|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-224 |
7.75e-110 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 315.83 E-value: 7.75e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:COG1136 4 LLELRNLTKSYGT--GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-221 |
5.81e-101 |
|
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: 293.24 E-value: 5.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISA 82
Cdd:cd03255 1 IELKNLSKTYGG--GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03255 79 FRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-216 |
3.16e-77 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 232.51 E-value: 3.16e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 5 VKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFR 84
Cdd:TIGR03608 1 LKNISKKFGDK------VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 85 RDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPD 164
Cdd:TIGR03608 75 REKLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502662315 165 LVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFI 216
Cdd:TIGR03608 155 LILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
21-229 |
2.70e-74 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 225.70 E-value: 2.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 21 TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRdHLGFVFQDFNLLDT 100
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRR-RIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 LNVRDNIYLPLVLSKSSVELMKSRL-KILApKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKN 179
Cdd:COG2884 94 RTVYENVALPLRVTGKSRKEIRRRVrEVLD-LVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPET 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502662315 180 SEDLLNLFEEINDSGQTIIMVTH-SSLAASHAKRVLFIKDGVLYHQLYRGE 229
Cdd:COG2884 173 SWEIMELLEEINRRGTTVLIATHdLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
2-221 |
3.84e-67 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 207.26 E-value: 3.84e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRFSKeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:NF038007 1 MLNMQNAEKCYITKTIK--TKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIYLPL----VLSKSSVELMKSRLKILapklNIENLLEKQPFELSGGQKQRVAVAR 157
Cdd:NF038007 79 ILRRELIGYIFQSFNLIPHLSIFDNVALPLkyrgVAKKERIERVNQVLNLF----GIDNRRNHKPMQLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 158 ALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:NF038007 155 AMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
2.14e-62 |
|
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: 203.98 E-value: 2.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:COG1123 260 LLEVRNLSKRYPVR-GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQD-FNLLD-TLNVRDNIYLPL----VLSKSSV-----ELMKS-RLKilapklniENLLEKQPFELSGGQ 149
Cdd:COG1123 339 ELRR-RVQMVFQDpYSSLNpRMTVGDIIAEPLrlhgLLSRAERrervaELLERvGLP--------PDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 150 KQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlAVVRYIADRVAVMYDG 481
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
3.95e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 195.28 E-value: 3.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTRfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEI 80
Cdd:COG3638 1 PMLELRNLSKRYPGG-----TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRDhLGFVFQDFNLLDTLNVRDNI------YLPLVlsKSSVELMKSRLKILA----PKLNIENLLEKQPFELSGGQK 150
Cdd:COG3638 76 RRLRRR-IGMIFQQFNLVPRLSVLTNVlagrlgRTSTW--RSLLGLFPPEDRERAlealERVGLADKAYQRADQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQvDLARRYADRIIGLRDG 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-219 |
2.94e-61 |
|
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: 191.96 E-value: 2.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkeiSA 82
Cdd:cd03259 1 LELKGLSKTYG------SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-----PP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03259 70 ERRN-IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDqEEALALADRIAVMNEG 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-202 |
4.14e-61 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 195.68 E-value: 4.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISA 82
Cdd:COG1135 2 IELENLSKTFPTK--GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILapkLNIENLLEKQ---PFELSGGQKQRVAVARAL 159
Cdd:COG1135 80 ARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAEL---LELVGLSDKAdayPSQLSGGQKQRVGIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH 202
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITH 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-202 |
9.10e-61 |
|
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: 191.64 E-value: 9.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:cd03258 1 MIELKNVSKVFGDT--GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:cd03258 79 KARR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH 202
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITH 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-219 |
2.13e-60 |
|
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: 189.60 E-value: 2.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:cd03225 8 SYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL----RRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNL-LDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTA 173
Cdd:cd03225 84 PDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502662315 174 ALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:cd03225 164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDlDLLLELADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-219 |
4.98e-60 |
|
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: 189.25 E-value: 4.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:cd03257 1 LLEVKNLSVSFPTG--GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDhLGFVFQD-FNLLD-TLNVRDNIYLPLVLSKSSVElmKSRLKILAPKLNI-----ENLLEKQPFELSGGQKQRVA 154
Cdd:cd03257 79 IRRKE-IQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSK--KEARKEAVLLLLVgvglpEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502662315 155 VARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDlGVVAKIADRVAVMYAG 222
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-221 |
5.30e-60 |
|
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: 189.57 E-value: 5.30e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:COG4181 8 IIELRGLTKTVGT--GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLsKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLEL-AGRRDARARARALLE-RVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-203 |
5.40e-60 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 190.30 E-value: 5.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNkeditaikDKEI 80
Cdd:COG1116 6 PALELRGVSKRFPTG--GGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD--------GKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:COG1116 76 TGPGPD-RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS 203
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHD 198
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
23-219 |
2.46e-59 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 187.07 E-value: 2.46e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRdHLGFVFQDFNLLDTLN 102
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRR-RIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:TIGR02673 96 VYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSER 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 502662315 183 LLNLFEEINDSGQTIIMVTH-SSLAASHAKRVLFIKDG 219
Cdd:TIGR02673 176 ILDLLKRLNKRGTTVIVATHdLSLVDRVAHRVIILDDG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-219 |
3.14e-59 |
|
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: 187.54 E-value: 3.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLkkifktRFS-KEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikDKEIS 81
Cdd:COG1122 1 IELENL------SFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQD-----FNLldtlNVRDNI-YLPLVLSKSSVElMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAV 155
Cdd:COG1122 72 ELRR-KVGLVFQNpddqlFAP----TVEEDVaFGPENLGLPREE-IRERVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 156 ARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDG 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-220 |
1.93e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 185.58 E-value: 1.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAiKDKEIS 81
Cdd:COG1126 1 MIEIENLHKSFG------DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQDFNLLDTLNVRDNIYLPL--VLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:COG1126 74 KLRR-KVGMVFQQFNLFPHLTVLENVTLAPikVKKMSKAEAEERAMELLE-RVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGV 220
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEmGFAREVADRVVFMDGGR 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-219 |
3.96e-58 |
|
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: 185.08 E-value: 3.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISA 82
Cdd:cd03256 1 IEVENLSKTYP-----NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSR---------LKILApKLNIENLLEKQPFELSGGQKQRV 153
Cdd:cd03256 76 LRR-QIGMIFQQFNLIERLSVLENVLSGRLGRRSTWRSLFGLfpkeekqraLAALE-RVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 154 AVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQvDLAREYADRIVGLKDG 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-221 |
2.91e-57 |
|
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: 181.84 E-value: 2.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 21 TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRdHLGFVFQDFNLLDT 100
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRR-KIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 LNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNS 180
Cdd:cd03292 93 RNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 181 EDLLNLFEEINDSGQTIIMVTH-SSLAASHAKRVLFIKDGVL 221
Cdd:cd03292 173 WEIMNLLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-203 |
3.86e-56 |
|
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: 179.20 E-value: 3.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdkeisa 82
Cdd:cd03293 1 LEVRNVSKTYGGG--GGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 fRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03293 71 -PGPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502662315 163 PDLVLADEPTAALDF--KNS--EDLLNLFEEindSGQTIIMVTHS 203
Cdd:cd03293 150 PDVLLLDEPFSALDAltREQlqEELLDIWRE---TGKTVLLVTHD 191
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-222 |
3.03e-54 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 177.55 E-value: 3.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKP---TSGQVLLNKEDITAIKDK 78
Cdd:COG0444 1 LLEVRNLKVYFPTR--RGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 EISAFRRDHLGFVFQD-FNLLD-TLNVRDNIYLPL----VLSKS-----SVELMKsRLKILAPklniENLLEKQPFELSG 147
Cdd:COG0444 79 ELRKIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLrihgGLSKAearerAIELLE-RVGLPDP----ERRLDRYPHELSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502662315 148 GQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVlfikdGVLY 222
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDlGVVAEIADRV-----AVMY 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-221 |
3.13e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 178.37 E-value: 3.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdkeIS 81
Cdd:COG3842 5 ALELENVSKRYG------DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:COG3842 74 PEKRN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 162 QPDLVLADEPTAALDFKN----SEDLLNLFEEIndsGQTIIMVTHSSL-AASHAKRVLFIKDGVL 221
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLreemREELRRLQREL---GITFIYVTHDQEeALALADRIAVMNDGRI 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-224 |
7.86e-54 |
|
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: 174.01 E-value: 7.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:COG1127 5 MIEVRNLTKSFGDR------VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQDFNLLDTLNVRDNIYLPLV----LSKSSVE---LMKsrlkiLApKLNIENLLEKQPFELSGGQKQRVA 154
Cdd:COG1127 79 ELRR-RIGMLFQGGALFDSLTVFENVAFPLRehtdLSEAEIRelvLEK-----LE-LVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502662315 155 VARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH--SSLAAShAKRVLFIKDGVLYHQ 224
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHdlDSAFAI-ADRVAVLADGKIIAE 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-219 |
2.30e-53 |
|
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: 170.83 E-value: 2.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkDKEISA 82
Cdd:cd03229 1 LELKNVSKRYG------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDhLGFVFQDFNLLDTLNVRDNIYLPlvlskssvelmksrlkilapklnienllekqpfeLSGGQKQRVAVARALISQ 162
Cdd:cd03229 74 LRRR-IGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEIND-SGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDlDEAARLADRVVVLRDG 177
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-221 |
3.57e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 175.65 E-value: 3.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEisa 82
Cdd:COG3839 4 LELENVSKSYG------GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:COG3839 75 --RN-IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 163 PDLVLADEPTAALDFKnsedL-LNLFEEI----NDSGQTIIMVTHSSL-AASHAKRVLFIKDGVL 221
Cdd:COG3839 152 PKVFLLDEPLSNLDAK----LrVEMRAEIkrlhRRLGTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-221 |
7.02e-53 |
|
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: 170.79 E-value: 7.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAiKDKEISA 82
Cdd:cd03262 1 IEIKNLHKSFGDF------HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTLNVRDNIYLPL--VLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:cd03262 74 LRQ-KVGMVFQQFNLFPHLTVLENITLAPikVKGMSKAEAEERALELLE-KVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEmGFAREVADRVIFMDDGRI 213
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-219 |
7.53e-53 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 171.71 E-value: 7.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:TIGR02315 1 MLEVENLSKVYPN-----GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRL----KILA----PKLNIENLLEKQPFELSGGQKQRV 153
Cdd:TIGR02315 76 KLRR-RIGMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLGRFseedKERAlsalERVGLADKAYQRADQLSGGQQQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 154 AVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQvDLAKKYADRIVGLKAG 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-219 |
8.14e-53 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 181.08 E-value: 8.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:PRK10535 4 LLELKDIRRSYPS--GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:PRK10535 82 QLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-229 |
1.09e-52 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 171.14 E-value: 1.09e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeis 81
Cdd:COG1124 1 MLEVRNLSVSYGQG--GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDhLGFVFQDFnlLDTLN----VRDNIYLPLVLSKssVELMKSRLKILAPKLNI-ENLLEKQPFELSGGQKQRVAVA 156
Cdd:COG1124 76 AFRRR-VQMVFQDP--YASLHprhtVDRILAEPLRIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 157 RALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASH-AKRVLFIKDGVLYHQLYRGE 229
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-221 |
2.06e-51 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.55 E-value: 2.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdKEISA 82
Cdd:COG1131 1 IEVRGLTKRYG------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:COG1131 71 VRR-RIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRI 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-219 |
7.36e-51 |
|
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: 166.14 E-value: 7.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISA 82
Cdd:cd03261 1 IELRGLTKSF------GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTLNVRDNIYLPL----VLSKSSVElMKSRLKILApkLNIENLLEKQPFELSGGQKQRVAVARA 158
Cdd:cd03261 75 LRR-RMGMLFQSGALFDSLTVFENVAFPLrehtRLSEEEIR-EIVLEKLEA--VGLRGAEDLYPAELSGGMKKRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 159 LISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH---SSLAAshAKRVLFIKDG 219
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHdldTAFAI--ADRIAVLYDG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-202 |
8.74e-51 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 169.21 E-value: 8.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 4 EVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAF 83
Cdd:PRK11153 3 ELKNISKVFPQG--GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 84 RRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQP 163
Cdd:PRK11153 81 RRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTH 202
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINrELGLTIVLITH 199
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-224 |
1.97e-50 |
|
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: 165.60 E-value: 1.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:COG1120 1 MLEAENL------SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 afRRdhLGFVFQDFNLLDTLNVRDNI------YLPLvLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAV 155
Cdd:COG1120 75 --RR--IAYVPQEPPAPFGLTVRELValgrypHLGL-FGRPSAEDREAVEEALE-RTGLEHLADRPVDELSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 156 ARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDlNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-202 |
2.50e-50 |
|
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: 164.72 E-value: 2.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTrfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkeiSA 82
Cdd:cd03300 1 IELENVSKFYGG------FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03300 70 HKR-PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH 202
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-221 |
1.26e-49 |
|
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: 161.03 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdKEISA 82
Cdd:cd03230 1 IEVRNLSKRYGKK------TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTLNVRDNIylplvlskssvelmksrlkilapklnienllekqpfELSGGQKQRVAVARALISQ 162
Cdd:cd03230 71 VKR-RIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-224 |
2.44e-49 |
|
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: 162.33 E-value: 2.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRFskeettALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdKEIS 81
Cdd:COG4555 1 MIEVENLSKKYGKVP------ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:COG4555 71 EARR-QIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG-VLYHQ 224
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEALCDRVVILHKGkVVAQG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-221 |
5.45e-49 |
|
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: 160.50 E-value: 5.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEisa 82
Cdd:cd03301 1 VELENVTKRFG------NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03301 72 --RD-IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 163 PDLVLADEPTAALD----FKNSEDLLNLFEEIndsGQTIIMVTHSSLAA-SHAKRVLFIKDGVL 221
Cdd:cd03301 149 PKVFLMDEPLSNLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-221 |
6.03e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.37 E-value: 6.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeISA 82
Cdd:COG4619 1 LELEGL------SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTlNVRDNiyLPLVLSKSSVELMKSRLKILAPKLNI-ENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:COG4619 72 WRR-QVAYVPQEPALWGG-TVRDN--LPFPFQLRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEE-INDSGQTIIMVTHSS-LAASHAKRVLFIKDGVL 221
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
24-221 |
7.33e-49 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 160.57 E-value: 7.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQV-LLNKEdITAIKDKEISAFRRdHLGFVFQDFNLLDTLN 102
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLkVLGQE-LHGASKKQLVQLRR-RIGYIFQAHNLLGFLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPLVLS-KSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSE 181
Cdd:TIGR02982 99 ARQNVQMALELQpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502662315 182 DLLNLFEEI-NDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:TIGR02982 179 DVVELMQKLaKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-221 |
8.62e-49 |
|
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: 168.16 E-value: 8.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKkifkTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPT---SGQVLLNKEDITAIKDK 78
Cdd:COG1123 4 LLEVRDLS----VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 EisafRRDHLGFVFQDF-NLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVAR 157
Cdd:COG1123 80 L----RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 158 ALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDlGVVAEIADRVVVMDDGRI 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-219 |
9.00e-49 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 162.24 E-value: 9.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIF--KTRFskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEI 80
Cdd:TIGR04521 1 IKLKNVSYIYqpGTPF---EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRdHLGFVFQdF--NLLDTLNVRDNI-YLPLVLSKSSVELmKSRLKILAPKLNI-ENLLEKQPFELSGGQKQRVAVA 156
Cdd:TIGR04521 78 KDLRK-KVGLVFQ-FpeHQLFEETVYKDIaFGPKNLGLSEEEA-EERVKEALELVGLdEEYLERSPFELSGGQMRRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 157 RALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:TIGR04521 155 GVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSmEDVAEYADRVIVMHKG 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-223 |
1.81e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 160.25 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdkei 80
Cdd:COG1121 5 PAIELENL------TVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 safRRDHLGFVFQDFNLLDT--LNVRDNIYLPLV--------LSKSSVELMKSRLKilapKLNIENLLEKQPFELSGGQK 150
Cdd:COG1121 73 ---ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYgrrglfrrPSRADREAVDEALE----RVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYH 223
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDlGAVREYFDRVLLLNRGLVAH 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-224 |
2.14e-48 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 159.56 E-value: 2.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKifKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:PRK10584 6 IVEVHHLKK--SVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:PRK10584 84 KLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
23-222 |
8.05e-48 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 158.11 E-value: 8.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRdHLGFVFQDFNLLDTLN 102
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRR-QIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502662315 183 LLNLFEEINDSGQTIIMVTH-SSLAASHAKRVLFIKDGVLY 222
Cdd:PRK10908 176 ILRLFEEFNRVGVTVLMATHdIGLISRRSYRMLTLSDGHLH 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-224 |
3.11e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.84 E-value: 3.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 27 IDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDIT--AIKDKEISAfrrdhlgfVFQDFNLLDTLNVR 104
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTalPPAERPVSM--------LFQENNLFPHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 105 DNIYLPL--VLSKSSVElmKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:COG3840 90 QNIGLGLrpGLKLTAEQ--RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502662315 183 LLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG-VLYHQ 224
Cdd:COG3840 168 MLDLVDELCRErGLTVLMVTHDpEDAARIADRVLLVADGrIAADG 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-202 |
3.82e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 159.93 E-value: 3.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkeI 80
Cdd:COG1118 1 MSIEVRNISKRFGSF------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN----L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:COG1118 71 PPRER-RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDL-LNLFEEINDSGQTIIMVTH 202
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELrRWLRRLHDELGGTTVFVTH 192
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-224 |
3.89e-47 |
|
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: 154.90 E-value: 3.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 4 EVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISaf 83
Cdd:cd03214 1 EVENL------SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 84 rrDHLGFVFQdfnlldtlnvrdniylplvlskssvelmksrlkILApKLNIENLLEKQPFELSGGQKQRVAVARALISQP 163
Cdd:cd03214 73 --RKIAYVPQ---------------------------------ALE-LLGLAHLADRPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDlNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-173 |
1.14e-46 |
|
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: 152.42 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeisaFRRDHLGFVFQDFNLLDTLNVRD 105
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK----SLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 106 NIYLPLVLSKSSVELMKSRLKILAPKLNIENLLE----KQPFELSGGQKQRVAVARALISQPDLVLADEPTA 173
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-221 |
4.09e-46 |
|
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: 155.11 E-value: 4.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTR-----------FSKEE-------TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQ 64
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgKSKEEilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 65 VLLNKEDITAIKDKEISAFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSR-LKILApKLNIENLLEKQPF 143
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERaAEALE-LVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 144 ELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIND-SGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAeLQKTIVFITHDlDEALRLGDRIAIMKDGRL 239
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-219 |
1.27e-45 |
|
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: 150.61 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:cd03228 9 SYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL----RKNIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTlNVRDNIylplvlskssvelmksrlkilapklnienllekqpfeLSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:cd03228 85 PFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502662315 175 LDFKNSEDLLNLFEEINDsGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03228 127 LDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-223 |
1.62e-45 |
|
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: 152.49 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRFskeettaLVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkEISA 82
Cdd:cd03299 1 LKVENLSKDWKEFK-------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03299 69 EKRD-ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDGVLYH 223
Cdd:cd03299 148 PKILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDfEEAWALADKVAIMLNGKLIQ 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-219 |
6.70e-45 |
|
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: 148.16 E-value: 6.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEisafRRDHLGFVFQd 94
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE----LRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 fnlldtlnvrdniylplvlskssvelmksrlkilapklnienllekqpfeLSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:cd00267 81 --------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502662315 175 LDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:cd00267 111 LDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-224 |
7.46e-45 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 151.44 E-value: 7.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNkeDITAIKDKEISA 82
Cdd:PRK11264 4 IEVKNLVKKFHGQ------TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FR------RDHLGFVFQDFNLLDTLNVRDNIYL-PLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAV 155
Cdd:PRK11264 76 QKglirqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 156 ARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEmSFARDVADRAIFMDQGRIVEQ 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-225 |
7.88e-45 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 150.74 E-value: 7.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:PRK11629 5 LLQCDNLCKRYQE--GSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:PRK11629 83 ELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHSSLAASHAKRVLFIKDGVLYHQL 225
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
9.39e-45 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 150.55 E-value: 9.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTrfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLL--NKEDI-TAIKD 77
Cdd:PRK11124 1 MSIQLNGINCFYGA------HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFsKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEISAFRRDhLGFVFQDFNLLDTLNVRDN-IYLPL-VLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAV 155
Cdd:PRK11124 75 KAIRELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCrVLGLSKDQALARAEKLLE-RLRLKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 156 ARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEvEVARKTASRVVYMENG 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-219 |
1.64e-43 |
|
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: 147.49 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKtRFskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkei 80
Cdd:cd03296 1 MSIEVRNVSKRFG-DF-----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 saFRRDHLGFVFQDFNLLDTLNVRDNIYLPL----VLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVA 156
Cdd:cd03296 71 --VQERNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 157 RALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH-SSLAASHAKRVLFIKDG 219
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHdQEEALEVADRVVVMNKG 213
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
3.79e-43 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 146.70 E-value: 3.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTrfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLL--NKEDITA-IKD 77
Cdd:COG4161 1 MSIQLKNINCFYGS------HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFSQkPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEISAFRRDhLGFVFQDFNLLDTLNVRDN-IYLPL-VLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAV 155
Cdd:COG4161 75 KAIRLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCkVLGLSKEQAREKAMKLLA-RLRLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 156 ARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEvEFARKVASQVVYMEKG 217
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
7.86e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 147.54 E-value: 7.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTRfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQV---LLNKEDITAIKD 77
Cdd:PRK13651 1 MQIKVKNIVKIFNKK-LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEI---------SAFR--------RDHLGFVFQ--DFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLL 138
Cdd:PRK13651 80 KEKvleklviqkTRFKkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 139 EKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIK 217
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDlDNVLEWTKRTIFFK 239
|
..
