 ---FQ---NyALYpHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMG--RAIvrEP 153
|
....*...
gi 446879615 156 PLLLLDEP 163
Cdd:PRK11650 154 AVFLFDEP 161
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-212 |
1.30e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA-KVGVLFQEAE--NQLfhsTV 95
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlGIGIIYQELSviDEL---TV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ADEIAFGLKLQK--CPAD-----EITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK09700 98 LENLYIGRHLTKkvCGVNiidwrEMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446879615 169 ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK09700 178 NKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-163 |
1.48e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKnLKNRQRA--AKV 79
Cdd:PRK11288 5 LSFDGIGKTFPGVKA--LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR-FASTTAAlaAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 GVLFQE---------AEN----QLFHStvadeiaFGLklqkcpADEITQRTHAALQCCQLA-DTANSHPL-DLHSAQRRM 144
Cdd:PRK11288 82 AIIYQElhlvpemtvAENlylgQLPHK-------GGI------VNRRLLNYEAREQLEHLGvDIDPDTPLkYLSIGQRQM 148
|
170
....*....|....*....
gi 446879615 145 VAVACLEALSPPLLLLDEP 163
Cdd:PRK11288 149 VEIAKALARNARVIAFDEP 167
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-219 |
1.89e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.17 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGL--LTPTA---GTVML-----QQQAMKNLKNRQraaKVGVLFQeAENQL 90
Cdd:PRK14267 22 GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEArveGEVRLfgrniYSPDVDPIEVRR---EVGMVFQ-YPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 91 FHSTVADEIAFGLKLQKC--PADEITQRTHAALQCCQL----ADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPS 164
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 165 RDFDENWLSVFESWLEKCGQRGTsVVAISHDAAFTRRHFSRVVRLEDGLIRNVNP 219
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEYT-IVLVTHSPAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-223 |
4.44e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.35 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 3 TLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVL 82
Cdd:PRK10575 13 ALRNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 83 FQE---AENQlfhsTVADEIAFGlklqKCP--------ADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLE 151
Cdd:PRK10575 91 PQQlpaAEGM----TVRELVAIG----RYPwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446879615 152 ALSPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDiAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
5.15e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLrvmaGLLT----PTAGTVMLQQQAMKNLKNRQRAA 77
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTrawdPQQGEILLNGQPIADYSEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVLFQEAenQLFHSTVADEiafgLKLQKCPADEitQRTHAALQCCQLAD-TANSHPLD---------LHSAQRRMVAV 147
Cdd:PRK11160 415 AISVVSQRV--HLFSATLRDN----LLLAAPNASD--EALIEVLQQVGLEKlLEDDKGLNawlgeggrqLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 148 AclEAL--SPPLLLLDEPSRDFD-ENWLSVFESWLEKCgqRGTSVVAISHdaaftrR-----HFSRVVRLEDGLIRN 216
Cdd:PRK11160 487 A--RALlhDAPLLLLDEPTEGLDaETERQILELLAEHA--QNKTVLMITH------RltgleQFDRICVMDNGQIIE 553
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-220 |
6.91e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.06 E-value: 6.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGA--ATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA- 77
Cdd:PRK10535 4 LLELKDIRRSYPSGeeQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 ---KVGVLFQEAeNQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVAclEAL- 153
Cdd:PRK10535 84 rreHFGFIFQRY-HLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIA--RALm 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 154 -SPPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHfSRVVRLEDGLIRNVNPP 220
Cdd:PRK10535 161 nGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQA-ERVIEIRDGEIVRNPPA 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-194 |
8.03e-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: 66.77 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLtPTA---GTVMLQQQAMK--NLKNRQR 75
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKA--LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKasNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 76 AakvGVLFQEAENQLFHS-TVADEIAFG----LKLQKCPADEITQRTHAALQCCQLADTANSHPL-DLHSAQRRMVAVAc 149
Cdd:TIGR02633 78 A---GIVIIHQELTLVPElSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIA- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446879615 150 lEALSPP--LLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:TIGR02633 154 -KALNKQarLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
21-168 |
8.31e-13 |
|
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: 65.08 E-value: 8.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGT-VMLQQQAMKNLKNRQRaaKVGVLFQE--AENQLfhsTVAD 97
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVREPREVRR--RIGIVFQDlsVDDEL---TGWE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446879615 98 EIAFGLKLQKCPADEITQRTHAALQCCQLADTANsHPLDLHSA--QRRM-VAVACLEalSPPLLLLDEPSRDFD 168
Cdd:cd03265 93 NLYIHARLYGVPGAERRERIDELLDFVGLLEAAD-RLVKTYSGgmRRRLeIARSLVH--RPEVLFLDEPTIGLD 163
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
21-163 |
8.86e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 66.63 E-value: 8.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLtPTAGTVMLQQQAMKNLKNRQRAA---KVGVLFQEAenqlFHS---- 93
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPlrrRMQVVFQDP----FGSlspr 378
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 94 -TVADEIAFGLKLQKCPAD--EITQRTHAALQCCQL-ADTANSHPLDLHSAQRRMVAVA-CLeALSPPLLLLDEP 163
Cdd:COG4172 379 mTVGQIIAEGLRVHGPGLSaaERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIArAL-ILEPKLLVLDEP 452
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-194 |
1.20e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKnlknRQRAAkvgvlFQEAENQLFHSTvadE 98
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCT-----YQKQLCFVGHRS---G 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQK-CPADEITQRTHAAL-QCCQLADTanSHPLD-----LHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENW 171
Cdd:PRK13540 85 INPYLTLREnCLYDIHFSPGAVGItELCRLFSL--EHLIDypcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 446879615 172 LSVFESWLEKCGQRGTSVVAISH 194
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
18-203 |
1.26e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 18 CLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQqamknlknrqrAAKVGVLFQEAenQLFHS-TVA 96
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP-----------GIKVGYLPQEP--QLDPEkTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGL-----KLQKcpADEITQR-------------THAALQccQLADTANSHPLD---------------------L 137
Cdd:PRK11819 89 ENVEEGVaevkaALDR--FNEIYAAyaepdadfdalaaEQGELQ--EIIDAADAWDLDsqleiamdalrcppwdakvtkL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 138 HSAQRRMVAVaC---LEAlsPPLLLLDEPSRDFD-EnwlSVfeSWLEKCGQR--GTsVVAISHDaaftrRHF 203
Cdd:PRK11819 165 SGGERRRVAL-CrllLEK--PDMLLLDEPTNHLDaE---SV--AWLEQFLHDypGT-VVAVTHD-----RYF 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-163 |
1.73e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM--KNLKNRQRaakVGV------LFQE---AEN- 88
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRR---VGYmsqafsLYGEltvRQNl 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 89 ----QLFHstvadeiafglklqkCPADEITQRTHAALQCCQLADTANSHP--LDLHSAQRRMVAVACLEalSPPLLLLDE 162
Cdd:NF033858 361 elhaRLFH---------------LPAAEIAARVAEMLERFDLADVADALPdsLPLGIRQRLSLAVAVIH--KPELLILDE 423
|
.