gi 502662315 218 DG 219
Cdd:PRK13651 240 DG 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-219 |
8.84e-43 |
|
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: 144.32 E-value: 8.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 18 KEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItaiKDKEisafRRDHLGFVFQDFNL 97
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKE----RRKSIGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 -LDTLNVRDNIYLPLVLSKSSVELMKSRLKilapKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:cd03226 83 qLFTDSVREELLLGLKELDAGNEQAETVLK----DLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 177 FKNSEDLLNLFEEINDSGQTIIMVTH-SSLAASHAKRVLFIKDG 219
Cdd:cd03226 159 YKNMERVGELIRELAAQGKAVIVITHdYEFLAKVCDRVLLLANG 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-223 |
9.55e-43 |
|
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: 145.27 E-value: 9.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeisA 82
Cdd:cd03219 1 LEVRGLTKRFG------GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-----P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDHLGFV--FQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLK-----------ILApKLNIENLLEKQPFELSGGQ 149
Cdd:cd03219 70 HEIARLGIGrtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARReereareraeeLLE-RVGLADLADRPAGELSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 150 KQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLfikdgVLYH 223
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDmDVVMSLADRVT-----VLDQ 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
13-219 |
1.23e-42 |
|
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: 144.17 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 13 KTRFSKEETTalVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIK--DKEISAfrrdhlgf 90
Cdd:cd03298 5 KIRFSYGEQP--MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpaDRPVSM-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 91 VFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADE 170
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502662315 171 PTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASH-AKRVLFIKDG 219
Cdd:cd03298 155 PFAALDPALRAEMLDLVLDLHaETKMTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-219 |
5.01e-42 |
|
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: 146.78 E-value: 5.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKE---DITAIKDkeISAFRRdHLGFVFQDFNLLDTLN 102
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIF--LPPHRR-RIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNiyLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:COG4148 94 VRGN--LLYGRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 183 LLNLFEEINDSGQT-IIMVTHS-----SLAAshakRVLFIKDG 219
Cdd:COG4148 172 ILPYLERLRDELDIpILYVSHSldevaRLAD----HVVLLEQG 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-202 |
1.81e-41 |
|
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: 142.05 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRFskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsa 82
Cdd:cd03295 1 IEFENVTKRYGGGK-----KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIE--NLLEKQPFELSGGQKQRVAVARALI 160
Cdd:cd03295 74 --RRKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTH 202
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQqELGKTIVFVTH 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-213 |
2.44e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 140.69 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItaikDKEI 80
Cdd:COG4133 1 MMLEAENLSCRR------GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRdHLGFVFQDFNLLDTLNVRDNI-----YLPLVLSKSSVElmksrlKILApKLNIENLLEKQPFELSGGQKQRVAV 155
Cdd:COG4133 71 EDYRR-RLAYLGHADGLKPELTVRENLrfwaaLYGLRADREAID------EALE-AVGLAGLADLPVRQLSAGQKRRVAL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 156 ARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRV 213
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-202 |
5.96e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 143.33 E-value: 5.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTR---FSKEETT--ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIK 76
Cdd:COG4608 7 LLEVRDLKKHFPVRgglFGRTVGVvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 77 DKEISAFRRDhLGFVFQD-FNLLDT-LNVRDNIYLPLVLSKssvelMKSRLKILApklNIENLLEK----------QPFE 144
Cdd:COG4608 87 GRELRPLRRR-MQMVFQDpYASLNPrMTVGDIIAEPLRIHG-----LASKAERRE---RVAELLELvglrpehadrYPHE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH 202
Cdd:COG4608 158 FSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISH 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-224 |
6.84e-41 |
|
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: 139.74 E-value: 6.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEgEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKediTAIKDKEISAF---RRDHLGFV 91
Cdd:cd03297 5 DIEKRLPDFTLKIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRKKINlppQQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 92 FQDFNLLDTLNVRDNIYLPLVLSKSSVelMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEP 171
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRKRNRE--DRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 172 TAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNlNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-223 |
1.56e-40 |
|
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: 139.18 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeisa 82
Cdd:cd03263 1 LQIRNLTKTYKKG----TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 fRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03263 73 -ARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINdSGQTIIMVTHSSLAASH-AKRVLFIKDGVLYH 223
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEAlCDRIAIMSDGKLRC 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
3.97e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 139.23 E-value: 3.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTRfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkei 80
Cdd:COG4525 2 SMLTVRHVSVRYPGG--GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRrdhlGFVFQDFNLLDTLNVRDNIYLPLVLSKssVELMKSR---LKILApKLNIENLLEKQPFELSGGQKQRVAVAR 157
Cdd:COG4525 75 GADR----GVVFQKDALLPWLNVLDNVAFGLRLRG--VPKAERRaraEELLA-LVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502662315 158 ALISQPDLVLADEPTAALDFKNSED----LLNLFEEindSGQTIIMVTHS 203
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQmqelLLDVWQR---TGKGVFLITHS 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
20-219 |
6.06e-40 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 138.30 E-value: 6.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDIT--AIKDKEIsafrRDHLGFVFQDFNL 97
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLI----RQEAGMVFQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 LDTLNVRDNI-YLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK09493 89 FPHLTALENVmFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 177 FKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTHEiGFAEKVASRLIFIDKG 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-224 |
6.90e-40 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 137.79 E-value: 6.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 28 DFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkeiSAFRRDhLGFVFQDFNLLDTLNVRDNI 107
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT-----PPSRRP-VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 108 YL---P-LVLSKSSvelmKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDL 183
Cdd:PRK10771 93 GLglnPgLKLNAAQ----REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 184 LNLFEEINDSGQ-TIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK10771 169 LTLVSQVCQERQlTLLMVSHSlEDAARIAPRSLVVADGRIAWD 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-223 |
7.11e-40 |
|
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: 137.28 E-value: 7.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 22 TALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdkeisafRRDHLGFVFQDFNLLDT- 100
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---------ERKRIGYVPQRRSIDRDf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 -LNVRDNIYLPLV--------LSKSSVELMKSRLKilapKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEP 171
Cdd:cd03235 84 pISVRDVVLMGLYghkglfrrLSKADKAKVDEALE----RVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502662315 172 TAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYH 223
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDlGLVLEYFDRVLLLNRTVVAS 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-221 |
1.68e-39 |
|
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: 144.98 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkEISAFRRdHLGFVFQD 94
Cdd:COG2274 482 RYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRR-QIGVVLQD 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTlNVRDNIylplVLSKSSV---ELMKSrLKIlapkLNIENLLEKQP--FE---------LSGGQKQRVAVARALI 160
Cdd:COG2274 558 VFLFSG-TIRENI----TLGDPDAtdeEIIEA-ARL----AGLHDFIEALPmgYDtvvgeggsnLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEInDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
15-221 |
6.25e-39 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 135.39 E-value: 6.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEK-----PTSGQVLLNKEDITAIKDKEISAFRRdhLG 89
Cdd:cd03260 7 NVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLELRRR--VG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 90 FVFQDFNLLDtLNVRDNIYLPLVL-----SKSSVELMKSRLKILApkLNIENLLEKQPFELSGGQKQRVAVARALISQPD 164
Cdd:cd03260 85 MVFQKPNPFP-GSIYDNVAYGLRLhgiklKEELDERVEEALRKAA--LWDEVKDRLHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 165 LVLADEPTAALDFKNSEDLLNLFEEINDSgQTIIMVTHSSL-AASHAKRVLFIKDGVL 221
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQqAARVADRTAFLLNGRL 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
19-221 |
1.05e-38 |
|
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: 141.82 E-value: 1.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 19 EETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD---F 95
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW----RRQIAWVPQNpylF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NllDTlnVRDNI--YLPlvlsKSSVELMKSRLKilapKLNIENLLEKQP-----------FELSGGQKQRVAVARALISQ 162
Cdd:COG4988 424 A--GT--IRENLrlGRP----DASDEELEAALE----AAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDsGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-202 |
1.14e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 135.74 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTR---FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDK 78
Cdd:COG4167 4 LLEVRNLSKTFKYRtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 eisaFRRDHLGFVFQDFNllDTLNVRDNI----YLPLVLSkssvelmkSRLKILAPKLNIENLLEK----------QPFE 144
Cdd:COG4167 84 ----YRCKHIRMIFQDPN--TSLNPRLNIgqilEEPLRLN--------TDLTAEEREERIFATLRLvgllpehanfYPHM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTH 202
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQeKLGISYIYVSQ 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
15-219 |
1.16e-38 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 137.94 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRDHLGFVFQD 94
Cdd:TIGR02142 4 RFSKRLGDFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTLNVRDNiyLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:TIGR02142 84 ARLFPHLSVRGN--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502662315 175 LDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEfGIPILYVSHSlQEVLRLADRVVVLEDG 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-219 |
1.78e-38 |
|
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: 133.87 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 19 EETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQDFNLL 98
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIGYVPQDVTLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 99 -DTLnvRDNIYLPLVLSkSSVELMKSrlkilAPKLNIENLLEKQP-----------FELSGGQKQRVAVARALISQPDLV 166
Cdd:cd03245 91 yGTL--RDNITLGAPLA-DDERILRA-----AELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 167 LADEPTAALDfKNSEDllNLFEEIND--SGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03245 163 LLDEPTSAMD-MNSEE--RLKERLRQllGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-219 |
3.07e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 135.18 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIF--KTRFskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikDK 78
Cdd:PRK13637 1 MSIKIENLTHIYmeGTPF---EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT---DK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 EIS-AFRRDHLGFVFQ--DFNLLDTLNVRDNIYLP--LVLSKSSVElMKSRLKILAPKLNIENLLEKQPFELSGGQKQRV 153
Cdd:PRK13637 75 KVKlSDIRKKVGLVFQypEYQLFEETIEKDIAFGPinLGLSEEEIE-NRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 154 AVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSmEDVAKLADRIIVMNKG 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-202 |
4.17e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 134.49 E-value: 4.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAI-KDKEISAFRRdHLGFVFQ--DFN 96
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQIRK-KVGLVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK13649 98 LFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180
....*....|....*....|....*.
gi 502662315 177 FKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-219 |
4.78e-38 |
|
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: 132.56 E-value: 4.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISafrRDHLGFVFQDFNLLD 99
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA---RAGIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 TLNVRDNIYLPL-VLSKSSVELMKSRLKILAPKLniENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFK 178
Cdd:cd03224 89 ELTVEENLLLGAyARRRAKRKARLERVYELFPRL--KERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 179 NSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNaRFALEIADRAYVLERG 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-219 |
6.28e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 134.38 E-value: 6.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 13 KTRFskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITA-IKDKEISAFRRdHLGFV 91
Cdd:PRK13634 15 KTPF---ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRK-KVGIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 92 FQ--DFNLLDTLNVRDNIYLPL---VLSKSSVELMKSRLKILApkLNiENLLEKQPFELSGGQKQRVAVARALISQPDLV 166
Cdd:PRK13634 91 FQfpEHQLFEETVEKDICFGPMnfgVSEEDAKQKAREMIELVG--LP-EELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 167 LADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHkEKGLTTVLVTHSmEDAARYADQIVVMHKG 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-221 |
6.93e-38 |
|
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: 130.80 E-value: 6.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL----GDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTlNVRDNIylplvlskssvelmksrlkilapklnienllekqpfeLSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:cd03246 85 DELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502662315 175 LDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
15-219 |
8.75e-38 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 139.13 E-value: 8.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:COG4987 342 RYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL----RRRIAVVPQR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTlNVRDNiyLPLVLSKSSVELMKSRLKilapKLNIENLLEKQP-----------FELSGGQKQRVAVARALISQP 163
Cdd:COG4987 418 PHLFDT-TLREN--LRLARPDATDEELWAALE----RVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEInDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMDRILVLEDG 545
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-224 |
3.88e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.65 E-value: 3.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:PRK13632 16 SYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI----RKKIGIIFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 -FNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTA 173
Cdd:PRK13632 92 pDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502662315 174 ALDFKNSEDLLNLFEEINDSG-QTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK13632 172 MLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQ 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-220 |
4.84e-37 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 131.08 E-value: 4.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKifktRFSKEETtaLVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKD----- 77
Cdd:COG4598 9 LEVRDLHK----SFGDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 -----KEISAFRRdHLGFVFQDFNLLDTLNVRDNIYL-PL-VLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQK 150
Cdd:COG4598 83 vpadrRQLQRIRT-RLGMVFQSFNLWSHMTVLENVIEaPVhVLGRPKAEAIERAEALLA-KVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGV 220
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEmGFARDVSSHVVFLHQGR 231
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-202 |
5.65e-37 |
|
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: 130.28 E-value: 5.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLnkeditaiKDKEISAFRRDHLgFVFQDFNLLDTLNV 103
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL--------EGKQITEPGPDRM-VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 104 RDNIYLPL--VLSKSSVElmkSRLKILAPKLNIENLLE---KQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFK 178
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKS---ERRAIVEEHIALVGLTEaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180
....*....|....*....|....*
gi 502662315 179 NSEDLLNLFEEI-NDSGQTIIMVTH 202
Cdd:TIGR01184 149 TRGNLQEELMQIwEEHRVTVLMVTH 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-220 |
6.20e-37 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.92 E-value: 6.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkEIS 81
Cdd:PRK09452 14 LVELRGISKSF------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:PRK09452 83 AENR-HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 162 QPDLVLADEPTAALDFK-----NSEdLLNLFEEIndsGQTIIMVTHSSLAA-SHAKRVLFIKDGV 220
Cdd:PRK09452 162 KPKVLLLDESLSALDYKlrkqmQNE-LKALQRKL---GITFVFVTHDQEEAlTMSDRIVVMRDGR 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-221 |
6.32e-37 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 133.29 E-value: 6.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkEI 80
Cdd:PRK10851 1 MSIEIANIKKSF------GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAfRRDHLGFVFQDFNLLDTLNVRDNIYLPL-VL---SKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVA 156
Cdd:PRK10851 70 HA-RDRKVGFVFQHYALFRHMTVFDNIAFGLtVLprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 157 RALISQPDLVLADEPTAALDFKNSEDL----LNLFEEINdsgQTIIMVTHSSLAASH-AKRVLFIKDGVL 221
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELrrwlRQLHEELK---FTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
28-219 |
1.40e-36 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 128.83 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 28 DFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdkeiSAFRRDHLGFVFQDFNLLDTLNVRDNI 107
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG------LAPYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 108 YLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLF 187
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....
gi 502662315 188 EEINDSGQ-TIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:TIGR01277 172 KQLCSERQrTLLMVTHHlSDARAIASQIAVVSQG 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-224 |
4.06e-36 |
|
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: 129.09 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVL------LNKEDITAIk 76
Cdd:TIGR04520 1 IEVENVSF----SYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvdgldtLDEENLWEI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 77 dkeisafrRDHLGFVFQ--DFNLLDTLnVRD-------NIYLPLvlskssvELMKSRLKILAPKLNIENLLEKQPFELSG 147
Cdd:TIGR04520 76 --------RKKVGMVFQnpDNQFVGAT-VEDdvafgleNLGVPR-------EEMRKRVDEALKLVGMEDFRDREPHLLSG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 148 GQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-203 |
6.43e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 128.28 E-value: 6.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISA 82
Cdd:COG1101 2 LELKNLSKTFNPG-TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FrrdhLGFVFQDfNLLDT---LNVRDNI----------YLPLVLSKSSVELMKSRLKILapKLNIENLLEKQPFELSGGQ 149
Cdd:COG1101 81 Y----IGRVFQD-PMMGTapsMTIEENLalayrrgkrrGLRRGLTKKRRELFRELLATL--GLGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 150 KQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS 203
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHN 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-228 |
2.67e-35 |
|
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: 125.56 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKifktRFSKEETT--ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLnkEDITAIKDKe 79
Cdd:cd03266 1 MITADALTK----RFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV--DGFDVVKEP- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 80 ISAFRRdhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:cd03266 74 AEARRR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLyhqLYRG 228
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRV---VYEG 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-219 |
5.21e-35 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 127.61 E-value: 5.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 39 IMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkEISAFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSV 118
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLR-HINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 119 ELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTI 197
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITF 154
|
170 180
....*....|....*....|...
gi 502662315 198 IMVTH-SSLAASHAKRVLFIKDG 219
Cdd:TIGR01187 155 VFVTHdQEEAMTMSDRIAIMRKG 177
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
9.28e-35 |
|
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: 125.15 E-value: 9.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkei 80
Cdd:COG0411 3 PLLEVRGLTKRFG------GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 sAFRRDHLGFV--FQDFNLLDTLNVRDNIYLPLVL-SKSSVELMKSRLK---------------ILApKLNIENLLEKQP 142
Cdd:COG0411 73 -PHRIARLGIArtFQNPRLFPELTVLENVLVAAHArLGRGLLAALLRLPrarreereareraeeLLE-RVGLADRADEPA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 143 FELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIND-SGQTIIMVTHS-SLAASHAKRVL 214
Cdd:COG0411 151 GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDmDLVMGLADRIV 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-219 |
2.37e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 129.90 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFS-KEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQ 93
Cdd:COG1132 346 SFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL----RRQIGVVPQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 94 DFNLLDTlNVRDNIylplVLSKSSV---ELMKSrlkilAPKLNIENLLEKQPF-----------ELSGGQKQRVAVARAL 159
Cdd:COG1132 422 DTFLFSG-TIRENI----RYGRPDAtdeEVEEA-----AKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARAL 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINdSGQTIIMVTH--SSLAasHAKRVLFIKDG 219
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHrlSTIR--NADRILVLDDG 550
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-224 |
2.89e-34 |
|
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: 122.69 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYiAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeisa 82
Cdd:cd03264 1 LQLENLTKRYGKK------RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 fRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03264 70 -LRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINdSGQTIIMVTH-SSLAASHAKRVLFIKDGVLYHQ 224
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHiVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-219 |
4.25e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 123.63 E-value: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkeisa 82
Cdd:PRK11247 13 LLLNAVSKRYGER------TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDHLGFVFQDFNLLDTLNVRDNIYLPLvlsksSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:PRK11247 80 --REDTRLMFQDARLLPWKKVIDNVGLGL-----KGQWRDAALQALA-AVGLADRANEWPAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDvSEAVAMADRVLLIEEG 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-224 |
4.38e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 123.54 E-value: 4.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKifktRFSKEETtaLVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDK--EI 80
Cdd:PRK10619 6 LNVIDLHK----RYGEHEV--LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFR-------RDHLGFVFQDFNLLDTLNVRDNIY-LPL-VLSKSSVELMKSRLKILApKLNI-ENLLEKQPFELSGGQK 150
Cdd:PRK10619 80 KVADknqlrllRTRLTMVFQHFNLWSHMTVLENVMeAPIqVLGLSKQEARERAVKYLA-KVGIdERAQGKYPVHLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASH-AKRVLFIKDGVLYHQ 224
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
3-223 |
6.12e-34 |
|
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: 121.12 E-value: 6.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILS--TLEKPTSGQVLLNKeditaiKDKEI 80
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING------RPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKssvelmksrlkilapklnienllekqpfeLSGGQKQRVAVARALI 160
Cdd:cd03213 78 RSFRK-IIGYVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH--SSLAASHAKRVLFIKDG-VLYH 223
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpSSEIFELFDKLLLLSQGrVIYF 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-202 |
8.58e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.44 E-value: 8.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKifktRFSKeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaIKDkeI 80
Cdd:COG1129 3 PLLEMRGISK----SFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-FRS--P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSV---ELMKSR-LKILApKLNIENLLEKQPFELSGGQKQRVAVA 156
Cdd:COG1129 74 RDAQAAGIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRaRELLA-RLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502662315 157 RALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-219 |
3.27e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 122.15 E-value: 3.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 21 TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAI-KDKEISAFRRDhLGFVFQ--DFNL 97
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIKPVRKK-VGVVFQfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 LDTLNVRDNIYLP--LVLSKSSVElmksrlKILAPKLNIENL----LEKQPFELSGGQKQRVAVARALISQPDLVLADEP 171
Cdd:PRK13643 98 FEETVLKDVAFGPqnFGIPKEKAE------KIAAEKLEMVGLadefWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502662315 172 TAALDFKNSEDLLNLFEEINDSGQTIIMVTH-SSLAASHAKRVLFIKDG 219
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQTVVLVTHlMDDVADYADYVYLLEKG 220
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-222 |
4.87e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.51 E-value: 4.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTR------FSKEETTALVD-IDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDIT 73
Cdd:PRK15079 7 VLLEVADLKVHFDIKdgkqwfWQPPKTLKAVDgVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 74 AIKDKEISAFRRDhLGFVFQDfnLLDTLNVR----DNIYLPLV-----LSKSSVelmKSRLKILAPKLNI-ENLLEKQPF 143
Cdd:PRK15079 87 GMKDDEWRAVRSD-IQMIFQD--PLASLNPRmtigEIIAEPLRtyhpkLSRQEV---KDRVKAMMLKVGLlPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 144 ELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASH-AKRVLfikdgVL 221
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQrEMGLSLIFIAHDLAVVKHiSDRVL-----VM 235
|
.
gi 502662315 222 Y 222
Cdd:PRK15079 236 Y 236
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-232 |
5.31e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 121.07 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTR---FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDK 78
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 EISAFRRDhLGFVFQD----FNLLDTlnVRDNIYLPL--VLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQR 152
Cdd:TIGR02769 82 QRRAFRRD-VQLVFQDspsaVNPRMT--VRQIIGEPLrhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 153 VAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQLYRGEK 230
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDlRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
..
gi 502662315 231 SS 232
Cdd:TIGR02769 239 LS 240
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-224 |
6.15e-33 |
|
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: 120.19 E-value: 6.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVL------LNKEDITA 74
Cdd:COG1119 2 PLLELRNV------TVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlfgerRGGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 75 IkdkeisafrRDHLGFVFQDF--NLLDTLNVRDniylpLVLS--KSSVEL-------MKSRLKILAPKLNIENLLEKQPF 143
Cdd:COG1119 76 L---------RKRIGLVSPALqlRFPRDETVLD-----VVLSgfFDSIGLyreptdeQRERARELLELLGLAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 144 ELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQ-TIIMVTHsslaasHA-------KRVLF 215
Cdd:COG1119 142 TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTH------HVeeippgiTHVLL 215
|
....*....
gi 502662315 216 IKDGVLYHQ 224
Cdd:COG1119 216 LKDGRVVAA 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-176 |
6.72e-33 |
|
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: 125.18 E-value: 6.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTR---FSK--EETTALVDIDFGVEEGEYIAIMGESGSGKTTL-LNILSTLekPTSGQVLLNKEDITAI 75
Cdd:COG4172 275 LLEARDLKVWFPIKrglFRRtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 76 KDKEISAFRRdHLGFVFQD-FNLLDT-LNVRDNIYLPlvlskssvelmksrLKILAPKLNIE-----------------N 136
Cdd:COG4172 353 SRRALRPLRR-RMQVVFQDpFGSLSPrMTVGQIIAEG--------------LRVHGPGLSAAerrarvaealeevgldpA 417
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502662315 137 LLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:COG4172 418 ARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-248 |
8.38e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.02 E-value: 8.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRFskeettALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkEIS 81
Cdd:PRK11607 19 LLEIRNLTKSFDGQH------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:PRK11607 88 PYQRP-INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 162 QPDLVLADEPTAALDFKNSEDL-LNLFEEINDSGQTIIMVTH-SSLAASHAKRVLFIKDGVLYH-----QLYrgEKSSTE 234
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQigepeEIY--EHPTTR 244
|
250
....*....|....
gi 502662315 235 FAKEITLSMTAFLG 248
Cdd:PRK11607 245 YSAEFIGSVNVFEG 258
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-202 |
9.60e-33 |
|
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: 119.08 E-value: 9.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFK--TRFSKEeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKE----DITAI 75
Cdd:COG4778 4 LLEVENLSKTFTlhLQGGKR-LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 76 KDKEISAFRRDHLGFVFQdFnlldtLNV------RDNIYLPLVLSKSSVELMKSRLKILAPKLNI-ENLLEKQPFELSGG 148
Cdd:COG4778 83 SPREILALRRRTIGYVSQ-F-----LRViprvsaLDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502662315 149 QKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:COG4778 157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFH 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-221 |
1.19e-32 |
|
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: 124.80 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKT-TLLNILSTLEKP---TSGQVLLNKEDITAIKD 77
Cdd:COG4172 6 LLSVEDLSVAFGQ--GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEISAFRRDHLGFVFQD----FNLLDTlnVRDNIYLPLVLSKS---------SVELMKsRLKILAPklniENLLEKQPFE 144
Cdd:COG4172 84 RELRRIRGNRIAMIFQEpmtsLNPLHT--IGKQIAEVLRLHRGlsgaaararALELLE-RVGIPDP----ERRLDAYPHQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-221 |
1.78e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 119.93 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITA-IKDKEISAFRRDhLGFVFQ--DFN 96
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKKLRKK-VSLVFQfpEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK13641 98 LFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502662315 177 FKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNmDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-224 |
1.89e-32 |
|
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: 118.74 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItAIKDKeisAFRRDHLGFVFQD 94
Cdd:cd03252 9 RYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDL-ALADP---AWLRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 fNLLDTLNVRDNIYL-----PLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLAD 169
Cdd:cd03252 85 -NVLFNRSIRDNIALadpgmSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 170 EPTAALDFKNSEDLLNLFEEINDsGQTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-214 |
4.89e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.81 E-value: 4.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEKP--TSGQVLLNKEDITAIKdkeisAFRRdHLGFVFQDFNLLDTLN 102
Cdd:COG4136 19 PLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP-----AEQR-RIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIY--LPLVLSKSsvelmKSRLKILAP--KLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFK 178
Cdd:COG4136 93 VGENLAfaLPPTIGRA-----QRRARVEQAleEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 502662315 179 NSEDLLNL-FEEINDSGQTIIMVTHSSLAASHAKRVL 214
Cdd:COG4136 168 LRAQFREFvFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-219 |
6.07e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.26 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 21 TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAfrRDHLGFVFQdfnlldt 100
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEV--RKTVGIVFQ------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 lNVRDNIYLPLV------------LSKSSVElmkSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLA 168
Cdd:PRK13639 86 -NPDDQLFAPTVeedvafgplnlgLSKEEVE---KRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502662315 169 DEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK13639 162 DEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvDLVPVYADKVYVMSDG 213
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
26-207 |
7.01e-32 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 120.13 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISafrrdhLGFVFQDFNLLDTLNVRD 105
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------VGMVFQSYALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 106 NIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEP----TAALDFKNSE 181
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPlsnlDAALRVQMRI 174
|
170 180
....*....|....*....|....*.
gi 502662315 182 DLLNLFEEIndsGQTIIMVTHSSLAA 207
Cdd:PRK11000 175 EISRLHKRL---GRTMIYVTHDQVEA 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-220 |
1.02e-31 |
|
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: 116.87 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 17 SKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItaiKDKEISAFRRdHLGFVFQDFN 96
Cdd:cd03249 12 SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLRS-QIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTlNVRDNIYLPLvlSKSSVELMKSRLKilapKLNIENLLEKQP-----------FELSGGQKQRVAVARALISQPDL 165
Cdd:cd03249 88 LFDG-TIAENIRYGK--PDATDEEVEEAAK----KANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502662315 166 VLADEPTAALDfKNSEDLLNlfEEIND--SGQTIIMVTHSSLAASHAKRVLFIKDGV 220
Cdd:cd03249 161 LLLDEATSALD-AESEKLVQ--EALDRamKGRTTIVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-176 |
4.27e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 115.13 E-value: 4.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkei 80
Cdd:COG1137 2 MTLEAENLVKSYGKR------TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRDHLGF--------VFQDfnlldtLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQR 152
Cdd:COG1137 71 PMHKRARLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
|
170 180
....*....|....*....|....
gi 502662315 153 VAVARALISQPDLVLADEPTAALD 176
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVD 168
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-219 |
5.48e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.55 E-value: 5.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKT---RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDK 78
Cdd:PRK10419 3 LLNVSGLSHHYAHgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 EISAFRRDhLGFVFQD----FNLLDTlnVRDNIYLPL--VLSKSSVELMKSRLKIL-APKLNIEnLLEKQPFELSGGQKQ 151
Cdd:PRK10419 83 QRKAFRRD-IQMVFQDsisaVNPRKT--VREIIREPLrhLLSLDKAERLARASEMLrAVDLDDS-VLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 152 RVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIND-SGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDlRLVERFCQRVMVMDNG 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
15-219 |
5.66e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 120.74 E-value: 5.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeiSAFRRDHLGFVFQD 94
Cdd:TIGR03375 472 AYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQID----PADLRRNIGYVPQD 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLL-DTLnvRDNIYL--PLVlskSSVELMKSrlkilAPKLNIENLLEKQP--FE---------LSGGQKQRVAVARALI 160
Cdd:TIGR03375 548 PRLFyGTL--RDNIALgaPYA---DDEEILRA-----AELAGVTEFVRRHPdgLDmqigergrsLSGGQRQAVALARALL 617
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 161 SQPDLVLADEPTAALDfKNSEDLL--NLFEEIndSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:TIGR03375 618 RDPPILLLDEPTSAMD-NRSEERFkdRLKRWL--AGKTLVLVTHRTSLLDLVDRIIVMDNG 675
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-224 |
7.48e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.65 E-value: 7.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITA-IKDKEISAFRRDhLGFVFQ--DFN 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRPVRKR-IGMVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTLNVRDNIYLPLVLsKSSVELMKSRLKILAPKLNIE-NLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:PRK13646 98 LFEDTVEREIIFGPKNF-KMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502662315 176 DFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSIVSQ 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-219 |
7.99e-31 |
|
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: 112.79 E-value: 7.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeisafRRDHLGFVFQDF 95
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLLDTlNVRDNIYLPLvlskssvelmksrlkilapklnienllekqpfelSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:cd03247 85 YLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502662315 176 DFKNSEDLLNL-FEEINDsgQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03247 130 DPITERQLLSLiFEVLKD--KTLIWITHHLTGIEHMDKILFLENG 172
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-202 |
8.17e-31 |
|
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: 114.18 E-value: 8.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikDKEISA 82
Cdd:cd03218 1 LRAENLSKRYGKR------KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT---KLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03218 72 RARLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-222 |
9.70e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.11 E-value: 9.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKkifkTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQV-----LLNKEDITAIk 76
Cdd:PRK13635 5 IIRVEHIS----FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmVLSEETVWDV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 77 dkeisafrRDHLGFVFQ--DFNLLDTlNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVA 154
Cdd:PRK13635 80 --------RRQVGMVFQnpDNQFVGA-TVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 155 VARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIND-SGQTIIMVTHSSLAASHAKRVLFIKDGVLY 222
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
1.27e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 116.10 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQV----LLNKEDITAIKD 77
Cdd:PRK13631 21 ILRVKNLYCVFDEK-QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 ------KEISAFR--RDHLGFVFQ--DFNLLDTLNVRDNIYLPLVLSKSSVElMKSRLKILAPKLNI-ENLLEKQPFELS 146
Cdd:PRK13631 100 itnpysKKIKNFKelRRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 147 GGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSslaashAKRVLFIKDGVL 221
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT------MEHVLEVADEVI 247
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
20-200 |
1.30e-30 |
|
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: 113.92 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISafrRDHLGFVFQDFNLLD 99
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA---RLGIGYVPEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 TLNVRDNIYLPLVLSKSSVELMKSRLKILA--PKLniENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDF 177
Cdd:COG0410 92 SLTVEENLLLGAYARRDRAEVRADLERVYElfPRL--KERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAP 169
|
170 180
....*....|....*....|...