gi 446879615 163 P 163
Cdd:NF033858 424 P 424
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-223 |
1.84e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.55 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 16 TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGL--LTPTA---GTVMLQQQAMKNLKNRQRAAKVGVLFQeAENQL 90
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQ-IPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 91 FHSTVADEIAFGLKLQKCPAD--EITQRTHAALQCCQL----ADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPS 164
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 165 RDFD-ENWLSVFESWLEKcgQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK14247 175 ANLDpENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-168 |
2.86e-12 |
|
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: 65.42 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 33 ALTGDNGAGKSTLLRVMAGLLTPTAGTVMLqqqAMKNLKNRQRAAKVGVLFQEAENQLFHS-TVADEIAFGLKLQKCPAD 111
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLV---GGKDIETNLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWE 1036
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 112 EITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:TIGR01257 1037 EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-195 |
3.13e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGA-ATDclcDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNrQRAAKV 79
Cdd:PRK11300 5 LLSVSGLMMRFGGLlAVN---NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 GV--------LFQE---AENQLF--HSTVADEIAFGlkLQKCPA-----DEITQRTHAALQCCQLADTANSHPLDLHSAQ 141
Cdd:PRK11300 81 GVvrtfqhvrLFREmtvIENLLVaqHQQLKTGLFSG--LLKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 142 RRMVAVACLEALSPPLLLLDEPS-----RDFDEnwLSVFESWLEKcgQRGTSVVAISHD 195
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAaglnpKETKE--LDELIAELRN--EHNVTVLLIEHD 213
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-195 |
7.19e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.57 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVML-----QQQAMKNLKNrqraakVGVLF-QeaENQLF-HS 93
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyvpFKRRKEFARR------IGVVFgQ--RSQLWwDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADeiafGLKLQKC----PADEITQRTHaalqccQLADTANSHPLdLHSAQR------RM---VAVACLEalSPPLLLL 160
Cdd:COG4586 112 PAID----SFRLLKAiyriPDAEYKKRLD------ELVELLDLGEL-LDTPVRqlslgqRMrceLAAALLH--RPKILFL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 161 DEPS-----------RDFdenwLsvfeswLEKCGQRGTSVVAISHD 195
Cdd:COG4586 179 DEPTigldvvskeaiREF----L------KEYNRERGTTILLTSHD 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-212 |
7.59e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLtPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAeNQLFHSTVADEIAF 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQ-TPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 102 GLKlQKCPADEITQRTHAALQCCQLADTANSHPLDLHSA--QRRMVAVACLE---ALSP--PLLLLDEPSRDFD---ENW 171
Cdd:PRK03695 93 HQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQvwpDINPagQLLLLDEPMNSLDvaqQAA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446879615 172 LsvfESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK03695 172 L---DRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-162 |
7.84e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAENQLF-HSTVADEI 99
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNpRQRISQIL 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 100 AFGLKLQ-KCPADEITQRTHAAL-QCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:PRK15112 111 DFPLRLNtDLEPEQREKQIIETLrQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
21-223 |
1.06e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.22 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAK-VGVLFQEAenQLFHS-TVADE 98
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEA--SIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQK-CPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFES 177
Cdd:PRK10895 99 LMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 178 WLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK10895 179 IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
21-215 |
1.19e-11 |
|
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: 61.53 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRqraaKVGVLFQeaENQLFHS-TVADEI 99
Cdd:cd03269 18 DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLPE--ERGLYPKmKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 100 AFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFESWL 179
Cdd:cd03269 92 VYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 446879615 180 EKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIR 215
Cdd:cd03269 172 RELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-168 |
1.23e-11 |
|
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: 61.46 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRaaKVGVLFqeaENQLF--HSTVA 96
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR--RIGALI---EAPGFypNLTAR 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446879615 97 DEIAFGLKLQKCPADEITQrthaALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:cd03268 91 ENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-168 |
1.46e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNlKNRQRAAKVGVL---------FQEAENQLF 91
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVpqfdnldpdFTVRENLLV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 92 HSTVadeiaFGLklqkcPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK13537 104 FGRY-----FGL-----SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-214 |
1.87e-11 |
|
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: 61.47 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAenQLFHSTVADE 98
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT--FLFSGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGlklqkcpaDEITQRThaalQCCQLADTANSHPL-----------------DLHSAQRRMVAVAclEALS--PPLLL 159
Cdd:cd03254 97 IRLG--------RPNATDE----EVIEAAKEAGAHDFimklpngydtvlgenggNLSQGERQLLAIA--RAMLrdPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 160 LDEPSRDFDENWLSVFESWLEKCGQRGTSVVaISHDAAfTRRHFSRVVRLEDGLI 214
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSII-IAHRLS-TIKNADKILVLDDGKI 215
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-194 |
2.39e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 7 ISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMkNLKNRQRAAKVGVLFQEA 86
Cdd:PRK10982 4 ISKSFPGVKA--LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 87 E-NQLFHSTVADEIAFGLKLQKCP---ADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:PRK10982 81 ElNLVLQRSVMDNMWLGRYPTKGMfvdQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190
....*....|....*....|....*....|..
gi 446879615 163 PSRDFDENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISH 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-212 |
2.48e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKST----LLRvmaglLTPTAGTVMLQQQAMKNLKNRQRAA---KVGVLFQEAENQLF 91
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLR-----LINSQGEIWFDGQPLHNLNRRQLLPvrhRIQVVFQDPNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 92 -HSTVADEIAFGLKLQK--CPADEITQRTHAALQCCQL-ADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDF 167
Cdd:PRK15134 377 pRLNVLQIIEEGLRVHQptLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 168 DENWLSVFESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-222 |
2.54e-11 |
|
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: 61.02 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAenQLFHSTVADEIA 100
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEP--VLFDGTIAENIR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 101 FGLklqkcPADEITQRTHAALQcCQLADTANSHP-----------LDLHSAQRRMVAVAclEAL--SPPLLLLDEPSRDF 167
Cdd:cd03249 99 YGK-----PDATDEEVEEAAKK-ANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIA--RALlrNPKILLLDEATSAL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 168 DENWLSVFESWLEKCgQRGTSVVAISHDAAfTRRHFSRVVRLEDGLIRNVNPPDD 222
Cdd:cd03249 171 DAESEKLVQEALDRA-MKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-195 |
3.28e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.32 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLkNRQR----AAKVGVLFQEAenQLFHS-TV 95
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM-SRSRlytvRKRMSMLFQSG--ALFTDmNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ADEIAFGLKLQ-KCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSV 174
Cdd:PRK11831 102 FDNVAYPLREHtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181
|
170 180
....*....|....*....|..