gi 502662315 178 KNSEDLLNLFEEINDSGQTIIMV 200
Cdd:COG0410 170 LIVEEIFEIIRRLNREGVTILLV 192
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-220 |
1.92e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.45 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLkkifkTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsa 82
Cdd:PRK13647 5 IEVEDL-----HFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDHLGFVFQD-FNLLDTLNVRDNI-YLPLVLSKSSVELmKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:PRK13647 78 --RSKVGLVFQDpDDQVFSSTVWDDVaFGPVNMGLDKDEV-ERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGV 220
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-222 |
1.97e-30 |
|
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: 112.76 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTrfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLlnkeditaIKDKEISA 82
Cdd:cd03269 1 LEVENVTKRFGR------VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL--------FDGKPLDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDHLGFVFQDFNLLDTLNVRDN-IYLPLV--LSKSSVelmKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:cd03269 67 AARNRIGYLPEERGLYPKMKVIDQlVYLAQLkgLKKEEA---RRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG--VLY 222
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGraVLY 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-221 |
2.00e-30 |
|
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: 110.98 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEisA 82
Cdd:cd03216 1 LELRGITKRF------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 fRRDHLGFVFQdfnlldtlnvrdniylplvlskssvelmksrlkilapklnienllekqpfeLSGGQKQRVAVARALISQ 162
Cdd:cd03216 73 -RRAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-187 |
4.22e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 114.68 E-value: 4.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTR---FSKEETT-ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDiTAIKD 77
Cdd:PRK11308 5 LLQAIDLKKHYPVKrglFKPERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD-LLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEISAFRRDHLGFVFQdfNLLDTLNVRDNI--YL--PLV----LSKSsvelmKSRLKILApklnienLLEK--------- 140
Cdd:PRK11308 84 PEAQKLLRQKIQIVFQ--NPYGSLNPRKKVgqILeePLLintsLSAA-----ERREKALA-------MMAKvglrpehyd 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502662315 141 -QPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLF 187
Cdd:PRK11308 150 rYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLM 197
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-219 |
7.32e-30 |
|
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: 111.94 E-value: 7.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeISAFRRdHLGFVFQD---FNllDT 100
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRR-AIGVVPQDtvlFN--DT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 lnVRDNI-YLPLvlSKSSVELMKSrlkilAPKLNIENLLEKQPF-----------ELSGGQKQRVAVARALISQPDLVLA 168
Cdd:cd03253 91 --IGYNIrYGRP--DATDEEVIEA-----AKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502662315 169 DEPTAALDfKNSEDllNLFEEIND--SGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03253 162 DEATSALD-THTER--EIQAALRDvsKGRTTIVIAHRLSTIVNADKIIVLKDG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-219 |
1.52e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.13 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKkiFKTRFSKEETTaLVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIs 81
Cdd:PRK13650 4 IIEVKNLT--FKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 afrRDHLGFVFQD-FNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:PRK13650 80 ---RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQ-TIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVALSDRVLVMKNG 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-214 |
2.71e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 115.46 E-value: 2.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeiSAFRRDHLGFVFQDFNLLD 99
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 TlNVRDNIYLplVLSKSSVELMKSRLK-------ILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPT 172
Cdd:TIGR02857 410 G-TIAENIRL--ARPDASDAEIREALEragldefVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 173 AALDFKNSEDLLNLFEEINdSGQTIIMVTHSSLAASHAKRVL 214
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAALADRIV 527
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-214 |
3.38e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKkifktrFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEI 80
Cdd:PRK10247 6 PLLQLQNVG------YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 safrRDHLGFVFQDFNLL-DTlnVRDNIYLPLVLSKSSVElMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:PRK10247 80 ----RQQVSYCAQTPTLFgDT--VYDNLIFPWQIRNQQPD-PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASHAKRVL 214
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEINHADKVI 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-214 |
8.12e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.70 E-value: 8.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 22 TALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVllnkeditaikdkEISAFRRdhLGFVFQDFNLLDTL 101
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------------RRAGGAR--VAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 102 --NVRDNIYL-----------PLVLSKSSVELMKSRLKILApklnienlLEKQPF-ELSGGQKQRVAVARALISQPDLVL 167
Cdd:NF040873 71 plTVRDLVAMgrwarrglwrrLTRDDRAAVDDALERVGLAD--------LAGRQLgELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502662315 168 ADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVL 214
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
15-243 |
8.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.84 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:PRK13648 16 QYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 -FNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTA 173
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 174 ALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASHAKRVLFIKDGVLY-----HQLYRGEKSSTEFAKEITLSM 243
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVMNKGTVYkegtpTEIFDHAEELTRIGLDLPFPI 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-176 |
8.55e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.43 E-value: 8.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIF-----------KTRFSKE---ETTALV----DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQ 64
Cdd:PRK10070 5 LEIKNLYKIFgehpqrafkyiEQGLSKEqilEKTGLSlgvkDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 65 VLLNKEDITAIKDKEISAFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFE 144
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
|
170 180 190
....*....|....*....|....*....|..
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-219 |
1.14e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 19 EETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDK-EIsafrRDHLGFVFQ--DF 95
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDI----RNKAGMVFQnpDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLLDTLNVRDNIYLPLVLSKSSVELmKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:PRK13633 97 QIVATIVEEDVAFGPENLGIPPEEI-RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502662315 176 DFKNSEDLLNLFEEIND-SGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PRK13633 176 DPSGRREVVNTIKELNKkYGITIILITHYMEEAVEADRIIVMDSG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-203 |
1.28e-28 |
|
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: 113.22 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFrrdhLGFVFQDFNLLDTlN 102
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYL--PLVlskSSVELMKsrlkiLAPKLNIENLLEKQP-----------FELSGGQKQRVAVARALISQPDLVLAD 169
Cdd:TIGR02868 425 VRENLRLarPDA---TDEELWA-----ALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLD 496
|
170 180 190
....*....|....*....|....*....|....*
gi 502662315 170 EPTAALDFKNSEDLL-NLFEEinDSGQTIIMVTHS 203
Cdd:TIGR02868 497 EPTEHLDAETADELLeDLLAA--LSGRTVVLITHH 529
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-203 |
1.97e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 110.73 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 38 AIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRDHLGFVFQDFNLLDTLNVRDNiyLPLVLSKSS 117
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGN--LRYGMAKSM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 118 VELMKSRLKILApklnIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLN----LFEEINds 193
Cdd:PRK11144 106 VAQFDKIVALLG----IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPylerLAREIN-- 179
|
170
....*....|
gi 502662315 194 gQTIIMVTHS 203
Cdd:PRK11144 180 -IPILYVSHS 188
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-213 |
2.37e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.59 E-value: 2.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLL---NILSTLEkP---TSGQVLLNKEDITAiKDKEISAFRRdHLGFVFQDFN 96
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLI-PgarVEGEILLDGEDIYD-PDVDVVELRR-RVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLdTLNVRDNIYLPL----VLSKSSV-ELMKSRLKILApkL--NIENLLEKQPFELSGGQKQRVAVARALISQPDLVLAD 169
Cdd:COG1117 103 PF-PKSIYDNVAYGLrlhgIKSKSELdEIVEESLRKAA--LwdEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502662315 170 EPTAALDFKNS---EDLLN-LFEEIndsgqTIIMVTHSslaASHAKRV 213
Cdd:COG1117 180 EPTSALDPISTakiEELILeLKKDY-----TIVIVTHN---MQQAARV 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-238 |
2.76e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.56 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTL----EKPTSGQVLLNKEDITAIKD 77
Cdd:PRK09984 4 IIRVEKLAKTF------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQREGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEISAFRRDHLGFVFQDFNLLDTLNVRDNIylpLVLSKSSVELMKSRLKILAP-----------KLNIENLLEKQPFELS 146
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRLSVLENV---LIGALGSTPFWRTCFSWFTReqkqralqaltRVGMVHFAHQRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 147 GGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDGvlyHQ 224
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQvDYALRYCERIVALRQG---HV 231
|
250
....*....|....
gi 502662315 225 LYRGekSSTEFAKE 238
Cdd:PRK09984 232 FYDG--SSQQFDNE 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-202 |
3.78e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 3.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTrfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaIKDkei 80
Cdd:COG3845 4 PALELRGITKRFGG------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-IRS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRDH-LGFVFQDFNLLDTLNVRDNIylplVLSKSSVELMKSRLKILAPKlnIENLLEKQPFE---------LSGGQK 150
Cdd:COG3845 74 PRDAIALgIGMVHQHFMLVPNLTVAENI----VLGLEPTKGGRLDRKAARAR--IRELSERYGLDvdpdakvedLSVGEQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-176 |
4.14e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.81 E-value: 4.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 8 LKKIFKtRFSKeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDIT--AIKDKEISafrr 85
Cdd:PRK11432 9 LKNITK-RFGS--NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrSIQQRDIC---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 86 dhlgFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDL 165
Cdd:PRK11432 82 ----MVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170
....*....|.
gi 502662315 166 VLADEPTAALD 176
Cdd:PRK11432 158 LLFDEPLSNLD 168
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-228 |
4.84e-28 |
|
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: 107.03 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfSKE----------------ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVL 66
Cdd:cd03267 1 IEVSNLSKSYRVY-SKEpgligslkslfkrkyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 67 LNKEditaIKDKEISAFRRdHLGFVF-QDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFEL 145
Cdd:cd03267 80 VAGL----VPWKRRKKFLR-RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 146 SGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDGvlyH 223
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrERGTTVLLTSHYmKDIEALARRVLVIDKG---R 231
|
....*
gi 502662315 224 QLYRG 228
Cdd:cd03267 232 LLYDG 236
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-221 |
5.45e-28 |
|
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: 106.69 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdKEISA 82
Cdd:cd03265 1 IEVENLVKKY------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPRE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ 162
Cdd:cd03265 71 VRR-RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHSSLAASH-AKRVLFIKDGVL 221
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQlCDRVAIIDHGRI 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-219 |
5.48e-28 |
|
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: 106.93 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FS-KEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:cd03254 10 FSyDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL----RSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTlNVRDNIYLplvlskSSVELMKSRLKILAPKLNIENLLEKQP-----------FELSGGQKQRVAVARALISQP 163
Cdd:cd03254 86 TFLFSG-TIMENIRL------GRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEINDsGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
23-202 |
1.17e-27 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 106.71 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkdkeiSAFRrdhlGFVFQDFNLLDTLN 102
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-----GAER----GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|.
gi 502662315 183 LLNLFEEI-NDSGQTIIMVTH 202
Cdd:PRK11248 167 MQTLLLKLwQETGKQVLLITH 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-239 |
1.42e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 1.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTL-----EKPTSGQVLLNKEDITAIkd 77
Cdd:PRK14247 4 IEIRDLKVSFG------QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 kEISAFRRdHLGFVFQDFNLLDTLNVRDNIYLPLVLS---KSSVELmKSRLKILAPKLN----IENLLEKQPFELSGGQK 150
Cdd:PRK14247 76 -DVIELRR-RVQMVFQIPNPIPNLSIFENVALGLKLNrlvKSKKEL-QERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSgQTIIMVTHSSLAASHakrvlfIKDGVLYhqLYRGEK 230
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAAR------ISDYVAF--LYKGQI 223
|
....*....
gi 502662315 231 SSTEFAKEI 239
Cdd:PRK14247 224 VEWGPTREV 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-224 |
1.60e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.25 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAfrrdHLGFVFQDFNLLD 99
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR----RLALLPQHHLTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 TLNVRDNI------YLPL--VLSKSSVELMKSRLKilapKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEP 171
Cdd:PRK11231 90 GITVRELVaygrspWLSLwgRLSAEDNARVNQAME----QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502662315 172 TAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAAS-HAKRVLFIKDGVLYHQ 224
Cdd:PRK11231 166 TTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQ 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-202 |
2.18e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 107.50 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKT-TLLNILSTLEKP--TSGQVLLNKEDITAIKDK 78
Cdd:PRK09473 12 LLDVKDLRVTFST--PDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 EISAFRRDHLGFVFQDfnLLDTLN----VRDNIYLPLVLSK--SSVELMKSRLKIL-APKL-NIENLLEKQPFELSGGQK 150
Cdd:PRK09473 90 ELNKLRAEQISMIFQD--PMTSLNpymrVGEQLMEVLMLHKgmSKAEAFEESVRMLdAVKMpEARKRMKMYPHEFSGGMR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQT-IIMVTH 202
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITH 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-178 |
2.97e-27 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 107.62 E-value: 2.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 21 TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEisafrRDhLGFVFQDFNLLDT 100
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD-IAMVFQNYALYPH 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 101 LNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFK 178
Cdd:PRK11650 91 MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-201 |
8.00e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.49 E-value: 8.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTR---FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLlnkeditaIKD 77
Cdd:PRK15112 3 TLLEVRNLSKTFRYRtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL--------IDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEIS----AFRRDHLGFVFQDFNllDTLNVRDNIY----LPLVLSkssVEL-MKSRLKILAPKLNIENLLEKQ----PFE 144
Cdd:PRK15112 75 HPLHfgdySYRSQRIRMIFQDPS--TSLNPRQRISqildFPLRLN---TDLePEQREKQIIETLRQVGLLPDHasyyPHM 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVT 201
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVT 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-219 |
2.18e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 107.14 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkDKEisAFRRdHLGFVFQDFNLLD-Tln 102
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-DRE--ELGR-HIGYLPQDVELFDgT-- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIylplvlskssvelmkSRLK-------ILAPKL-NIENLLEKQP-----------FELSGGQKQRVAVARALISQP 163
Cdd:COG4618 422 IAENI---------------ARFGdadpekvVAAAKLaGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-221 |
6.97e-26 |
|
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: 100.75 E-value: 6.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdKEISA 82
Cdd:cd03268 1 LKTNDLTKTYGKK------RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ----KNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRdhLGFVFQDFNLLDTLNVRDNIYLplvlskssvelmKSRLKILaPKLNIENLLE--------KQPF-ELSGGQKQRV 153
Cdd:cd03268 71 LRR--IGALIEAPGFYPNLTARENLRL------------LARLLGI-RKKRIDEVLDvvglkdsaKKKVkGFSLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 154 AVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIimvthssLAASH--------AKRVLFIKDGVL 221
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITV-------LISSHllseiqkvADRIGIINKGKL 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-219 |
8.73e-26 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.54 E-value: 8.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:PRK11701 6 LLSVRGLTKLYGPR------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHL-----GFVFQdfNLLDTLNVR----DNIYLPLV-----------------LSKssVELMKSRlkilapklnie 135
Cdd:PRK11701 80 EAERRRLlrtewGFVHQ--HPRDGLRMQvsagGNIGERLMavgarhygdiratagdwLER--VEIDAAR----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 136 nlLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEE-INDSGQTIIMVTHsSLAASH--AKR 212
Cdd:PRK11701 145 --IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTH-DLAVARllAHR 221
|
....*..
gi 502662315 213 VLFIKDG 219
Cdd:PRK11701 222 LLVMKQG 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-221 |
1.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 101.62 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 13 KTRFskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITA--IKDKEISAFRRDhLGF 90
Cdd:PRK13645 19 KTPF---EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLRKE-IGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 91 VFQ--DFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLA 168
Cdd:PRK13645 95 VFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502662315 169 DEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHsslaasHAKRVLFIKDGVL 221
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTH------NMDQVLRIADEVI 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-219 |
1.97e-25 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 100.00 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDitaIKDKEISAFRRdHLGFVFQD 94
Cdd:cd03251 9 RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHD---VRDYTLASLRR-QIGLVSQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTlNVRDNI-YLPLVLSKSSVElmkSRLKILAPKLNIENL-------LEKQPFELSGGQKQRVAVARALISQPDLV 166
Cdd:cd03251 85 VFLFND-TVAENIaYGRPGATREEVE---EAARAANAHEFIMELpegydtvIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502662315 167 LADEPTAALDfKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03251 161 ILDEATSALD-TESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDG 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-201 |
2.47e-25 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 98.27 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdKEISAFRRDHLGFVFQD---FNLLDTLN 102
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR---RSPRDAIRAGIAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPLVLSkssvelmksrlkilapklnienllekqpfelsGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:cd03215 95 VAENIALSSLLS--------------------------------GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170
....*....|....*....