gi 446879615 175 FESWLEKCGQR-GTSVVAISHD 195
Cdd:PRK11831 182 LVKLISELNSAlGVTCVVVSHD 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
10-194 |
5.19e-11 |
|
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: 59.49 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 10 RWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTA--GTVML--QQQAMKNLKNRqraakVGvlFQE 85
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLIngRPLDKRSFRKI-----IG--YVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 86 AENQLF-HSTVADEIAFGLKLQKcpadeitqrthaalqccqladtanshpldLHSAQRRMVAVACLEALSPPLLLLDEPS 164
Cdd:cd03213 89 QDDILHpTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190
....*....|....*....|....*....|.
gi 446879615 165 RDFDE-NWLSVFESwLEKCGQRGTSVVAISH 194
Cdd:cd03213 140 SGLDSsSALQVMSL-LRRLADTGRTIICSIH 169
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-194 |
6.25e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTP---TAGTVMLQQQAMKNLKNRQRAAKVgvlfQEAENQLFHSTV 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYV----QQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ADEIAFG--LKLQK-CPADEITQRTHAALQCCQLADTANS---HPLD---LHSAQRRMVAVAClEALS-PPLLLLDEPSR 165
Cdd:TIGR00955 117 REHLMFQahLRMPRrVTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFAS-ELLTdPPLLFCDEPTS 195
|
170 180
....*....|....*....|....*....
gi 446879615 166 DFDENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-168 |
6.70e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.01 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLtPTAGTVMLQQQAMKNL---KNRQRAAKVGvlfQEAenQLFHSTVADE 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELdpeSWRKHLSWVG---QNP--QLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGlklqKCPADEitQRTHAALQCCQLADTANSHPLDLHS-------------AQRrmVAVAclEALSPP--LLLLDEP 163
Cdd:PRK11174 443 VLLG----NPDASD--EQLQQALENAWVSEFLPLLPQGLDTpigdqaaglsvgqAQR--LALA--RALLQPcqLLLLDEP 512
|
....*
gi 446879615 164 SRDFD 168
Cdd:PRK11174 513 TASLD 517
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
21-212 |
6.92e-11 |
|
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: 59.76 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQA----MKNLKNRQ----RAAKVGVLFQeaenqlFH 92
Cdd:COG4778 29 GVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREilalRRRTIGYVSQ------FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 93 STV----ADEI-AFGLKLQKCPADEITQRTHAALQCCQLadtanshPLDLHSA----------QRrmVAVACLEALSPPL 157
Cdd:COG4778 103 RVIprvsALDVvAEPLLERGVDREEARARARELLARLNL-------PERLWDLppatfsggeqQR--VNIARGFIADPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 158 LLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-214 |
1.09e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAENQ--LF------- 91
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEDRQSsgLYldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 92 --HSTVADEIAFGLKLQKCPAdeITQRTHAAL--QCCQLADTANShpldLHSAQRRMVAVA-CLEAlSPPLLLLDEPSRD 166
Cdd:PRK15439 361 nvCALTHNRRGFWIKPARENA--VLERYRRALniKFNHAEQAART----LSGGNQQKVLIAkCLEA-SPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446879615 167 FDENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-194 |
1.44e-10 |
|
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: 60.41 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQA-MKNLKNRQRAAKV 79
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSiLTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 80 GVLFQEAENQLfhsTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLL 159
Cdd:TIGR01257 2017 CPQFDAIDDLL---TGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190
....*....|....*....|....*....|....*
gi 446879615 160 LDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-170 |
1.58e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.97 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWpgAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlkNRQRAAKVG 80
Cdd:PRK09544 4 LVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAE-NQLFHSTVADEIAFGLKLQKCPADEITQRTHAAlqccQLADtansHPLDLHSA---QRRMVAVACLEalSPP 156
Cdd:PRK09544 71 YVPQKLYlDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAG----HLID----APMQKLSGgetQRVLLARALLN--RPQ 140
|
170
....*....|....
gi 446879615 157 LLLLDEPSRDFDEN 170
Cdd:PRK09544 141 LLVLDEPTQGVDVN 154
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-206 |
1.87e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 59.33 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAK---VGVLFQEAENQLF-HSTVA 96
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNpRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLKL--QKCPADEITQRTHA-ALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLS 173
Cdd:PRK15079 119 EIIAEPLRTyhPKLSRQEVKDRVKAmMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQA 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 446879615 174 VFESWLEKCgQR--GTSVVAISHDAAFTrRHFS-RV 206
Cdd:PRK15079 199 QVVNLLQQL-QRemGLSLIFIAHDLAVV-KHISdRV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-212 |
2.35e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNlKNRQRAAKVGVL---------FQEAENQLF 91
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVpqfdnldleFTVRENLLV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 92 HSTVadeiaFGLKlqkcpADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENW 171
Cdd:PRK13536 138 FGRY-----FGMS-----TREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446879615 172 LSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK13536 208 RHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-212 |
2.74e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.49 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLT----PTAGTVML----QQQAMKNLKNRQRAAKVGVLFQEAeNQLFHS 93
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLgrtvQREGRLARDIRKSRANTGYIFQQF-NLVNRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEIAFGlKLQKCP---------ADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPS 164
Cdd:PRK09984 102 SVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446879615 165 RDFDENWLSVFESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK09984 181 ASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-75 |
3.59e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.58 E-value: 3.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMkNLKNRQR 75
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDRRR 72
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-168 |
4.01e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQqamKNLKNRQRAAKVGVLFQEAENQLFHSTVaDEIAF 101
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAYLGHLPGLKADLSTL-ENLHF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 102 GLKLQKCPADeitQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLeALSP-PLLLLDEPSRDFD 168
Cdd:PRK13543 106 LCGLHGRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARL-WLSPaPLWLLDEPYANLD 169
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-212 |
4.28e-10 |
|
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: 57.09 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATD---CLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlknrQRAAK 78
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 79 VGVLFQEAenQLFHSTVADEIAFGLklqkcPADEitQRTHAALQCCQL-ADTANSHPLD----------LHSAQRRMVAV 147
Cdd:cd03250 68 IAYVSQEP--WIQNGTIRENILFGK-----PFDE--ERYEKVIKACALePDLEILPDGDlteigekginLSGGQKQRISL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 148 AclEAL--SPPLLLLDEP--SRDFD-ENWLsvFESWLEKCGQRGTSVVAISHDAAFTrRHFSRVVRLEDG 212
Cdd:cd03250 139 A--RAVysDADIYLLDDPlsAVDAHvGRHI--FENCILGLLLNNKTRILVTHQLQLL-PHADQIVVLDNG 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-194 |
4.67e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGA-ATDclcDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLtPTA---GTVML--QQQAMKNLKNRQ 74
Cdd:PRK13549 5 LLEMKNITKTFGGVkALD---NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFegEELQASNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 75 RAAKVgVLFQEaenqLF---HSTVADEIAFGLKLQK---CPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVA 148
Cdd:PRK13549 81 RAGIA-IIHQE----LAlvkELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446879615 149 clEALSPP--LLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISH 194
Cdd:PRK13549 156 --KALNKQarLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
19-168 |
5.06e-10 |
|
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: 57.28 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTP---TAGTVMLQQQAMKNLKNRQRAAKVgvlfQEAENQLFHSTV 95
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYV----RQDDILLPGLTV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 96 ADEIAFG--LKLQKCPADEITQRTHAALQCCQLADTANSHPL--DLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:cd03234 99 RETLTYTaiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
19-215 |
6.71e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA----KVGVLFQEAenQLFHST 94
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakHVGFVFQSF--MLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADE-IAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLS 173
Cdd:PRK10584 104 NALEnVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446879615 174 VFESWLEKCGQR-GTSVVAISHDAAFTRRhFSRVVRLEDGLIR 215
Cdd:PRK10584 184 KIADLLFSLNREhGTTLILVTHDLQLAAR-CDRRLRLVNGQLQ 225
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-223 |
6.85e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.41 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 33 ALTGDNGAGKSTLLRVMAGLLTPTAG-----TVMLQQQAMKNLKN----RQRaakVGVLFQEAENqlFHSTVADEIAFGL 103
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlefRRR---VGMLFQRPNP--FPMSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 104 KLQK-CPADEITQRTHAALQCCQLADTA----NSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFESW 178
Cdd:PRK14271 126 RAHKlVPRKEFRGVAQARLTEVGLWDAVkdrlSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446879615 179 LEKCGQRGTsVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK14271 206 IRSLADRLT-VIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-212 |
1.10e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 57.51 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlknrQRAAKVGVLF--QEAenQLFHSTVADE 98
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-------------ARPAGARVLFlpQRP--YLPLGTLREA 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQKCPADEItqrtHAALQCCQLADTANShpLDLHSA---------QRRmVAVACLEALSPPLLLLDEPSRDFDE 169
Cdd:COG4178 446 LLYPATAEAFSDAEL----REALEAVGLGHLAER--LDEEADwdqvlslgeQQR-LAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446879615 170 -NWLSVFESWLEKCgqRGTSVVAISHDAAfTRRHFSRVVRLEDG 212
Cdd:COG4178 519 eNEAALYQLLREEL--PGTTVISVGHRST-LAAFHDRVLELTGD 559
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-214 |
1.33e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.63 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTP----TAGTVMLQQQAMKNLKNRQRaaKVGVLFQ---EAENQLfHS 93
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGR--KIATIMQnprSAFNPL-HT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEIAFGLKLQKCPADeitQRTHAALQCCQLADTA---NSHPLDLHSA--QRRMVAVACL-EAlspPLLLLDEPSRDF 167
Cdd:PRK10418 98 MHTHARETCLALGKPADD---ATLTAALEAVGLENAArvlKLYPFEMSGGmlQRMMIALALLcEA---PFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446879615 168 D----ENWLSVFESWLEkcgQRGTSVVAISHDAAFTRRHFSRVVRLEDGLI 214
Cdd:PRK10418 172 DvvaqARILDLLESIVQ---KRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-191 |
1.57e-09 |
|
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: 56.08 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAenQLFHSTVADE 98
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDT--VLFNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGlklqKCPADEITQRthAALQCCQLADTANSHP-----------LDLHSAQRRMVAVACLEALSPPLLLLDEPSRDF 167
Cdd:cd03253 95 IRYG----RPDATDEEVI--EAAKAAQIHDKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180
....*....|....*....|....*
gi 446879615 168 D-ENWLSVFESWLEKCGQRGTSVVA 191
Cdd:cd03253 169 DtHTEREIQAALRDVSKGRTTIVIA 193
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
19-223 |
2.99e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.60 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTA--------GTVMLQQQAMKNLKNRQRAAKVGVLFQEAENQL 90
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 91 FHStvADEIA-FGLKLQKCPADEITQRTHA-ALQCCQLADTAnshPLD------LHSAQRRMVAVACL--------EALS 154
Cdd:PRK13547 97 AFS--AREIVlLGRYPHARRAGALTHRDGEiAWQALALAGAT---ALVgrdvttLSGGELARVQFARVlaqlwpphDAAQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446879615 155 PP-LLLLDEPSRDFD--------ENWLSVFESWlekcgQRGtsVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDI 223
Cdd:PRK13547 172 PPrYLLLDEPTAALDlahqhrllDTVRRLARDW-----NLG--VLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-195 |
4.00e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQamknlknrqraaKVGV 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK------------PVTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 82 LFQEAENQLFHSTVADEIAFG--LKLQKCPADEitQRTHAALQCCQLAD--TANSHP---LDLHSAQRRMVA--VACLEa 152
Cdd:PRK10522 390 EQPEDYRKLFSAVFTDFHLFDqlLGPEGKPANP--ALVEKWLERLKMAHklELEDGRisnLKLSKGQKKRLAllLALAE- 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446879615 153 lSPPLLLLDEPSRDFDENWLSVF-ESWLEKCGQRGTSVVAISHD 195
Cdd:PRK10522 467 -ERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHD 509
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-201 |
4.27e-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: 55.71 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQqamknlknrqrAAKVGVLFQEAENQLFHSTVADEIA 100
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-----------TVKLAYVDQSRDALDPNKTVWEEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 101 FGLKLQKCPADEITQRTHAALQCCQLADTANSHPlDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFESWLE 180
Cdd:TIGR03719 409 GGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVG-QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
170 180
....*....|....*....|.