gi 502662315 183 LLNLFEEINDSGQTIIMVT 201
Cdd:cd03215 143 IYRLIRELADAGKAVLLIS 161
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-222 |
1.07e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.16 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 4 EVKHLKKIFKTR-------------FS--KEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLN 68
Cdd:COG4586 3 EVENLSKTYRVYekepglkgalkglFRreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 69 KEDITaikdKEISAFRRdHLGFVF-------QDFNLLDTLNVRDNIYlplvlsKSSVELMKSRLKILAPKLNIENLLEKQ 141
Cdd:COG4586 83 GYVPF----KRRKEFAR-RIGVVFgqrsqlwWDLPAIDSFRLLKAIY------RIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 142 PFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVThsslaaSH--------AKRV 213
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLT------SHdmddiealCDRV 225
|
250
....*....|
gi 502662315 214 LFIKDG-VLY 222
Cdd:COG4586 226 IVIDHGrIIY 235
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-202 |
1.68e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 98.68 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRdHLGFVFQD 94
Cdd:PRK11831 14 SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK-RMSMLFQS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLDTLNVRDNIYLPL-VLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTA 173
Cdd:PRK11831 93 GALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190
....*....|....*....|....*....|
gi 502662315 174 ALDFKNSEDLLNLFEEINDS-GQTIIMVTH 202
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSAlGVTCVVVSH 202
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
2.54e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 98.34 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEettALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:PRK13652 3 LIETRDLCYSYSG--SKE---ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFrrdhLGFVFQ--DFNLLDTLNVRDNIYLPLVLSKSSvELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:PRK13652 78 KF----VGLVFQnpDDQIFSPTVEQDIAFGPINLGLDE-ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQlDLVPEMADYIYVMDKG 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
20-172 |
4.21e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 96.44 E-value: 4.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeisAFRRDH--LGFVFQDFNL 97
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP-----PHERARagIAYVPQGREI 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 98 LDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLniENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPT 172
Cdd:TIGR03410 87 FPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVL--KEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-202 |
7.96e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 7.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKeDITaikdkeisafrrdhLGFVFQDFNLLDTLNVRD 105
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR--------------IGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 106 NIY---------------LPLVLSKSSVELMK-----------------SRLKILAPKLNIENLLEKQPF-ELSGGQKQR 152
Cdd:COG0488 81 TVLdgdaelraleaeleeLEAKLAEPDEDLERlaelqeefealggweaeARAEEILSGLGFPEEDLDRPVsELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502662315 153 VAVARALISQPDLVLADEPTAALDFkNS----EDLLNLFEeindsGqTIIMVTH 202
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDL-ESiewlEEFLKNYP-----G-TVLVVSH 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-223 |
2.06e-23 |
|
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: 94.52 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 6 KHLKKIFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVllnkeditaIKDKEISAFRR 85
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV---------TVRGRVSSLLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 86 DHLGFvfqdfnlLDTLNVRDNIYLPLVLSKSSVELMKSRLKilapklNIENLLEKQPF------ELSGGQKQRVAVARAL 159
Cdd:cd03220 91 LGGGF-------NPELTGRENIYLNGRLLGLSRKEIDEKID------EIIEFSELGDFidlpvkTYSSGMKARLAFAIAT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYH 223
Cdd:cd03220 158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDpSSIKRLCDRALVLEKGKIRF 222
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-214 |
3.31e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 93.33 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDI-----------------TAIKDkEISAFrrDHL 88
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrdeyhqdllylghqPGIKT-ELTAL--ENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 89 GFVFQDFNLLDTLNVRDniylplvlskssvelmksrlkILApKLNI---ENLLEKQpfeLSGGQKQRVAVARALISQPDL 165
Cdd:PRK13538 96 RFYQRLHGPGDDEALWE---------------------ALA-QVGLagfEDVPVRQ---LSAGQQRRVALARLWLTRAPL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502662315 166 VLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSL-AASHAKRVL 214
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLpVASDKVRKL 200
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
20-219 |
3.77e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.83 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISafRRdhLGFVFQDFNLLD 99
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS--RR--VASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 TLNVRDNIYLPLVLSKSSVELMKSrlkilAPKLNIENLLEK--------QPF-ELSGGQKQRVAVARALISQPDLVLADE 170
Cdd:PRK09536 91 EFDVRQVVEMGRTPHRSRFDTWTE-----TDRAAVERAMERtgvaqfadRPVtSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502662315 171 PTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK09536 166 PTASLDINHQVRTLELVRRLVDDGKTAVAAIHDlDLAARYCDELVLLADG 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
4.95e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKkifkTRFSkEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdKEIS 81
Cdd:PRK13636 5 ILKVEELN----YNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-KGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDhLGFVFQD-FNLLDTLNVRDNI-YLPLVLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:PRK13636 79 KLRES-VGMVFQDpDNQLFSASVYQDVsFGAVNLKLPEDEVRKRVDNALK-RTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDiDIVPLYCDNVFVMKEG 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-221 |
5.35e-23 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 93.69 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTR---FS---KEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAI 75
Cdd:cd03248 2 SLAPDHLKGIVKFQnvtFAyptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 76 KDKeisaFRRDHLGFVFQDfNLLDTLNVRDNIYLPLvlskSSVELMksRLKILAPKLNIENLLEKQPFE----------- 144
Cdd:cd03248 82 EHK----YLHSKVSLVGQE-PVLFARSLQDNIAYGL----QSCSFE--CVKEAAQKAHAHSFISELASGydtevgekgsq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSgQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-212 |
7.37e-23 |
|
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: 92.42 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 17 SKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeisafRRDHLGFVFQDFN 96
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTLNVRDNiylplvlskssvelmksrLKILAP-----KLNIENLLEK--------QPF-ELSGGQKQRVAVARALISQ 162
Cdd:TIGR01189 84 LKPELSALEN------------------LHFWAAihggaQRTIEDALAAvgltgfedLPAaQLSAGQQRRLALARLWLSR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502662315 163 PDLVLADEPTAALDfKNSEDLLN-LFEEINDSGQTIIMVTHSSLAASHAKR 212
Cdd:TIGR01189 146 RPLWILDEPTTALD-KAGVALLAgLLRAHLARGGIVLLTTHQDLGLVEARE 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-205 |
7.62e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 7.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIfktrfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEI 80
Cdd:PRK13539 1 MMLEGEDLACV------RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFrrdhLGFvfQDFnLLDTLNVRDNIYLplvlsksSVELMKSRLKILAPKLNIENL--LEKQPF-ELSGGQKQRVAVAR 157
Cdd:PRK13539 75 CHY----LGH--RNA-MKPALTVAENLEF-------WAAFLGGEELDIAAALEAVGLapLAHLPFgYLSAGQKRRVALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502662315 158 ALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSL 205
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHIPL 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-202 |
8.49e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.10 E-value: 8.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTL---EKPTSGQVLLNKEDITAIKdkeisafRRDHLGFVFQDFNLLDT 100
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQ-------FQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 LNVRDNIY------LPLVLSKS--SVELMKSRLKILAPKlNIENLLEKQpfeLSGGQKQRVAVARALISQPDLVLADEPT 172
Cdd:cd03234 96 LTVRETLTytailrLPRKSSDAirKKRVEDVLLRDLALT-RIGGNLVKG---ISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 502662315 173 AALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-202 |
9.58e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 96.84 E-value: 9.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLekPTSGQVLLNKediTAIKDKEISAFRRdHLGFVFQD 94
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKING---IELRELDPESWRK-HLSWVGQN 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLLD-TLnvRDNIYLplvlskSSVELMKSRLKILAPKLNIENLLEKQPF-----------ELSGGQKQRVAVARALISQ 162
Cdd:PRK11174 432 PQLPHgTL--RDNVLL------GNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQP 503
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502662315 163 PDLVLADEPTAALDfKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK11174 504 CQLLLLDEPTASLD-AHSEQLVMQALNAASRRQTTLMVTH 542
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-219 |
1.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.90 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 21 TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLlnkedITAIKDKEISAFR--RDHLGFVFQ--DFN 96
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL-----VSGIDTGDFSKLQgiRKLVGIVFQnpETQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTLNVRDNIYLPLVLSKSSVELMKSRLKILApKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK13644 90 FVGRTVEEDLAFGPENLCLPPIEIRKRVDRALA-EIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 177 FKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-202 |
1.33e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.43 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:PRK11160 347 TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL----RQAISVVSQR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNLL-DTLnvRDNiyLPLVLSKSSVELMKSRLKilapKLNIENLLE-KQPFE---------LSGGQKQRVAVARALISQP 163
Cdd:PRK11160 423 VHLFsATL--RDN--LLLAAPNASDEALIEVLQ----QVGLEKLLEdDKGLNawlgeggrqLSGGEQRRLGIARALLHDA 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEINdSGQTIIMVTH 202
Cdd:PRK11160 495 PLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH 532
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-222 |
1.75e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.63 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeisa 82
Cdd:COG4152 2 LELKGLTKRFGDK------TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDHLGfvfqdfnlldtlnvrdniYLP--------------LV-------LSKSSVelmKSRLKILAPKLNIENLLEKQ 141
Cdd:COG4152 70 --RRRIG------------------YLPeerglypkmkvgeqLVylarlkgLSKAEA---KRRADEWLERLGLGDRANKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 142 PFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG- 219
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQmELVEELCDRIVIINKGr 206
|
....
gi 502662315 220 -VLY 222
Cdd:COG4152 207 kVLS 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-202 |
1.81e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIkDKEIS 81
Cdd:PRK09700 5 YISMAGIGKSFGP------VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AfrRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVEL-------MKSRLKILAPKLNIENLLEKQPFELSGGQKQRVA 154
Cdd:PRK09700 78 A--QLGIGIIYQELSVIDELTVLENLYIGRHLTKKVCGVniidwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502662315 155 VARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-202 |
2.13e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 32 EEGEYIAIMGESGSGKTTLLNILSTLEKP---TSGQVLLNKEDITAIKDKEISAFrrdhlgfVFQDFNLLDTLNVRDNIY 108
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAY-------VQQDDLFIPTLTVREHLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 109 ------LPLVLSKSSVELMKSRLkILAPKL-NIENLLEKQPFE---LSGGQKQRVAVARALISQPDLVLADEPTAALDFK 178
Cdd:TIGR00955 122 fqahlrMPRRVTKKEKRERVDEV-LQALGLrKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180
....*....|....*....|....
gi 502662315 179 NSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
23-219 |
2.15e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 95.80 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeISAFRRdHLGFVFQDFNLLDTlN 102
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRR-NIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYL--PlvlSKSSVELMKSrlkilAPKLNIENLLEKQP--FE---------LSGGQKQRVAVARALISQPDLVLAD 169
Cdd:PRK13657 425 IEDNIRVgrP---DATDEEMRAA-----AERAQAHDFIERKPdgYDtvvgergrqLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502662315 170 EPTAALDFKNSEDLLNLFEEINdSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRILVFDNG 545
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-221 |
2.17e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 95.88 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 19 EETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLnkeDITAIKDKEISAFRRdHLGFVFQDFNLL 98
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL---DGADLKQWDRETFGK-HIGYLPQDVELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 99 DTlNVRDNIylplvlsKSSVELMKSRLKILAPKL-NIENLLEKQP-----------FELSGGQKQRVAVARALISQPDLV 166
Cdd:TIGR01842 405 PG-TVAENI-------ARFGENADPEKIIEAAKLaGVHELILRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 167 LADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-221 |
2.45e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.94 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeisaFRRDHLGFVFQDfNLLDTLNV 103
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH----YLHRQVALVGQE-PVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 104 RDNIYLPLVlSKSSVELMKSRLKILA-------PKLNIENLLEKQPFeLSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:TIGR00958 572 RENIAYGLT-DTPDEEIMAAAKAANAhdfimefPNGYDTEVGEKGSQ-LSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502662315 177 FKnSEDLlnLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:TIGR00958 650 AE-CEQL--LQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-224 |
4.13e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.56 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfsKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISA 82
Cdd:PRK13640 6 VEFKHVSFTYP----DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRrDHLGFVFQD-FNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:PRK13640 82 IR-EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 162 QPDLVLADEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQ 224
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-224 |
4.23e-22 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 90.92 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkeisa 82
Cdd:TIGR03740 1 LETKNLSKRFGKQ------TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 fRRD--HLGFVFQDFNLLDTLNVRDNIYLPLVLskssVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:TIGR03740 66 -RKDlhKIGSLIESPPLYENLTARENLKVHTTL----LGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASH-AKRVLFIKDGVLYHQ 224
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQlADHIGIISEGVLGYQ 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-219 |
4.28e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 4.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEI 80
Cdd:PRK13548 1 AMLEARNL------SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFR---RDH--LGFVFqdfnlldtlNVRDNIYL---PLVLSKSSVElmksrlKILAPKLNIENL--LEKQPF-ELSGGQ 149
Cdd:PRK13548 75 ARRRavlPQHssLSFPF---------TVEEVVAMgraPHGLSRAEDD------ALVAAALAQVDLahLAGRDYpQLSGGE 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 150 KQRVAVARAL--ISQPD----LVLADEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK13548 140 QQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDlNLAARYADRIVLLHQG 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
20-224 |
7.12e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.91 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISafRRdhLGFVFQDFNLLD 99
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA--KR--LAILRQENHINS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 TLNVRDniylpLV-----------LSKSSVELMKSRLKILapklNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLA 168
Cdd:COG4604 89 RLTVRE-----LVafgrfpyskgrLTAEDREIIDEAIAYL----DLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 169 DEPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDiNFASCYADHIVAMKDGRVVAQ 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
26-219 |
8.70e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.95 E-value: 8.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFR-----RDHLGFvfqDFNLLD- 99
Cdd:COG4559 19 DVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAF---PFTVEEv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 ---------TLNVRDNIYLPLVLSKSSVELMKSRLkilapklnienllekqpF-ELSGGQKQRVAVARAL--ISQPD--- 164
Cdd:COG4559 96 valgraphgSSAAQDRQIVREALALVGLAHLAGRS-----------------YqTLSGGEQQRVQLARVLaqLWEPVdgg 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 165 --LVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDlNLAAQYADRILLLHQG 216
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-221 |
1.07e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.67 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTL-----EKPTSGQVLLNKEDITAIKDKEISAFRRdhLGFVFQDFNLLDT 100
Cdd:PRK14267 22 GVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRRE--VGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 LNVRDNIYL-----PLVLSKSSV-ELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:PRK14267 100 LTIYDNVAIgvklnGLVKSKKELdERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502662315 175 LDFKNSEDLLNLFEEINDSgQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKE-YTIVLVTHSpAQAARVSDYVAFLYLGKL 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-219 |
1.07e-21 |
|
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: 89.45 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 17 SKEETTALV--DIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEKpTSGQVLLNKeditaikdkeisafrrdHLGFVFQ 93
Cdd:cd03250 12 SGEQETSFTlkDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPG-----------------SIAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 94 D---FNllDTlnVRDNI----------YlplvlsKSSVEL--MKSRLKILAPKLNIE------NLlekqpfelSGGQKQR 152
Cdd:cd03250 74 EpwiQN--GT--IRENIlfgkpfdeerY------EKVIKAcaLEPDLEILPDGDLTEigekgiNL--------SGGQKQR 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 153 VAVARALISQPDLVLADEPTAALDFKNSEDLLN--LFEEINDsGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLN-NKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-219 |
1.43e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 93.33 E-value: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNkeditaikdkeisafRRDHLGFVFQDFNL-LDTLnvR 104
Cdd:COG4178 381 DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARP---------------AGARVLFLPQRPYLpLGTL--R 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 105 DNIYLPLVLSKSSVE-----LMKSRLKILAPKLNIENLLEKqpfELSGGQKQRVAVARALISQPDLVLADEPTAALDFKN 179
Cdd:COG4178 444 EALLYPATAEAFSDAelreaLEAVGLGHLAERLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 180 SEDLLNLF-EEINDSgqTIIMVTH-SSLAASHAKRVLFIKDG 219
Cdd:COG4178 521 EAALYQLLrEELPGT--TVISVGHrSTLAAFHDRVLELTGDG 560
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-224 |
2.11e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.51 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEkPTSGQVLLNKEDITAIKDKEISAFR------RDHLGF--VFQdf 95
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRaylsqqQSPPFAmpVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 nlldtlnvrdniYLPLVLSKS-SVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI-------SQPDLVL 167
Cdd:COG4138 89 ------------YLALHQPAGaSSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 168 ADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKLVAS 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-202 |
2.27e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKtrfskeETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItaikdKEISA 82
Cdd:PRK13537 8 IDFRNVEKRYG------DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSRAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDHLGFVFQDFNLLDTLNVRDNIylpLVLSKS---SVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:PRK13537 77 HARQRVGVVPQFDNLDPDFTVRENL---LVFGRYfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-202 |
2.47e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.46 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKT-TLLNILSTLEKP----TSGQVLLNKEDITAIK 76
Cdd:PRK15134 5 LLAIENLSVAF--RQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 77 DKEISAFRRDHLGFVFQD----FNLLDTLnvRDNIYLPLVLSKSsvelMK---SRLKILA--PKLNIENL---LEKQPFE 144
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEpmvsLNPLHTL--EKQLYEVLSLHRG----MRreaARGEILNclDRVGIRQAakrLTDYPHQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTH 202
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITH 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-221 |
2.93e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.72 E-value: 2.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTL------EKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQDFNL 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKL----RKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 LDTLNVRDNIYLPL----VLSKSSVE-LMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPT 172
Cdd:PRK14246 102 FPHLSIYDNIAYPLkshgIKEKREIKkIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502662315 173 AALDFKNSEDLLNLFEEINDSgQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNE-IAIVIVSHNpQQVARVADYVAFLYNGEL 230
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-214 |
3.20e-21 |
|
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: 88.32 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 17 SKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAfrrdhLGFVFQDFN 96
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG-----LLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTLNVRDNI-YLPLVLSKSSVELMKSRLKIlapklnieNLLEKQPF-ELSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:cd03231 84 IKTTLSVLENLrFWHADHSDEQVEEALARVGL--------NGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 175 LDfKNSEDLL-NLFEEINDSGQTIIMVTHSSLAASHAK-RVL 214
Cdd:cd03231 156 LD-KAGVARFaEAMAGHCARGGMVVLTTHQDLGLSEAGaREL 196
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-221 |
7.29e-21 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 87.55 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:cd03244 11 RYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL----RSRISIIPQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 ---------FNlLDTLNVRDNIYLPLVLSKSSvelMKSRLKILAPKLNIEnlLEKQPFELSGGQKQRVAVARALISQPDL 165
Cdd:cd03244 87 pvlfsgtirSN-LDPFGEYSDEELWQALERVG---LKEFVESLPGGLDTV--VEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 166 VLADEPTAALDFKnSEDLLN--LFEEINDSgqTIIMVTH--SSLAASHakRVLFIKDGVL 221
Cdd:cd03244 161 LVLDEATASVDPE-TDALIQktIREAFKDC--TVLTIAHrlDTIIDSD--RILVLDKGRV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-202 |
1.16e-20 |
|
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: 90.63 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQ--VLLNKEDITAIKDKEISAFR-RDHLGFVFQDFNLLD 99
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRGRaKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 TLNVRDN------IYLPLVLSKssvelMKSRLKILAPKLN---IENLLEKQPFELSGGQKQRVAVARALISQPDLVLADE 170
Cdd:TIGR03269 379 HRTVLDNlteaigLELPDELAR-----MKAVITLKMVGFDeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190
....*....|....*....|....*....|....*.
gi 502662315 171 PTAALD----FKNSEDLLNLFEEINdsgQTIIMVTH 202
Cdd:TIGR03269 454 PTGTMDpitkVDVTHSILKAREEME---QTFIIVSH 486
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-203 |
1.70e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.26 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdkeIS 81
Cdd:PRK10895 3 TLTAKNLAKAYKGR------RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKS-SVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:PRK10895 74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDDlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-219 |
2.29e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.46 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLkkIFKtrFSKE-ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdKEI 80
Cdd:PRK13642 4 ILEVENL--VFK--YEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRDhLGFVFQD-FNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARAL 159
Cdd:PRK13642 77 WNLRRK-IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQ-TIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASSDRILVMKAG 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-202 |
4.30e-20 |
|
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: 89.09 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLE--KPTSGQVL-------------- 66
Cdd:TIGR03269 1 IEVKNLTKKF------DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 67 --------------LNKEDITAIK--DKEISAFRRdHLGFVFQ-DFNLLDTLNVRDNIYLPL-VLSKSSVELMKSRLKIL 128
Cdd:TIGR03269 75 pskvgepcpvcggtLEPEEVDFWNlsDKLRRRIRK-RIAIMLQrTFALYGDDTVLDNVLEALeEIGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 129 ApKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEE-INDSGQTIIMVTH 202
Cdd:TIGR03269 154 E-MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSH 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-221 |
4.87e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 8 LKKIF--KTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEdITAIkdKEISAfrr 85
Cdd:COG1134 24 LKELLlrRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL--LELGA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 86 dhlGFVFQdfnlldtLNVRDNIYLP-LVLSKSSVElMKSRLKilapklNIENL--LEK---QPFE-LSGGQKQRVAVARA 158
Cdd:COG1134 98 ---GFHPE-------LTGRENIYLNgRLLGLSRKE-IDEKFD------EIVEFaeLGDfidQPVKtYSSGMRARLAFAVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 159 LISQPDLVLADEPTAALD--FKnsEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:COG1134 161 TAVDPDILLVDEVLAVGDaaFQ--KKCLARIRELRESGRTVIFVSHSmGAVRRLCDRAIWLEKGRL 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-221 |
5.89e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 85.98 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFgvEEGEYIAIMGESGSGKTTLLNILSTL-----EKPTSGQVLLNKEDITAIKDKEISAfrRDHLGF 90
Cdd:PRK14239 15 YNKKKALNSVSLDF--YPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVDL--RKEIGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 91 VFQDFNLLdTLNVRDNIYLPLVLS----KSSV-ELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDL 165
Cdd:PRK14239 91 VFQQPNPF-PMSIYENVVYGLRLKgikdKQVLdEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 166 VLADEPTAALD----FKNSEDLLNLFEEIndsgqTIIMVTHSSLAASH-AKRVLFIKDGVL 221
Cdd:PRK14239 170 ILLDEPTSALDpisaGKIEETLLGLKDDY-----TMLLVTRSMQQASRiSDRTGFFLDGDL 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-202 |
1.16e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.66 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItaikdkeisAFR--RDHLG----FVFQDFN 96
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM---------RFAstTAALAagvaIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLDTLNVRDNIYL---P----LVLSKSSVELMKSRLKILAPKLNIENLLEkqpfELSGGQKQRVAVARALISQPDLVLAD 169
Cdd:PRK11288 90 LVPEMTVAENLYLgqlPhkggIVNRRLLNYEAREQLEHLGVDIDPDTPLK----YLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190
....*....|....*....|....*....|...