gi 446879615 181 KCGqrGTSVVaISHDAAFTRR 201
Cdd:TIGR03719 488 NFA--GCAVV-ISHDRWFLDR 505
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-60 |
4.87e-09 |
|
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: 53.70 E-value: 4.87e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAatDCLC-DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTV 60
Cdd:cd03223 1 IELENLSLATPDG--RVLLkDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI 58
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-194 |
6.04e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAM--KNLKNRQRAAk 78
Cdd:PRK10762 4 LLQLKGIDKAFPGVKA--LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQEAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 79 VGVLFQEAeNQLFHSTVADEI--------AFGLKLQK---CPADEITQRthaalqccqLADTANSHPL--DLHSAQRRMV 145
Cdd:PRK10762 81 IGIIHQEL-NLIPQLTIAENIflgrefvnRFGRIDWKkmyAEADKLLAR---------LNLRFSSDKLvgELSIGEQQMV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446879615 146 AVAclEALS--PPLLLLDEPSRDF-DENWLSVF----ESWLEKCGqrgtsVVAISH 194
Cdd:PRK10762 151 EIA--KVLSfeSKVIIMDEPTDALtDTETESLFrvirELKSQGRG-----IVYISH 199
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-221 |
6.55e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGL-----LTPTAGTVMLQQQAMKNLK---NRQRAaKVGVLFQEAenQLFHS 93
Cdd:PRK14258 26 VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRvnlNRLRR-QVSMVHPKP--NLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 94 TVADEIAFGLKLQKC-PADEITQRTHAALQCCQLADTA----NSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK14258 103 SVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDEIkhkiHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 169 ENWLSVFESWLEKCGQRGT-SVVAISHD----------AAFTRRHFSRVVRL-EDGLIRNV--NPPD 221
Cdd:PRK14258 183 PIASMKVESLIQSLRLRSElTMVIVSHNlhqvsrlsdfTAFFKGNENRIGQLvEFGLTKKIfnSPHD 249
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-164 |
1.12e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRWpgAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVG 80
Cdd:PRK11614 5 MLSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAENQLFHSTVADEIAFG-LKLQKCPADEITQRTHAALQccQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLL 159
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGgFFAERDQFQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
....*
gi 446879615 160 LDEPS 164
Cdd:PRK11614 161 LDEPS 165
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-194 |
1.36e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 54.25 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTllrvMAGLLTP----TAGTVML-----QQQAMKNLKN 72
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLdghdlRDYTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 73 rqraaKVGVLFQEAenQLFHSTVADEIAFGLKlQKCPADEItqrTHAALQCCQLaDTANS--HPLD---------LHSAQ 141
Cdd:PRK11176 418 -----QVALVSQNV--HLFNDTIANNIAYART-EQYSREQI---EEAARMAYAM-DFINKmdNGLDtvigengvlLSGGQ 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 142 RRMVAVAclEAL--SPPLLLLDEPSRDFDENWLSVFESWLEKCGQRGTSVVaISH 194
Cdd:PRK11176 486 RQRIAIA--RALlrDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAH 537
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-163 |
1.50e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.50 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGL--LTPTA---GTVMLQQQamkNLKNRQ------RaAKVGVLFQEAe 87
Cdd:COG1117 27 LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGE---DIYDPDvdvvelR-RRVGMVFQKP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 88 NqLFHSTVADEIAFGLKLQ----KCPADEITQR--THAALqccqladtanshpLD-----LH-SA-------QRRMvava 148
Cdd:COG1117 102 N-PFPKSIYDNVAYGLRLHgiksKSELDEIVEEslRKAAL-------------WDevkdrLKkSAlglsggqQQRL---- 163
|
170
....*....|....*...
gi 446879615 149 CLE---ALSPPLLLLDEP 163
Cdd:COG1117 164 CIAralAVEPEVLLMDEP 181
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-60 |
2.06e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 2.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTV 60
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
22-203 |
2.13e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQqqamKNLknrqraaKVGVLFQEA---ENQlfhsTVADE 98
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD----PNE-------RLGKLRQDQfafEEF----TVLDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFG-LKLQKCPAD--------EITQR--THAALQCCQLAD----TANSH----------PLDLHSAQRRMVA------V 147
Cdd:PRK15064 85 VIMGhTELWEVKQErdriyalpEMSEEdgMKVADLEVKFAEmdgyTAEARagelllgvgiPEEQHYGLMSEVApgwklrV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446879615 148 ACLEAL--SPPLLLLDEPSRDFDENWLsvfeSWLEKC-GQRGTSVVAISHDaaftrRHF 203
Cdd:PRK15064 165 LLAQALfsNPDILLLDEPTNNLDINTI----RWLEDVlNERNSTMIIISHD-----RHF 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-85 |
2.68e-08 |
|
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: 52.14 E-value: 2.68e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGL--LTPTAGTVMLQQQAMKNLKNRQRAAK-VGVLFQE 85
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLgIFLAFQY 85
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-168 |
2.88e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.47 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVM--AGLLTP---TAGTVMLQQQAM--KNLKNRQRAAKVGVLFQEAENqlF 91
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNP--F 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 92 HSTVADEIAFGLKLQ----KCPADEITQRT-HAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRD 166
Cdd:PRK14239 99 PMSIYENVVYGLRLKgikdKQVLDEAVEKSlKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
..
gi 446879615 167 FD 168
Cdd:PRK14239 179 LD 180
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-80 |
3.63e-08 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 51.28 E-value: 3.63e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446879615 17 DCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQR-AAKVG 80
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiRAGIA 78
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-212 |
4.01e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 52.36 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLL------TPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAeNQLFH 92
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQP-NPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 93 STVADEIAFGLKLQKCPAD-EITQRTHAALQCC----QLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDF 167
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446879615 168 DENWLSVFESWLEKCgQRGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK14246 185 DIVNSQAIEKLITEL-KNEIAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-212 |
4.51e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 24 LQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAmknlknrqraaKVGVLFQEAENQLfHSTVADEIAFGL 103
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDL-----------IVARLQQDPPRNV-EGTVYDFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 104 K---------------LQKCPADEITQRThAALQ------------------CCQLADTANSHPLDLHSAQRRMVAVAcl 150
Cdd:PRK11147 92 EeqaeylkryhdishlVETDPSEKNLNEL-AKLQeqldhhnlwqlenrinevLAQLGLDPDAALSSLSGGWLRKAALG-- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 151 EAL--SPPLLLLDEPSRDFD-------ENWLSVFeswlekcgqRGtSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK11147 169 RALvsNPDVLLLDEPTNHLDietiewlEGFLKTF---------QG-SIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
21-60 |
6.06e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.85 E-value: 6.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTV 60
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-195 |
6.99e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 32 LALTGDNGAGKSTLLRVMAGLLTPTAGTVMlqqqamknlknrqRAAKV--GVLFQEAENQLFHSTVADeiafgLKLQKCP 109
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVF-------------RSAKVrmAVFSQHHVDGLDLSSNPL-----LYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 110 ADEITQRTHAALQCCQLADTANSHPL-DLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDenwLSVFESWLEKCGQRGTS 188
Cdd:PLN03073 600 PGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVEALIQGLVLFQGG 676
|
....*..
gi 446879615 189 VVAISHD 195
Cdd:PLN03073 677 VLMVSHD 683
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-162 |
8.16e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.89 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 7 ISYRWPGAATdCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEA 86
Cdd:PRK13657 340 VSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 87 enQLFHSTVADEIAFGlklqkcPADEITQRTHAALQCCQLAD--TANSHPLDLHSA-----------QRRMVAVACLEal 153
Cdd:PRK13657 419 --GLFNRSIEDNIRVG------RPDATDEEMRAAAERAQAHDfiERKPDGYDTVVGergrqlsggerQRLAIARALLK-- 488
|
....*....
gi 446879615 154 SPPLLLLDE 162
Cdd:PRK13657 489 DPPILILDE 497
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-163 |
9.40e-08 |
|
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: 51.40 E-value: 9.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 15 ATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlKNRQRaakvgVLFQEAENQLFHST 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------KHSGR-----ISFSSQFSWIMPGT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFGLKLqkcpaDEItqRTHAALQCCQLADTANSHP-----------LDLHSAQRRMVAVACLEALSPPLLLLDEP 163
Cdd:cd03291 114 IKENIIFGVSY-----DEY--RYKSVVKACQLEEDITKFPekdntvlgeggITLSGGQRARISLARAVYKDADLYLLDSP 186
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-193 |
1.38e-07 |
|
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: 51.45 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 16 TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlKNRQRaakvgVLFQEAENQLFHSTV 95
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------KHSGR-----ISFSPQTSWIMPGTI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ADEIAFGLKLqkcpaDEItqRTHAALQCCQLADTANSHP-----------LDLHSAQRRMVAVACLEALSPPLLLLDEPS 164
Cdd:TIGR01271 504 KDNIIFGLSY-----DEY--RYTSVIKACQLEEDIALFPekdktvlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190
....*....|....*....|....*....|..
gi 446879615 165 RDFD---ENwlSVFESWLEKCGQRGTSVVAIS 193
Cdd:TIGR01271 577 THLDvvtEK--EIFESCLCKLMSNKTRILVTS 606
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-120 |
1.62e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKN---RQRAAK 78
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLdswRSRLAV 393
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446879615 79 VgvlfqeaeNQ---LFHSTVADEIAFGlklqkCPADEITQRTHAA 120
Cdd:PRK10789 394 V--------SQtpfLFSDTVANNIALG-----RPDATQQEIEHVA 425
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-197 |
1.72e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.90 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYRW-----PGAATDclcDISLQLKQGEWLALTGDNGAGKS-TLLRVMAGLLTPtaGTVMLQQ-----QAMKN 69
Cdd:PRK11022 3 LLNVDKLSVHFgdesaPFRAVD---RISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEKlefngQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 70 LKNRQR----AAKVGVLFQEAENQLFHS-TVADEIAFGLKL-QKCPADEITQRTHAALQCCQLADTANS-----HPLDLH 138
Cdd:PRK11022 78 ISEKERrnlvGAEVAMIFQDPMTSLNPCyTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvypHQLSGG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 139 SAQRRMVAVACleALSPPLLLLDEPSRDFDEN-WLSVFESWLEKCGQRGTSVVAISHDAA 197
Cdd:PRK11022 158 MSQRVMIAMAI--ACRPKLLIADEPTTALDVTiQAQIIELLLELQQKENMALVLITHDLA 215
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-194 |
2.89e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 50.49 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNrqRAAKVGVLFQEAENQLFHSTVADE 98
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH--SVLRQGVAMVQQDPVVLADTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQKcpadeitQRTHAALQCCQLADTANSHPLDLHS-----------AQRRMVAVACLEALSPPLLLLDEPSRDF 167
Cdd:PRK10790 435 VTLGRDISE-------EQVWQALETVQLAELARSLPDGLYTplgeqgnnlsvGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180
....*....|....*....|....*..
gi 446879615 168 DENWLSVFESWLEKCGQRGTSVVaISH 194
Cdd:PRK10790 508 DSGTEQAIQQALAAVREHTTLVV-IAH 533
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-198 |
5.35e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlknrQRAAKVGVLF--QEAENQLFHSTVADE 98
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-------------HCGTKLEVAYfdQHRAELDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKlqkcpadEIT---QRTHAA--LQccqladtanshplD-LHSAQRRMVAVACLEA------------LSPP-LLL 159
Cdd:PRK11147 404 LAEGKQ-------EVMvngRPRHVLgyLQ-------------DfLFHPKRAMTPVKALSGgernrlllarlfLKPSnLLI 463
|
170 180 190
....*....|....*....|....*....|....*....
gi 446879615 160 LDEPSRDFDENWLSVFESWLEkcGQRGTsVVAISHDAAF 198
Cdd:PRK11147 464 LDEPTNDLDVETLELLEELLD--SYQGT-VLLVSHDRQF 499
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-219 |
6.66e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.47 E-value: 6.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAA---KVGVLFQEAENQLF-HSTVA 96
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDPYASLDpRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLKLQKCPADEITQRTHAAL--QCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLS- 173
Cdd:PRK10261 422 DSIMEPLRVHGLLPGKAAAARVAWLleRVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGq 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446879615 174 VFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNP 219
Cdd:PRK10261 502 IINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP 547
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-103 |
6.74e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ-QQAMKNLKNRQRAAKVGVLFQEAenQLFHSTVADEI 99
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDP--LLFSNSIKNNI 480
|
....
gi 446879615 100 AFGL 103
Cdd:PTZ00265 481 KYSL 484
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
7-168 |
8.70e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 7 ISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNlKNRQ------------ 74
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRR-RSRQvielseqsaaqm 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 75 ---RAAKVGVLFQE---AENQLFhsTVADEIAFGLKL-QKCPADEITQRTHAALQCCQLADTA---NSHPLDLHSAQRRM 144
Cdd:PRK10261 99 rhvRGADMAMIFQEpmtSLNPVF--TVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQR 176
|
170 180
....*....|....*....|....
gi 446879615 145 VAVACLEALSPPLLLLDEPSRDFD 168
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALD 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-195 |
9.28e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.42 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKN-----LKNRQRaaKVGVLFQEAENQLF-H 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpeaQKLLRQ--KIQIVFQNPYGSLNpR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 93 STVADEIAFGLKLQ-KCPADEITQRTHAALQCCQL-ADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFD-- 168
Cdd:PRK11308 109 KKVGQILEEPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDvs 188
|
170 180
....*....|....*....|....*....
gi 446879615 169 --ENWLSVFESwLEKcgQRGTSVVAISHD 195
Cdd:PRK11308 189 vqAQVLNLMMD-LQQ--ELGLSYVFISHD 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-223 |
9.39e-07 |
|
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: 48.65 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGL--LTPTAGTVM------------------------------LQQQA 66
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlePEEVD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 67 MKNLKNRQRAA---KVGVLFQEAENQLFHSTVADEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRR 143
Cdd:TIGR03269 96 FWNLSDKLRRRirkRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEKQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 144 MVAVACLEALSPPLLLLDEPSRDFD-ENWLSVFESWLEKCGQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDD 222
Cdd:TIGR03269 176 RVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDE 255
|
.
gi 446879615 223 I 223
Cdd:TIGR03269 256 V 256
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-168 |
9.72e-07 |
|
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: 47.87 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNL---KNRQRaakVGVLFQEAenQLFHSTV 95
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIglhDLRSR---ISIIPQDP--VLFSGTI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 96 ADEIAFglkLQKCPADEItqrtHAALQCCQLADTANSHP--LDLH--------SA-QRRMVAVAclEAL--SPPLLLLDE 162
Cdd:cd03244 95 RSNLDP---FGEYSDEEL----WQALERVGLKEFVESLPggLDTVveeggenlSVgQRQLLCLA--RALlrKSKILVLDE 165
|
....*.