gi 502662315 170 EPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVILYVSH 198
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-219 |
1.20e-19 |
|
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: 87.95 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD---FNllDT 100
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQDtvlFN--DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 LnvRDNI-YLPLVLSKSSVELmksrlkilAPKL-NIENLLEKQP-----------FELSGGQKQRVAVARALISQPDLVL 167
Cdd:COG5265 448 I--AYNIaYGRPDASEEEVEA--------AARAaQIHDFIESLPdgydtrvgergLKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502662315 168 ADEPTAALDFKNSEDLLNLFEEINdSGQTIIMVTH--SSLAasHAKRVLFIKDG 219
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVA-RGRTTLVIAHrlSTIV--DADEILVLEAG 568
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-202 |
1.31e-19 |
|
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: 87.57 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTL--EKPTSGQVLLNKEDITA--IKD 77
Cdd:TIGR02633 1 LLEMKGIVKTF------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKAsnIRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEisafrRDHLGFVFQDFNLLDTLNVRDNIYLPLVLS----KSSVELMKSRLKILAPKLNIENLLEKQPF-ELSGGQKQR 152
Cdd:TIGR02633 75 TE-----RAGIVIIHQELTLVPELSVAENIFLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502662315 153 VAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISH 199
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-224 |
1.47e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.53 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 22 TALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSG-----QVLLNKEDITAIKDkeISAFRRdHLGFVFQDFN 96
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRR-RVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 LLdTLNVRDNIYL-----PLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEP 171
Cdd:PRK14271 112 PF-PMSIMDNVLAgvrahKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502662315 172 TAALDFKNSEDLLNLFEEINDSgQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADR-LTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-219 |
1.69e-19 |
|
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: 83.35 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLE--KPTSGQVLLNKEDITAIKDKEI 80
Cdd:cd03217 1 LEIKDL------HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SafrRDHLGFVFQdfnlldtlnvrdniylplvlskSSVELmksrlkilaPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:cd03217 75 A---RLGIFLAFQ----------------------YPPEI---------PGVKNADFLRYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSS--LAASHAKRVLFIKDG 219
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQrlLDYIKPDRVHVLYDG 181
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
26-219 |
1.84e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISafRRdhLGFVFQDFNLLDTLNVRD 105
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA--RR--IGLLAQNATTPGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 106 NI------YLPLVLS--KSSVELMKSRLKILApklnIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDF 177
Cdd:PRK10253 101 LVargrypHQPLFTRwrKEDEEAVTKAMQATG----ITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 178 KNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK10253 177 SHQIDLLELLSELNrEKGYTLAAVLHDlNQACRYASHLIALREG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
23-219 |
2.67e-19 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 86.72 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQDFNLLDTlN 102
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL----RQFINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPlVLSKSSVELMKSRLKILAPKLNIENL-------LEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:TIGR01193 564 ILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMplgyqteLSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 176 DFKNSEDLLNLFEEINDsgQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:TIGR01193 643 DTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-176 |
2.88e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKTR---FSK--EETTALVDIDFGVEEGEYIAIMGESGSGK-TTLLNILSTLekPTSGQVLLNKEDITA 74
Cdd:PRK15134 274 PLLDVEQLQVAFPIRkgiLKRtvDHNVVVKNISFTLRPGETLGLVGESGSGKsTTGLALLRLI--NSQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 75 IKDKEISAFRRdHLGFVFQDFNllDTLNVRDNIylplvlskssVELMKSRLKILAPKLN--------IENLLE------- 139
Cdd:PRK15134 352 LNRRQLLPVRH-RIQVVFQDPN--SSLNPRLNV----------LQIIEEGLRVHQPTLSaaqreqqvIAVMEEvgldpet 418
|
170 180 190
....*....|....*....|....*....|....*....
gi 502662315 140 --KQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK15134 419 rhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-202 |
3.81e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfskeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLeKPT---SGQVLLNKEDITA--IK 76
Cdd:PRK13549 5 LLEMKNITKTFGG------VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQAsnIR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 77 DKEisafrRDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSV---ELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRV 153
Cdd:PRK13549 78 DTE-----RAGIAIIHQELALVKELSVLENIFLGNEITPGGImdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502662315 154 AVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-202 |
3.88e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.45 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTRFS-----KEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIK 76
Cdd:PRK10261 313 ILQVRNLVTRFPLRSGllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 77 DKEISAFRRDhLGFVFQD-FNLLDT-LNVRDNIYLPL-VLSKSSVELMKSRLKILAPKLNI--ENLLeKQPFELSGGQKQ 151
Cdd:PRK10261 393 PGKLQALRRD-IQFIFQDpYASLDPrQTVGDSIMEPLrVHGLLPGKAAAARVAWLLERVGLlpEHAW-RYPHEFSGGQRQ 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502662315 152 RVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTH 202
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQrDFGIAYLFISH 522
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-219 |
6.07e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.12 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKkifkTRFSKeeTTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIS 81
Cdd:PRK11300 5 LLSVSGLM----MRFGG--LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 afrrdHLGFV--FQDFNLLDTLNVRDNIylpLVLSKSSVE------LMKS------------RLKILAPKLNIENLLEKQ 141
Cdd:PRK11300 79 -----RMGVVrtFQHVRLFREMTVIENL---LVAQHQQLKtglfsgLLKTpafrraesealdRAATWLERVGLLEHANRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 142 PFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDS-GQTIIMVTHS-SLAASHAKRVLFIKDG 219
Cdd:PRK11300 151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDmKLVMGISDRIYVVNQG 230
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-202 |
1.30e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 82.09 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISafrrdHLGFV--FQDFNLLDT 100
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIA-----RLGIGrkFQKPTVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 LNVRDNIYLPLVLSKSSVELMKSRLKiLAPKLNIENLLE---------KQPFELSGGQKQRVAVARALISQPDLVLADEP 171
Cdd:COG4674 100 LTVFENLELALKGDRGVFASLFARLT-AEERDRIEEVLEtigltdkadRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEP 178
|
170 180 190
....*....|....*....|....*....|.
gi 502662315 172 TAALDFKNSEDLLNLFEEINdSGQTIIMVTH 202
Cdd:COG4674 179 VAGMTDAETERTAELLKSLA-GKHSVVVVEH 208
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-222 |
1.61e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 84.25 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 19 EETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdKEISAFRRdHLGFVFQDFNLL 98
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYRK-LFSAVFTDFHLF 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 99 DTLNVRDNiylplvlSKSSVELMKSRLKIL--APKLNIEN--LLEKQpfeLSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:PRK10522 410 DQLLGPEG-------KPANPALVEKWLERLkmAHKLELEDgrISNLK---LSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502662315 175 LD--FKNS--EDLLNLFEEindSGQTIIMVTHSSLAASHAKRVLFIKDGVLY 222
Cdd:PRK10522 480 QDphFRREfyQVLLPLLQE---MGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-229 |
2.30e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKifKTRFSkeettalvDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDIT------AI 75
Cdd:COG1129 256 VLEVEGLSV--GGVVR--------DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAI 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 76 KDKeisafrrdhLGFVFQD---FNLLDTLNVRDNIYLPlVLSKSS-------------VELMKSRLKILAPklNIENLLE 139
Cdd:COG1129 326 RAG---------IAYVPEDrkgEGLVLDLSIRENITLA-SLDRLSrgglldrrreralAEEYIKRLRIKTP--SPEQPVG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 140 kqpfELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVthSS-----LAASHakRVL 214
Cdd:COG1129 394 ----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI--SSelpelLGLSD--RIL 465
|
250
....*....|....*
gi 502662315 215 FIKDGVLYHQLYRGE 229
Cdd:COG1129 466 VMREGRIVGELDREE 480
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-222 |
2.87e-18 |
|
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: 84.29 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 5 VKHLKKIFKTrfSKEETTALVDIDFgvEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItaikDKEISAFR 84
Cdd:TIGR01257 931 VKNLVKIFEP--SGRPAVDRLNITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 85 RDhLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPD 164
Cdd:TIGR01257 1003 QS-LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 165 LVLADEPTAALDFKNSEDLLNLFEEINdSGQTIIMVTHSSLAAS-HAKRVLFIKDGVLY 222
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-210 |
3.75e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 79.99 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItaikDKEISAFRRdHLGFVFQDF 95
Cdd:PRK13540 9 FDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK-QLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLLDTLNVRDNIYLPLVLSKSSVELMKsrlkiLAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:PRK13540 84 GINPYLTLRENCLYDIHFSPGAVGITE-----LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 502662315 176 DFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHA 210
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKA 193
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
26-218 |
3.76e-18 |
|
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: 79.12 E-value: 3.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVllnkeditaikdkeISAFRRDHLgfvfqdfnlldtlnvrd 105
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------------GMPEGEDLL----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 106 niYLPLvlskssvelmksrlkilAPKLNIENLLEkQ---PF--ELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNS 180
Cdd:cd03223 68 --FLPQ-----------------RPYLPLGTLRE-QliyPWddVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*...
gi 502662315 181 EDLLNLfeeINDSGQTIIMVTHSSLAASHAKRVLFIKD 218
Cdd:cd03223 128 DRLYQL---LKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-239 |
5.26e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKT-TLLNILSTLEKP----TSGQVLLNKE-----D 71
Cdd:PRK10261 12 VLAVENLNIAFMQ--EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRsrqviE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 72 ITAIKDKEISAFRRDHLGFVFQDfnLLDTLN--------VRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPF 143
Cdd:PRK10261 90 LSEQSAAQMRHVRGADMAMIFQE--PMTSLNpvftvgeqIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 144 ELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFikdgvl 221
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkEMSMGVIFITHDmGVVAEIADRVLV------ 241
|
250
....*....|....*...
gi 502662315 222 yhqLYRGEKSSTEFAKEI 239
Cdd:PRK10261 242 ---MYQGEAVETGSVEQI 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-219 |
8.08e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.30 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLL-NILSTLEKpTSGQVLLNKEDITAIKDKEISAFRRDHLGFVFQDFNLLDTlN 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPLVLSKSSVELMKSRLKiLAPKLNI-----ENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDF 177
Cdd:cd03290 95 VEENITFGSPFNKQRYKAVTDACS-LQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 178 KNSEDLLN--LFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03290 174 HLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
2-239 |
9.89e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.94 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKkifkTRFSKEETT--ALVDIDFGVEEGEYIAIMGESGSGKT-TLLNILSTLEKP---TSGQVLLNKEDITAI 75
Cdd:PRK11022 3 LLNVDKLS----VHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 76 KDKEisafRRDHLG----FVFQD------------FNLLDTLNVRDNIYLPlVLSKSSVELMKsRLKILAPklniENLLE 139
Cdd:PRK11022 79 SEKE----RRNLVGaevaMIFQDpmtslnpcytvgFQIMEAIKVHQGGNKK-TRRQRAIDLLN-QVGIPDP----ASRLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 140 KQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQ-TIIMVTHS-SLAASHAKRVLFik 217
Cdd:PRK11022 149 VYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDlALVAEAAHKIIV-- 226
|
250 260
....*....|....*....|..
gi 502662315 218 dgvlyhqLYRGEKSSTEFAKEI 239
Cdd:PRK11022 227 -------MYAGQVVETGKAHDI 241
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-202 |
4.16e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 4 EVKHLKKIFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEK--PTSGQVllnkeditAIKDKEIS 81
Cdd:COG2401 26 RVAIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCV--------DVPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 afrrdhlgfvfQDFNLLDTLNVRDNIylplvlsKSSVELmksrlkILAPKLNIENLLEKQPFELSGGQKQRVAVARALIS 161
Cdd:COG2401 98 -----------REASLIDAIGRKGDF-------KDAVEL------LNAVGLSDAVLWLRRFKELSTGQKFRFRLALLLAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 162 QPDLVLADEPTAALDFKNSEDL-LNLFEEINDSGQTIIMVTH 202
Cdd:COG2401 154 RPKLLVIDEFCSHLDRQTAKRVaRNLQKLARRAGITLVVATH 195
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-176 |
4.45e-17 |
|
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: 77.83 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 33 EGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDItAIKDKEISAfrrdhlgfvfqDFnlldTLNVRDniylpLV 112
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKA-----------DY----EGTVRD-----LL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 113 LSKSSVELMKSRLK--ILAPkLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:cd03237 83 SSITKDFYTHPYFKteIAKP-LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-202 |
4.45e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEK--PTSGQVLLNKEDITaikdkEI 80
Cdd:COG0396 1 LEIKNL------HVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDIL-----EL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 SAFRRDHLG-FV-FQD---------FNLLDT-LNVRDNIYLPLVLsksSVELMKSRLKILapKLNiENLLEKQPFE-LSG 147
Cdd:COG0396 70 SPDERARAGiFLaFQYpveipgvsvSNFLRTaLNARRGEELSARE---FLKLLKEKMKEL--GLD-EDFLDRYVNEgFSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 148 GQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-224 |
5.34e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.82 E-value: 5.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALV-DIDFGVEEGEYIAIMGESGSGKT----TLLNILSTLEKPTSGQVLLNKEDITAikdkeiSAFRRDHLGFVFQD--- 94
Cdd:PRK10418 17 PLVhGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP------CALRGRKIATIMQNprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 -FNLLDTL--NVRDNIylpLVLSKSSVE-LMKSRLKilAPKL-NIENLLEKQPFELSGGQKQRVAVARALISQPDLVLAD 169
Cdd:PRK10418 91 aFNPLHTMhtHARETC---LALGKPADDaTLTAALE--AVGLeNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502662315 170 EPTAALDFKNSEDLLNLFEEI-NDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDmGVVARLADDVAVMSHGRIVEQ 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-176 |
1.47e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 78.70 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 33 EGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLnKEDItAIKDKEISAfrrdhlgfvfqDFNLldtlNVRDniylplV 112
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKI-SYKPQYIKP-----------DYDG----TVED------L 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 113 LSKSSVELMKSRLK--ILAPkLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK13409 421 LRSITDDLGSSYYKseIIKP-LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-202 |
3.97e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 74.76 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKkifkTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsa 82
Cdd:cd03369 7 IEVENLS----VRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDHLGFVFQDFNLLDTlNVRDNiyLPLVLSKSSVELMKSrLKILAPKLNienllekqpfeLSGGQKQRVAVARALISQ 162
Cdd:cd03369 81 --RSSLTIIPQDPTLFSG-TIRSN--LDPFDEYSDEEIYGA-LRVSEGGLN-----------LSQGQRQLLCLARALLKR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 163 PDLVLADEPTAALDFKnSEDLLN--LFEEINDSgqTIIMVTH 202
Cdd:cd03369 144 PRVLVLDEATASIDYA-TDALIQktIREEFTNS--TILTIAH 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-223 |
4.04e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKeditaikdkeis 81
Cdd:COG0488 315 VLELEGLSKSY------GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE------------ 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 afrRDHLGFVFQDFNLLD-TLNVRDNIylplvlskssvelmkSRLKILAPKLNIENLLEKqpF------------ELSGG 148
Cdd:COG0488 377 ---TVKIGYFDQHQEELDpDKTVLDEL---------------RDGAPGGTEQEVRGYLGR--FlfsgddafkpvgVLSGG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 149 QKQRVAVARALISQPDLVLADEPT--------AALdfknsEDLLNLFEeindsGqTIIMVTH-SSLAASHAKRVLFIKDG 219
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTnhldietlEAL-----EEALDDFP-----G-TVLLVSHdRYFLDRVATRILEFEDG 505
|
....
gi 502662315 220 VLYH 223
Cdd:COG0488 506 GVRE 509
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-176 |
4.75e-16 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 77.13 E-value: 4.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 31 VEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVllnKEDIT-AIKDKEISAfrrdhlgfvfqDFNLLdtlnVRDNIYl 109
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKiSYKPQYISP-----------DYDGT----VEEFLR- 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 110 plvlSKSSVELMKSRLKI-LAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:COG1245 424 ----SANTDDFGSSYYKTeIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-208 |
6.50e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.20 E-value: 6.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEK--PT---SGQVLLNKEDITAiKDKEISAFRRdHLGFVFQDFNL 97
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRR-RIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 LDTlNVRDNI-YLPLVLS-KSSV-ELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:PRK14243 103 FPK-SIYDNIaYGARINGyKGDMdELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190
....*....|....*....|....*....|....