gi 446879615 163 PSRDFD 168
Cdd:cd03244 166 ATASVD 171
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
21-195 |
1.14e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 47.85 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGL--LTPTA---GTVM-----LQQQAMKNLKNRQRaakVGVLFQEAENql 90
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTfhgknLYAPDVDPVEVRRR---IGMVFQKPNP-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 91 FHSTVADEIAFGLKLQ--KCPADEITQRT--HAALQcCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRD 166
Cdd:PRK14243 103 FPKSIYDNIAYGARINgyKGDMDELVERSlrQAALW-DEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180
....*....|....*....|....*....
gi 446879615 167 FDENWLSVFESWLEKCGQRGTsVVAISHD 195
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYT-IIIVTHN 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-212 |
1.19e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 7 ISYRWPGAATDCLCDISLQLKQGEWLALTGDNGAGKS-TLLRVMAGLLTP----TAGTVMLQQQAMKNLKNRQ----RAA 77
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTlrgvRGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVLFQEAENQL--FHsTVADEIAFGLKLQKcpadeiTQRTHAA----LQCC------QLADTANSHPLDLHSA--QRR 143
Cdd:PRK15134 93 KIAMIFQEPMVSLnpLH-TLEKQLYEVLSLHR------GMRREAArgeiLNCLdrvgirQAAKRLTDYPHQLSGGerQRV 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 144 MVAVACLEalSPPLLLLDEPSRDFDENWLSVFESWLEKCGQR-GTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:PRK15134 166 MIAMALLT--RPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-214 |
1.31e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 29 GEWLALTGDNGAGKSTLLRVMAGLLTPT--AGTVMLQQQAMknlkNRQRAAKVGVLFQeaENQLF-HSTVADEIAFG--L 103
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP----TKQILKRTGFVTQ--DDILYpHLTVRETLVFCslL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 104 KLQKCPADEITQR------THAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSRDFDENWLSVFES 177
Cdd:PLN03211 168 RLPKSLTKQEKILvaesviSELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190
....*....|....*....|....*....|....*..
gi 446879615 178 WLEKCGQRGTSVVAISHDAAftrrhfSRVVRLEDGLI 214
Cdd:PLN03211 248 TLGSLAQKGKTIVTSMHQPS------SRVYQMFDSVL 278
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-51 |
3.19e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 3.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446879615 1 MLTLNKISYRWPGAATdcLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAG 51
Cdd:NF040905 1 ILEMRGITKTFPGVKA--LDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-62 |
3.32e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.94 E-value: 3.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVML 62
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL 311
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-213 |
4.94e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.06 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 32 LALTGDNGAGKSTLLRVMAGLLTPTAGTVMLqqqamknlknrqraakvgvlfqeaenqlfhstvadeiafglklqkCPAD 111
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------IDGE 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 112 EITQRTHAALQCcqlaDTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPSR------DFDENWLSVFESWLEKCGQR 185
Cdd:smart00382 40 DILEEVLDQLLL----IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSlldaeqEALLLLLEELRLLLLLKSEK 115
|
170 180 190
....*....|....*....|....*....|...
gi 446879615 186 GTSVVAISH-----DAAFTRRHFSRVVRLEDGL 213
Cdd:smart00382 116 NLTVILTTNdekdlGPALLRRRFDRRIVLLLIL 148
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-168 |
5.60e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 46.26 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTP---TAGTVMLQQQAMKNLK----NRQRAAKVGVLFQEAENQLF-H 92
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPekelNKLRAEQISMIFQDPMTSLNpY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 93 STVADEIAFGLKLQK----CPADEITQRTHAALQCCQLADTANSHPLDLHSA--QRRMVAVACLeaLSPPLLLLDEPSRD 166
Cdd:PRK09473 114 MRVGEQLMEVLMLHKgmskAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGmrQRVMIAMALL--CRPKLLIADEPTTA 191
|
..
gi 446879615 167 FD 168
Cdd:PRK09473 192 LD 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-64 |
5.82e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 45.72 E-value: 5.82e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLL--TPTAGTVMLQQ 64
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD 93
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-80 |
6.75e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 6.75e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQ-RAAKVG 80
Cdd:COG3845 276 DVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVA 336
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-146 |
7.17e-06 |
|
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: 45.48 E-value: 7.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQ-----LKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQ--------QQAMKNLKNRQRAakvgVLFQE 85
Cdd:cd03237 10 LGEFTLEveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEldtvsykpQYIKADYEGTVRD----LLSSI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446879615 86 AENQLFHSTVADEIAFGLKLQKCPADEIT-------QRThaALQCCqLADTANSHPLD-----LHSAQRRMVA 146
Cdd:cd03237 86 TKDFYTHPYFKTEIAKPLQIEQILDREVPelsggelQRV--AIAAC-LSKDADIYLLDepsayLDVEQRLMAS 155
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-163 |
7.60e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 45.64 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATdCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTV-MLQQQAMKNLKNRQRAAkvg 80
Cdd:PRK15056 7 IVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRQALQKNLVAY--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 VLFQEAENQLFHSTVADEIAFG----LKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPP 156
Cdd:PRK15056 83 VPQSEEVDWSFPVLVEDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
....*..
gi 446879615 157 LLLLDEP 163
Cdd:PRK15056 163 VILLDEP 169
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-169 |
8.45e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 1 MLTLNKISYrwpGAATDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKnRQRAAKVG 80
Cdd:PRK13541 1 MLSLHQLQF---NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-KPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 81 vlfqeaeNQL---FHSTVADEIAFGLKLQKCpadeiTQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPL 157
Cdd:PRK13541 77 -------HNLglkLEMTVFENLKFWSEIYNS-----AETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170
....*....|..
gi 446879615 158 LLLDEPSRDFDE 169
Cdd:PRK13541 145 WLLDEVETNLSK 156
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-163 |
1.20e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMK------NLKNRQRaaKVGVLFQEAenQLF-HS 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdaekgiCLPPEKR--RIGYVFQDA--RLFpHY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446879615 94 TVADEIAFGLKlQKCPA--DEITQrthaALQCCQLADtanSHPLDLHSAQRRMVAVAclEAL--SPPLLLLDEP 163
Cdd:PRK11144 92 KVRGNLRYGMA-KSMVAqfDKIVA----LLGIEPLLD---RYPGSLSGGEKQRVAIG--RALltAPELLLMDEP 155
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
16-84 |
4.41e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 4.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446879615 16 TDCLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAG--LLTPTAGTVMLQQQAMKNLKNRQRaAKVGVL--FQ 84
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEER-AHLGIFlaFQ 91
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-168 |
5.10e-05 |
|
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: 42.62 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 2 LTLNKISYRWPGAATD--CLCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTP--TAGTVMLQQQAMKnlKNRQRaa 77
Cdd:cd03232 4 LTWKNLNYTVPVKGGKrqLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLD--KNFQR-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 78 KVGVlfqeAENQLFH---STVADEIAFglklqkcpadeitqrtHAALQccqladtanshplDLHSAQRRMVAVACLEALS 154
Cdd:cd03232 80 STGY----VEQQDVHspnLTVREALRF----------------SALLR-------------GLSVEQRKRLTIGVELAAK 126
|
170
....*....|....