gi 502662315 175 LDFKNSEDLLNLFEEINDSgQTIIMVTHSSLAAS 208
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAA 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-207 |
8.71e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.73 E-value: 8.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLN-KEDITAIKDKEISAFrrDHLGFVFQD 94
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDgKTATRGDRSRFMAYL--GHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 fnlLDTLnvrDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQpfeLSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:PRK13543 97 ---LSTL---ENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180 190
....*....|....*....|....*....|....*
gi 502662315 175 LDFKNSeDLLN--LFEEINDSGQTIImVTHSSLAA 207
Cdd:PRK13543 168 LDLEGI-TLVNrmISAHLRGGGAALV-TTHGAYAA 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-202 |
8.81e-16 |
|
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: 72.10 E-value: 8.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRfskeetTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGqvllnkeDITAIKDKEISa 82
Cdd:cd03221 1 IELENLSKTYGGK------LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------IVTWGSTVKIG- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frrdhlgfvfqdfnlldtlnvrdniYLPlvlskssvelmksrlkilapklnienllekqpfELSGGQKQRVAVARALISQ 162
Cdd:cd03221 67 -------------------------YFE---------------------------------QLSGGEKMRLALAKLLLEN 88
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502662315 163 PDLVLADEPTAALDFKNSEDLLNLFEEINdsgQTIIMVTH 202
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEYP---GTVILVSH 125
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-227 |
1.08e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDitaIKDKEISAFrRDHLGFVFQDFNLL- 98
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASL-RNQVALVSQNVHLFn 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 99 DTL--NV---RDNIYlplvlSKSSVElmksrlkiLAPKL--------NIENLLEKQPFE----LSGGQKQRVAVARALIS 161
Cdd:PRK11176 431 DTIanNIayaRTEQY-----SREQIE--------EAARMayamdfinKMDNGLDTVIGEngvlLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 162 Q-PDLVLaDEPTAALDFKNSEDLLNLFEEINDSgQTIIMVTHSSLAASHAKRVLFIKDGVL---------------YHQL 225
Cdd:PRK11176 498 DsPILIL-DEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEIvergthaellaqngvYAQL 575
|
..
gi 502662315 226 YR 227
Cdd:PRK11176 576 HK 577
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-221 |
1.14e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.07 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 7 HLKKIFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTS--GQVLLNKEDITaikdKEIsaFR 84
Cdd:PLN03211 67 HKPKISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQI--LK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 85 RdhLGFVFQDFNLLDTLNVRDNIY------LPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPF--ELSGGQKQRVAVA 156
Cdd:PLN03211 141 R--TGFVTQDDILYPHLTVRETLVfcsllrLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirGISGGERKRVSIA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 157 RALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSlaashAKRVLFIKDGVL 221
Cdd:PLN03211 219 HEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP-----SSRVYQMFDSVL 278
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-200 |
1.29e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLkkifkTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdKEIS 81
Cdd:COG3845 257 VLEVENL-----SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG---LSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQD---FNLLDTLNVRDNIYL------PL----VLSKSSV-----ELMKsRLKILAPklNIENLLEKqpf 143
Cdd:COG3845 329 ERRRLGVAYIPEDrlgRGLVPDMSVAENLILgryrrpPFsrggFLDRKAIrafaeELIE-EFDVRTP--GPDTPARS--- 402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502662315 144 eLSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMV 200
Cdd:COG3845 403 -LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLI 458
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-203 |
1.35e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 22 TALVDIDFGVEEGEYIAIMGESGSGKttllnilSTLEKPTSGQVLLNKEDITAIKDKEISAFRRDHLGFVFQD------F 95
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGK-------STLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSeevdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:PRK15056 94 PVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180
....*....|....*....|....*...
gi 502662315 176 DFKNSEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-203 |
1.42e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 74.30 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTL---LNILSTLEKPT--SGQVLLNKEDITAiKDKEISAFRRdHLGF 90
Cdd:PRK14258 15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVrvEGRVEFFNQNIYE-RRVNLNRLRR-QVSM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 91 VFQDFNLLdTLNVRDNIY--LPLVLSKSSVEL---MKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDL 165
Cdd:PRK14258 93 VHPKPNLF-PMSVYDNVAygVKIVGWRPKLEIddiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 502662315 166 VLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHS 203
Cdd:PRK14258 172 LLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN 210
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
24-219 |
1.54e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 72.66 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILStlEKPTSGQVllnKEDITAIKDKEISAFRRdHLGFVFQDFNLLDTLNV 103
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVI---TGEILINGRPLDKNFQR-STGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 104 RDNIYLPLVLSKSSVElmksrlkilapklnienllekqpfelsggQKQRVAVARALISQPDLVLADEPTAALDFKNSEDL 183
Cdd:cd03232 97 REALRFSALLRGLSVE-----------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 502662315 184 LNLFEEINDSGQTIIMVTH--SSLAASHAKRVLFIKDG 219
Cdd:cd03232 148 VRFLKKLADSGQAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
23-200 |
1.61e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.37 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikDKEISAFRRDHLGFVFQDFNLLDTLN 102
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKIMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLP-LVLSKSSVELMKSRLKILAPKLNIENLleKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSE 181
Cdd:PRK11614 97 VEENLAMGgFFAERDQFQERIKWVYELFPRLHERRI--QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170
....*....|....*....
gi 502662315 182 DLLNLFEEINDSGQTIIMV 200
Cdd:PRK11614 175 QIFDTIEQLREQGMTIFLV 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
26-202 |
1.98e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.79 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQvllnkedITAIKDKEISAFR--RDHLGFVFQDFNLLDTLNV 103
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGK-------ITVLGVPVPARARlaRARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 104 RDNIylpLVLSKSSVelMKSR-LKILAPKL----NIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFK 178
Cdd:PRK13536 132 RENL---LVFGRYFG--MSTReIEAVIPSLlefaRLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180
....*....|....*....|....
gi 502662315 179 NSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK13536 207 ARHLIWERLRSLLARGKTILLTTH 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-202 |
2.16e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVllnkeditaikdkeisafRRDH---LGFVFQDFNLLDT 100
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------------KRNGklrIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 101 LNVRDNIYLPLVLSKSSVELMKSRLKILAPKLnIENLLEKqpfeLSGGQKQRVAVARALISQPDLVLADEPTAALDFKNS 180
Cdd:PRK09544 82 LPLTVNRFLRLRPGTKKEDILPALKRVQAGHL-IDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180
....*....|....*....|...
gi 502662315 181 EDLLNLFEEI-NDSGQTIIMVTH 202
Cdd:PRK09544 157 VALYDLIDQLrRELDCAVLMVSH 179
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-202 |
2.53e-14 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 72.12 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 32 EEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVllnkeDITAIKDKEISAFRrdhlGFVFQD-FNLLDTLNVR------ 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-----DEEPSWDEVLKRFR----GTELQDyFKKLANGEIKvahkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 105 --DNIylPLVLSKSSVELMKS-----RLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDF 177
Cdd:COG1245 168 yvDLI--PKVFKGTVRELLEKvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*
gi 502662315 178 KNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-201 |
3.68e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDIT------AIKD--KEISAFRRDHlGFvFQDFNL 97
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldAVKKgmAYITESRRDN-GF-FPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 LDTLNVRDNIYLP-------LVLSKSSVELMKSRLKILAPKLNIenlLEKQPFELSGGQKQRVAVARALISQPDLVLADE 170
Cdd:PRK09700 359 AQNMAISRSLKDGgykgamgLFHEVDEQRTAENQRELLALKCHS---VNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190
....*....|....*....|....*....|.
gi 502662315 171 PTAALDFKNSEDLLNLFEEINDSGQTIIMVT 201
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVS 466
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-202 |
4.00e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILS------TLEkptsGQVLLnkeditaikDKEISAFR--RD--HLGFVF 92
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSYE----GEILF---------DGEVCRFKdiRDseALGIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 93 --QDFNLLDTLNVRDNIYLPLVLSKSSV---ELMKSRLKILAPKLNienlLEKQPFELSG----GQKQRVAVARALISQP 163
Cdd:NF040905 83 ihQELALIPYLSIAENIFLGNERAKRGVidwNETNRRARELLAKVG----LDESPDTLVTdigvGKQQLVEIAKALSKDV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISH 197
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-224 |
6.66e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 20 ETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLeKPTSGQVLLNKEDITAIKDKEIsAFRRDHLG------F--- 90
Cdd:PRK03695 8 VSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAEL-ARHRAYLSqqqtppFamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 91 VFQdfnlldtlnvrdniYLPLVL-SKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVArALISQ--PD--- 164
Cdd:PRK03695 86 VFQ--------------YLTLHQpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLA-AVVLQvwPDinp 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 165 ---LVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK03695 151 agqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLLAS 214
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-202 |
7.72e-14 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 69.32 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 31 VEEGEYIAIMGESGSGKTTLLNILSTLEKPTsgqvlLNKEDITAIKDKEISAFRRDHLGFVFQDFNLLDTLNVRDNIY-- 108
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPN-----LGKFDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 109 -LPLVLSKSSVELMKSR-----LKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:cd03236 98 lIPKAVKGKVGELLKKKdergkLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|
gi 502662315 183 LLNLFEEINDSGQTIIMVTH 202
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEH 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-179 |
8.06e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 8.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 4 EVKHLKKI-FKT-RF---SKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNkeDITAIKDK 78
Cdd:PTZ00265 376 KLKDIKKIqFKNvRFhydTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDI 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 79 EISAFrRDHLGFVFQDfNLLDTLNVRDNIYLPL-----------------------------------------VLSKSS 117
Cdd:PTZ00265 454 NLKWW-RSKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDS 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 118 VELMKSRLKI----------LAPKLNIENLLEKQP-----------FELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PTZ00265 532 NELIEMRKNYqtikdsevvdVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
...
gi 502662315 177 FKN 179
Cdd:PTZ00265 612 NKS 614
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-219 |
1.58e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 4 EVKHLKKI-FKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILS---TLEKPTSGQVLLNKEDITaikdke 79
Cdd:TIGR00956 758 DIFHWRNLtYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLD------ 831
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 80 iSAFRRdHLGFVFQDFNLLDTLNVRDNI----YLPLVLSKSSVELMKSRLKILapklnieNLLEKQPFE----------L 145
Cdd:TIGR00956 832 -SSFQR-SIGYVQQQDLHLPTSTVRESLrfsaYLRQPKSVSKSEKMEYVEEVI-------KLLEMESYAdavvgvpgegL 902
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502662315 146 SGGQKQRVAVARALISQPDLVL-ADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH--SSLAASHAKRVLFIKDG 219
Cdd:TIGR00956 903 NVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpSAILFEEFDRLLLLQKG 979
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-176 |
2.72e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 31 VEEGEYIAIMGESGSGKTTLLNILSTLEKPTsgqvlLNKEDITAIKDKEISAFRRDHLGFVFQDfnlldtlnVRDN-I-- 107
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEVLKRFRGTELQNYFKK--------LYNGeIkv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 108 --------YLPLVLSKSSVELMKS-----RLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAA 174
Cdd:PRK13409 163 vhkpqyvdLIPKVFKGKVRELLKKvdergKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
..
gi 502662315 175 LD 176
Cdd:PRK13409 243 LD 244
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-176 |
6.09e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQDFNLL-DTLn 102
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLaDTF- 431
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 103 vRDNIYLPLVLSKSSV--ELMKSRLKILAPKL--NIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK10790 432 -LANVTLGRDISEEQVwqALETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-256 |
1.34e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 25 VDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEisafrRDHLGFVF-----QDFNLld 99
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-----RLARGLVYlpedrQSSGL-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 100 tlnvrdniYLPLVLSKSSVELMKSRLKI-LAPK------------LNIENLLEKQPFE-LSGGQKQRVAVARALISQPDL 165
Cdd:PRK15439 353 --------YLDAPLAWNVCALTHNRRGFwIKPArenavleryrraLNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 166 VLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVThSSL--AASHAKRVLFIKDGVLYHQLyRGEKSSTEfakeiTLSM 243
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFIS-SDLeeIEQMADRVLVMHQGEISGAL-TGAAINVD-----TIMR 497
|
250
....*....|...
gi 502662315 244 TAFlGASEDEEVS 256
Cdd:PRK15439 498 LAF-GEHQAQEAS 509
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
26-202 |
1.71e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLL----NKEDITAIKD-----------KEISAFRRDHLGF 90
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfkneHTNDMTNEQDyqgdeeqnvgmKNVNEFSLTKEGG 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 91 VFQDFN--------LLDTLNVRD----------------------NIYLPLVLSK--SSVELMKSRLKILAPKLNIENLL 138
Cdd:PTZ00265 1266 SGEDSTvfknsgkiLLDGVDICDynlkdlrnlfsivsqepmlfnmSIYENIKFGKedATREDVKRACKFAAIDEFIESLP 1345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502662315 139 EKQ-----PF--ELSGGQKQRVAVARALISQPDLVLADEPTAALDfKNSEDLL-NLFEEINDSG-QTIIMVTH 202
Cdd:PTZ00265 1346 NKYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIeKTIVDIKDKAdKTIITIAH 1417
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
34-224 |
1.73e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 34 GEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKeisAFRRDhLGFVFQDFNLLDTLNVRDNIYL---P 110
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARK-VAYLPQQLPAAEGMTVRELVAIgryP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 111 L--VLSKSSVELMKSRLKILApklnienLLEKQPF------ELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSED 182
Cdd:PRK10575 113 WhgALGRFGAADREKVEEAIS-------LVGLKPLahrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 183 LLNLFEEIN-DSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK10575 186 VLALVHRLSqERGLTVIAVLHDiNMAARYCDYLVALRGGEMIAQ 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-203 |
1.82e-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: 66.96 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFktrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLL-NKEDITAIKDKEi 80
Cdd:TIGR01257 1937 ILRLNELTKVY----SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSILTNISDVH- 2011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 81 safrrDHLGFVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALI 160
Cdd:TIGR01257 2012 -----QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-202 |
2.33e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKifktrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILS--TLEKPTSGQVLLNKEDITaikdkE 79
Cdd:CHL00131 7 ILEIKNLHA------SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESIL-----D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 80 ISAFRRDHLGfVFQDFNLLDTLNVRDNI-YLPLVLSKSSVELMKSRL------KILAPKLNIENL----LEKQPFE-LSG 147
Cdd:CHL00131 76 LEPEERAHLG-IFLAFQYPIEIPGVSNAdFLRLAYNSKRKFQGLPELdpleflEIINEKLKLVGMdpsfLSRNVNEgFSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 148 GQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2-209 |
2.87e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKT----TLLNILSTLEKPTSGQVLLNKEDITAIKD 77
Cdd:COG4170 3 LLDIRNLTIEIDT--PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEISAFRRDHLGFVFQD-FNLLD-TLNVRDNiyLPLVLSKSSVELM--------KSRLKILAPKLNIEN---LLEKQPFE 144
Cdd:COG4170 81 RERRKIIGREIAMIFQEpSSCLDpSAKIGDQ--LIEAIPSWTFKGKwwqrfkwrKKRAIELLHRVGIKDhkdIMNSYPHE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 145 LSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIND-SGQTIIMVTHSSLAASH 209
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQ 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-202 |
2.93e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKifktRFSKEETtaLVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkEIS 81
Cdd:PRK15439 11 LLCARSISK----QYSGVEV--LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA-----RLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLG--FVFQDFNLLDTLNVRDNIYLPLVLSKSSVELMKSRLKILAPKLNienlLEKQPFELSGGQKQRVAVARAL 159
Cdd:PRK15439 80 PAKAHQLGiyLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLD----LDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 160 ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISH 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-202 |
5.06e-12 |
|
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: 65.34 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 34 GEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLnKEDITaikdkeisafrrdhLGFVFQDFNLLDTLNVRDNIYLPLVL 113
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGIK--------------VGYLPQEPQLDPTKTVRENVEEGVAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 114 SKSSV-ELMKSRLKILAPKLNIENLLEKQ-----------------------------PFE-----LSGGQKQRVAVARA 158
Cdd:TIGR03719 96 IKDALdRFNEISAKYAEPDADFDKLAAEQaelqeiidaadawdldsqleiamdalrcpPWDadvtkLSGGERRRVALCRL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 159 LISQPDLVLADEPTAALDfknSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:TIGR03719 176 LLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTH 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-202 |
5.19e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.26 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEgeYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKdKEISAFRRdHLGFVFQD 94
Cdd:PRK13638 10 RYQDEPVLKGLNLDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQ-QVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 FNL-LDTLNVRDNIYLPLV-LSKSSVELMKSRLKILApkLNIENLLEKQPFE-LSGGQKQRVAVARALISQPDLVLADEP 171
Cdd:PRK13638 86 PEQqIFYTDIDSDIAFSLRnLGVPEAEITRRVDEALT--LVDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190
....*....|....*....|....*....|.
gi 502662315 172 TAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSH 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-201 |
9.88e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKE--------ISAFR-RDhlGFVFQdfn 96
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRkRD--GLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 97 lldtLNVRDNIYLPLV--LSKSSVELMKSRLKILAPK----LNIENLLEKQPF-ELSGGQKQRVAVARALISQPDLVLAD 169
Cdd:PRK10762 345 ----MSVKENMSLTALryFSRAGGSLKHADEQQAVSDfirlFNIKTPSMEQAIgLLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190
....*....|....*....|....*....|....*
gi 502662315 170 EPTAALDF---KNSEDLLNLFEEindSGQTIIMVT 201
Cdd:PRK10762 421 EPTRGVDVgakKEIYQLINQFKA---EGLSIILVS 452
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-224 |
1.51e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 17 SKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEKPTSGQVLLnkeditaikdkeisafrRDHLGFVFQD- 94
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVI-----------------RGTVAYVPQVs 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 --FNLldtlNVRDNIYLPLVLSKS------SVELMKSRLKILaPKLNIENLLEKQpFELSGGQKQRVAVARALISQPDLV 166
Cdd:PLN03130 689 wiFNA----TVRDNILFGSPFDPEryeraiDVTALQHDLDLL-PGGDLTEIGERG-VNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 167 LADEPTAALDFKNSEDLLN--LFEEIndSGQTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVFDkcIKDEL--RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
27-221 |
1.82e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.66 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 27 IDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdKEISAFrRDHLGFVFQDFNLLDTLNVRDN 106
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAY-RQLFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 107 IYLPLVLSkssvELMKsRLKiLAPKLNIENllekQPF---ELSGGQKQRVAVARALISQPDLVLADEPTAALD--FKNS- 180
Cdd:COG4615 427 EADPARAR----ELLE-RLE-LDHKVSVED----GRFsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDpeFRRVf 496
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502662315 181 -EDLLNlfeEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:COG4615 497 yTELLP---ELKARGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-216 |
2.95e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 60.41 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNilSTLEKptSGQVLLNKEditaikdkeISAFRRDHLGFVFQDF 95
Cdd:cd03238 3 VSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA--SGKARLISF---------LPKFSRNKLIFIDQLQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLLDT-LNvrdniYLPLVLSKSSvelmksrlkilapklnienllekqpfeLSGGQKQRVAVARALISQPD--LVLADEPT 172
Cdd:cd03238 70 FLIDVgLG-----YLTLGQKLST---------------------------LSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502662315 173 AALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFI 216
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-202 |
3.64e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafRRDHLGFVFQDFNLLDTLN 102
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA---LENGISMVHQELNLVLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYL---PLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKN 179
Cdd:PRK10982 90 VMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180
....*....|....*....|...