gi 446879615 155 PPLLLLDEPSRDFD 168
Cdd:cd03232 127 PSILFLDEPTSGLD 140
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-225 |
5.11e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVmlqqqamknlknrQRAAKVGVLFQEA--ENQLfhsTVA 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-------------DRNGEVSVIAISAglSGQL---TGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLKLQKCPADEITQRTHAALQCCQLADTANSHPLDLHSAQRRMVAVACLEALSPPLLLLDEPsrdfdenwLSVF- 175
Cdd:PRK13546 104 ENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA--------LSVGd 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446879615 176 ESWLEKC-------GQRGTSVVAISHDAAFTRRHFSRVVRLEDGLIRNVNPPDDIHP 225
Cdd:PRK13546 176 QTFAQKCldkiyefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLP 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-102 |
6.83e-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: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKnrQ---RAAkVGVLFQEAenQLFHSTV 95
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT--QaslRAA-IGIVPQDT--VLFNDTI 448
|
....*..
gi 446879615 96 ADEIAFG 102
Cdd:COG5265 449 AYNIAYG 455
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-56 |
9.88e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.29 E-value: 9.88e-05
10 20 30
....*....|....*....|....*....|....*.
gi 446879615 21 DISLQlKQGEWLALTGDNGAGKSTLLRVMAGLLTPT 56
Cdd:COG3950 18 EIDFD-NPPRLTVLVGENGSGKTTLLEAIALALSGL 52
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-195 |
1.21e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.59 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMkNLKNRQRAAKVGVLF----QEAENQLFHSTVAD 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAIRAGIMLcpedRKAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 98 EIAfglklqkcpadeITQRTHAALQCCQL-----ADTANSHPLDLH----SAQRRMVAV-------ACL-EALSPPL--L 158
Cdd:PRK11288 351 NIN------------ISARRHHLRAGCLInnrweAENADRFIRSLNiktpSREQLIMNLsggnqqkAILgRWLSEDMkvI 418
|
170 180 190
....*....|....*....|....*....|....*..
gi 446879615 159 LLDEPSRDFDENWLSVFESWLEKCGQRGTSVVAISHD 195
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSD 455
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-69 |
1.41e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 42.30 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKN 69
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT 318
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-192 |
1.43e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 23 SLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKNLKNRQRAAKVGVLFQEAENQLFHstvADEIAFG 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLS---PGEDDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 103 lklqKCPADEITQRTHAALQCCQLADTAN-SHPLD-----LHSAQRRMVAVAclEAL--SPPLLLLDEPSRDFDENWLSV 174
Cdd:PRK10938 100 ----RTTAEIIQDEVKDPARCEQLAQQFGiTALLDrrfkyLSTGETRKTLLC--QALmsEPDLLILDEPFDGLDVASRQQ 173
|
170
....*....|....*...
gi 446879615 175 FESWLEKCGQRGTSVVAI 192
Cdd:PRK10938 174 LAELLASLHQSGITLVLV 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
19-62 |
1.43e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVML 62
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL 371
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-60 |
1.43e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 1.43e-04
10 20 30
....*....|....*....|....*....|....*.
gi 446879615 25 QLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTV 60
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV 396
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-66 |
2.78e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 2.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQA 66
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA 87
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
33-55 |
2.92e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 2.92e-04
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-212 |
4.29e-04 |
|
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: 39.94 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTA---GTVMLQQQAMKNLKNRQRAAkvgVLFQEAENQLFHS-T 94
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGE---IIYVSEEDVHFPTlT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 95 VADEIAFGLklqKCPADEITQrthaalqccqladtanshplDLHSAQRRMVAVAclEAL-SPPLLLL-DEPSRDFDENwl 172
Cdd:cd03233 100 VRETLDFAL---RCKGNEFVR--------------------GISGGERKRVSIA--EALvSRASVLCwDNSTRGLDSS-- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446879615 173 SVFE--SWLEKCGQ--RGTSVVAISHDAAFTRRHFSRVVRLEDG 212
Cdd:cd03233 153 TALEilKCIRTMADvlKTTTFVSLYQASDEIYDLFDKVLVLYEG 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
36-60 |
5.14e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 5.14e-04
10 20
....*....|....*....|....*
gi 446879615 36 GDNGAGKSTLLRVMAGLLTPTAGTV 60
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-168 |
7.27e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.77 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 22 ISLQLKQGEWLALTGDNGAGKSTLLRVMAGL--LTPTAGTVMLQQQAMKNLKNRQRAAK-VGVLFQE------AENQLFH 92
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYpveipgVSNQFFL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 93 STV------------------ADEIAFGLKLQKCPADEITQRTHAALQccqladtanshpldlhSAQRRMVAVACLEALS 154
Cdd:PRK09580 100 QTAlnavrsyrgqepldrfdfQDLMEEKIALLKMPEDLLTRSVNVGFS----------------GGEKKRNDILQMAVLE 163
|
170
....*....|....
gi 446879615 155 PPLLLLDEPSRDFD 168
Cdd:PRK09580 164 PELCILDESDSGLD 177
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-58 |
8.82e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.71 E-value: 8.82e-04
10 20 30
....*....|....*....|....*....|...
gi 446879615 26 LKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAG 58
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD 54
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-215 |
3.10e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 38.42 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 19 LCDISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAmknlknrqraakvgVLFQEAENQLFHSTVADE 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGS--------------VAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 99 IAFGLKLQkcpadeiTQRTHAALQCcqladTANSHPLDL----------------HSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:PLN03232 699 ILFGSDFE-------SERYWRAIDV-----TALQHDLDLlpgrdlteigergvniSGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446879615 163 PSRDFDENWL-SVFESWLeKCGQRGTSVVAISHDAAFTRRhFSRVVRLEDGLIR 215
Cdd:PLN03232 767 PLSALDAHVAhQVFDSCM-KDELKGKTRVLVTNQLHFLPL-MDRIILVSEGMIK 818
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-168 |
7.61e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 37.07 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 21 DISLQLKQGEWLALTGDNGAGKSTLLRVMAGLLTPTAGTVMLQQQAMKnLKNRQRAAKVGVLF---QEAENQLFHS-TVA 96
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPLDAVKKGMAYiteSRRDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446879615 97 DEIAFGLKLQKC----------PADEI----TQRTHAALQCCQLadtaNSHPLDLHSAQRRMVAVACLEALSPPLLLLDE 162
Cdd:PRK09700 360 QNMAISRSLKDGgykgamglfhEVDEQrtaeNQRELLALKCHSV----NQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
....*.
gi 446879615 163 PSRDFD 168
Cdd:PRK09700 436 PTRGID 441
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
34-55 |
9.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 36.82 E-value: 9.81e-03
|
| |