gi 502662315 180 SEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISH 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
2-219 |
3.74e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.77 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILS-TLEKPT-------SGQVLLNKEDIT 73
Cdd:PRK13547 1 MLTADHL------HVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 74 AIKDKEISAFR-----RDHLGFVFqdfnlldtlNVRDNIYL---PLVlsKSSVELMKSRLKILAPKLNI---ENLLEKQP 142
Cdd:PRK13547 75 AIDAPRLARLRavlpqAAQPAFAF---------SAREIVLLgryPHA--RRAGALTHRDGEIAWQALALagaTALVGRDV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 143 FELSGGQKQRVAVARAL---------ISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQ--TIIMVTHSSLAASHAK 211
Cdd:PRK13547 144 TTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHAD 223
|
....*...
gi 502662315 212 RVLFIKDG 219
Cdd:PRK13547 224 RIAMLADG 231
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-221 |
4.19e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 28 DFGVEEGEYIAIMGESGSGKTTLLNILStlekptsGQVLLNKEDITAIKDKEISAFR----RDHLGFVFqDF------NL 97
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRIIYEQDLIVARLQqdppRNVEGTVY-DFvaegieEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 LDTLNVRDNIyLPLVLSKSSvELMKSRLKILAPKLNIENLL-----------------EKQPFELSGGQKQRVAVARALI 160
Cdd:PRK11147 95 AEYLKRYHDI-SHLVETDPS-EKNLNELAKLQEQLDHHNLWqlenrinevlaqlgldpDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSgqtIIMVTHS-SLAASHAKRVLFIKDGVL 221
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS---IIFISHDrSFIRNMATRIVDLDRGKL 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-222 |
4.73e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLKKIFKTrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKP----TSGQVLLNKEDITAIKD 77
Cdd:PRK15093 3 LLDIRNLTIEFKT--SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 78 KEISAFRRDHLGFVFQDFNllDTLNVRDNIYLPLVLS------------------KSSVELMKsRLKILAPKlnieNLLE 139
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQ--SCLDPSERVGRQLMQNipgwtykgrwwqrfgwrkRRAIELLH-RVGIKDHK----DAMR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 140 KQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEIN-DSGQTIIMVTHSSLAASH-AKRVlfik 217
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqNNNTTILLISHDLQMLSQwADKI---- 229
|
....*
gi 502662315 218 dGVLY 222
Cdd:PRK15093 230 -NVLY 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-222 |
8.53e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 11 IFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEkPTSGQVllnkeditaikdkeisafrrDHLG 89
Cdd:TIGR01271 429 LFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELE-PSEGKI--------------------KHSG 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 90 ---FVFQdFNLLDTLNVRDNIYLPLVLSK----SSVEL--MKSRLKILAPKLNIenLLEKQPFELSGGQKQRVAVARALI 160
Cdd:TIGR01271 488 risFSPQ-TSWIMPGTIKDNIIFGLSYDEyrytSVIKAcqLEEDIALFPEKDKT--VLGEGGITLSGGQRARISLARAVY 564
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDllnLFEEIN---DSGQTIIMVTHSSLAASHAKRVLFIKDGVLY 222
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDVVTEKE---IFESCLcklMSNKTRILVTSKLEHLKKADKILLLHEGVCY 626
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
26-202 |
8.64e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.80 E-value: 8.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEditaikdKEISAFRRDHLgfvfqdfnllDTLNVRD 105
Cdd:PLN03073 527 NLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-------VRMAVFSQHHV----------DGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 106 NiylPLV-LSKSSVELMKSRLKILAPKLNIENLLEKQP-FELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDL 183
Cdd:PLN03073 590 N---PLLyMMRCFPGVPEQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180
....*....|....*....|..
gi 502662315 184 ---LNLFEeindsgQTIIMVTH 202
Cdd:PLN03073 667 iqgLVLFQ------GGVLMVSH 682
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-219 |
9.70e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 9.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFktrfskEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVllnkeditaiKDKE--- 79
Cdd:PRK15064 320 LEVENLTKGF------DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSEnan 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 80 ISAFRRDHLGFVFQDFNLLDTL----NVRDNiylplvlsKSSVELMKSRLkilapkLNIENLLEKQPFELSGGQKQRVAV 155
Cdd:PRK15064 384 IGYYAQDHAYDFENDLTLFDWMsqwrQEGDD--------EQAVRGTLGRL------LFSQDDIKKSVKVLSGGEKGRMLF 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 156 ARALISQPDLVLADEPTAALDFKNSEDL---LNLFEeindsgQTIIMVTH-----SSLAAshakRVLFIKDG 219
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESLnmaLEKYE------GTLIFVSHdrefvSSLAT----RIIEITPD 511
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
16-257 |
1.68e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.11 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 16 FSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEKpTSGQVLLnkeditaikdkeisafrRDHLGFVFQD 94
Cdd:TIGR00957 646 WARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHM-----------------KGSVAYVPQQ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 fNLLDTLNVRDNIYLPLVLS----KSSVEL--MKSRLKILaPKLNIENLLEKQpFELSGGQKQRVAVARALISQPDLVLA 168
Cdd:TIGR00957 708 -AWIQNDSLRENILFGKALNekyyQQVLEAcaLLPDLEIL-PSGDRTEIGEKG-VNLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 169 DEPTAALDFKNSEdllNLFEEIND-----SGQTIIMVTHSSLAASHAKRVLFIKDGVL-----YHQLYRGEKSSTEFAKe 238
Cdd:TIGR00957 785 DDPLSAVDAHVGK---HIFEHVIGpegvlKNKTRILVTHGISYLPQVDVIIVMSGGKIsemgsYQELLQRDGAFAEFLR- 860
|
250
....*....|....*....
gi 502662315 239 iTLSMTAFLGASEDEEVSL 257
Cdd:TIGR00957 861 -TYAPDEQQGHLEDSWTAL 878
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-200 |
2.27e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 10 KIFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQ--------VLLNKEDITAIKDKEIS 81
Cdd:PRK10938 5 QISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDT----LNVRDNiylplvlskssvelmkSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVAR 157
Cdd:PRK10938 85 RNNTDMLSPGEDDTGRTTAeiiqDEVKDP----------------ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 502662315 158 ALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMV 200
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-237 |
2.61e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 17 SKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEKPTSGQVLLnkeditaikdkeisafrRDHLGFVFQdF 95
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-----------------RGSVAYVPQ-V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLLDTLNVRDNI-----YLPLVLSKS-SVELMKSRLKILAPKLNIEnlLEKQPFELSGGQKQRVAVARALISQPDLVLAD 169
Cdd:PLN03232 688 SWIFNATVRENIlfgsdFESERYWRAiDVTALQHDLDLLPGRDLTE--IGERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 170 EPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVLYHQLYRGE--KSSTEFAK 237
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAElsKSGSLFKK 835
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-203 |
3.05e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.96 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 39 IMGESGSGKTTLLNILSTLEKPTSGQVLlnkeditaIKDKEISAFRRDHLGFVFQDFNLLDTLNVRDNIYLplvLSK--S 116
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIY--------YKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLKF---WSEiyN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 117 SVELMKSRLKILapklNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQT 196
Cdd:PRK13541 100 SAETLYAAIHYF----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGI 175
|
....*..
gi 502662315 197 IIMVTHS 203
Cdd:PRK13541 176 VLLSSHL 182
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-176 |
3.19e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.14 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 22 TALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikdKEISAFRRdhLGFVFQDFNLLDTL 101
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA---GDIATRRR--VGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 102 NVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:NF033858 355 TVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-228 |
3.51e-10 |
|
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: 58.04 E-value: 3.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 11 IFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPT---SGQVLLNKEDItaikdKEISAFRRDH 87
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY-----KEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 88 LGFVFQDFNLLDTLNVRDNIYlplvlskssvelmksrlkiLAPKLNIENLLEKqpfeLSGGQKQRVAVARALISQPDLVL 167
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLD-------------------FALRCKGNEFVRG----ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502662315 168 ADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVthSSLAASHA-----KRVLFIKDGvlyHQLYRG 228
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLKTTTFV--SLYQASDEiydlfDKVLVLYEG---RQIYYG 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-202 |
4.75e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 31 VEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDIT--AIKDKEISAfrrdhLGFVFQDFNLLDTLNVRDNIY 108
Cdd:PRK10762 27 VYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQEAG-----IGIIHQELNLIPQLTIAENIF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 109 L--PLVLSKSSVEL--MKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLL 184
Cdd:PRK10762 102 LgrEFVNRFGRIDWkkMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLF 181
|
170
....*....|....*...
gi 502662315 185 NLFEEINDSGQTIIMVTH 202
Cdd:PRK10762 182 RVIRELKSQGRGIVYISH 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-224 |
6.21e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.96 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:PRK10789 322 TYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSW----RSRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 -FNLLDTlnVRDNIYL--PLVlSKSSVELMkSRL-----KILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLV 166
Cdd:PRK10789 398 pFLFSDT--VANNIALgrPDA-TQQEIEHV-ARLasvhdDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 167 LADEPTAALDFKNSEDLLNLFEEINDsGQTIIMVTHSSLAASHAKRVLFIKDGVLYHQ 224
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTEASEILVMQHGHIAQR 530
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-223 |
1.06e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTLLNILsTLEKPT--SGQVLL------NKEDITAIKDkeisafrrdHLGFVFQDF 95
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-TGDHPQgySNDLTLfgrrrgSGETIWDIKK---------HIGYVSSSL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLlD---TLNVRDNIYLPLVLSKSSVELMKSRLKILAPK----LNIENLLEKQPFE-LSGGQKQRVAVARALISQPDLVL 167
Cdd:PRK10938 346 HL-DyrvSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQwldiLGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 168 ADEPTAALDFKNSEDLLNLFEEINDSGQT-IIMVTHSSLAASH--AKRVLFIKDGVLYH 223
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSHHAEDAPAciTHRLEFVPDGDIYR 483
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
11-222 |
3.65e-09 |
|
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: 56.02 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 11 IFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLL-NILSTLEkPTSGQVllnkeditaikdkeisafrrDHLG 89
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELE-PSEGKI--------------------KHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 90 FV--FQDFNLLDTLNVRDNIYLPLVLS----KSSVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQP 163
Cdd:cd03291 99 RIsfSSQFSWIMPGTIKENIIFGVSYDeyryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVLY 222
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSY 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-202 |
4.08e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.67 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 37 IAIMGESGSGKTTLLNILSTLEKPTSGQVLLnKEDITaikdkeisafrrdhLGFVFQDFNLLDTLNVRDNIYLPLVLSKS 116
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-APGIK--------------VGYLPQEPQLDPEKTVRENVEEGVAEVKA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 117 SV------------------ELMK--SRL--KILAPKL-NIENLLEK-----------QPFE-LSGGQKQRVAVARALIS 161
Cdd:PRK11819 101 ALdrfneiyaayaepdadfdALAAeqGELqeIIDAADAwDLDSQLEIamdalrcppwdAKVTkLSGGERRRVALCRLLLE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502662315 162 QPDLVLADEPTAALDfknSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:PRK11819 181 KPDMLLLDEPTNHLD---AESVAWLEQFLHDYPGTVVAVTH 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-176 |
4.42e-09 |
|
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: 56.84 E-value: 4.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLKKIFKT-----------RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKpTSGQVllnk 69
Cdd:TIGR01271 1201 LVIENPHAQKCWPSggqmdvqgltaKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEI---- 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 70 eDITAIKDKEISAFR-RDHLGFVFQDFNLLdTLNVRDNI-----YLPLVLSKSSVEL-MKSRLKILAPKLNIenLLEKQP 142
Cdd:TIGR01271 1276 -QIDGVSWNSVTLQTwRKAFGVIPQKVFIF-SGTFRKNLdpyeqWSDEEIWKVAEEVgLKSVIEQFPDKLDF--VLVDGG 1351
|
170 180 190
....*....|....*....|....*....|....
gi 502662315 143 FELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-243 |
5.22e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 27 IDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAikDKEISAFR---------RDHLGFVfqdfnl 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI--RSPRDAIRagimlcpedRKAEGII------ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 98 lDTLNVRDNI-------YLP---LVLSKSSVELMKSRLKilapKLNIENLLEKQPF-ELSGGQKQRVAVARALISQPDLV 166
Cdd:PRK11288 344 -PVHSVADNInisarrhHLRagcLINNRWEAENADRFIR----SLNIKTPSREQLImNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 167 LADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVThSSLAA--SHAKRVLFIKDGVLYHQLYRGEksSTEfAKEITLSM 243
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVS-SDLPEvlGVADRIVVMREGRIAGELAREQ--ATE-RQALSLAL 493
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-213 |
6.52e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 54.57 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 24 LVDIDFGVEEGEYIAIMGESGSGKTTL-------------LNILSTLEKPTSGQvlLNKEDIT---------AIKDKEIS 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYARQFLGQ--MDKPDVDsieglspaiAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 AFRRDHLGFVFQDFNLLDTLNVRDNIylplvlskssvelmKSRLKILApKLNIENL-LEKQPFELSGGQKQRVAVARALI 160
Cdd:cd03270 89 RNPRSTVGTVTEIYDYLRLLFARVGI--------------RERLGFLV-DVGLGYLtLSRSAPTLSGGEAQRIRLATQIG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 161 SQPDLVL--ADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRV 213
Cdd:cd03270 154 SGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHV 208
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-219 |
1.46e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 6 KHLKKIFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEdITAIKDKE--ISAF 83
Cdd:PTZ00243 658 KTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS-IAYVPQQAwiMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 84 RRDHLGFvfqdFNLLDTLNVRDNIylplvlsksSVELMKSRLKILAPKLNIEnLLEKQpFELSGGQKQRVAVARALISQP 163
Cdd:PTZ00243 737 VRGNILF----FDEEDAARLADAV---------RVSQLEADLAQLGGGLETE-IGEKG-VNLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 164 DLVLADEPTAALDFKNSEDLLnlfEEI---NDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PTZ00243 802 DVYLLDDPLSALDAHVGERVV---EECflgALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-202 |
7.21e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 25 VDIDFGveEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDitaikdkEISAFRRDHlgFVFQDFNLLDTLNV- 103
Cdd:PRK15064 20 ISVKFG--GGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-------RLGKLRQDQ--FAFEEFTVLDTVIMg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 104 ----------RDNIY-LPlvlSKSSVELMK-----------------SRLKILAPKLNIEnllEKQPF----ELSGGQKQ 151
Cdd:PRK15064 89 htelwevkqeRDRIYaLP---EMSEEDGMKvadlevkfaemdgytaeARAGELLLGVGIP---EEQHYglmsEVAPGWKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502662315 152 RVAVARALISQPDLVLADEPTAALDFkNSEDLLNlfEEINDSGQTIIMVTH 202
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDI-NTIRWLE--DVLNERNSTMIIISH 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
8-203 |
8.46e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 8.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 8 LKKIFKTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLnKEDITAIKdkeISAfrrdh 87
Cdd:PRK13545 24 LKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI-KGSAALIA---ISS----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 88 lgfvfqdfNLLDTLNVRDNIYLPLVLskssVELMKSRLKILAPKL----NIENLLEKQPFELSGGQKQRVAVARALISQP 163
Cdd:PRK13545 95 --------GLNGQLTGIENIELKGLM----MGLTKEKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502662315 164 DLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:PRK13545 163 DILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHS 202
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-221 |
9.76e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEKPTSGQVLLNKEDIT------AIkdkeisafrRDHLGFVFQD---F 95
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKirnpqqAI---------AQGIAMVPEDrkrD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 NLLDTLNVRDNIYLPlVLSKSS---------------VELMKSRLKILAPKLNIENLlekqpfelSGGQKQRVAVARALI 160
Cdd:PRK13549 351 GIVPVMGVGKNITLA-ALDRFTggsriddaaelktilESIQRLKVKTASPELAIARL--------SGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502662315 161 SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVThSSLAashakRVLFIKDGVL 221
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVIS-SELP-----EVLGLSDRVL 476
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-202 |
1.52e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRFSKEettalvDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEisa 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLID------DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQS--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDHLG---FVFQDF-NLLDTLNVrdniylplvlskSSVElMKSRLKILApkLNIE-NLLEKQPFELSGGQKQRVAVAR 157
Cdd:TIGR03719 394 --RDALDpnkTVWEEIsGGLDIIKL------------GKRE-IPSRAYVGR--FNFKgSDQQKKVGQLSGGERNRVHLAK 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502662315 158 ALISQPDLVLADEPTAALDFknsEDLLNLFEEINDSGQTIIMVTH 202
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDV---ETLRALEEALLNFAGCAVVISH 498
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-221 |
1.74e-07 |
|
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: 51.75 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLN-ILSTLEKPTSGQVLLNKEDItAIKDKEISAfrRDHLGFVFQD---FNLLDTL 101
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPV-DIRNPAQAI--RAGIAMVPEDrkrHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 102 NVRDNIYLPLVLSKSSVELMKSRLKILAPKLNIENLLEK--QPF----ELSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtaSPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502662315 176 DFKNSEDLLNLFEEINDSGQTIIMVThSSLAA--SHAKRVLFIKDGVL 221
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQEGVAIIVVS-SELAEvlGLSDRVLVIGEGKL 481
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
37-219 |
2.14e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 37 IAIMGESGSGKTTLLNILSTLEKPTSGQVllnkeditaikdkeisafrrdhlgfvfqdfnlldtlnvrdniylplvlsks 116
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 117 sVELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKNSEDLL------NLFEEI 190
Cdd:smart00382 34 -IYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLLLLLK 112
|
170 180 190
....*....|....*....|....*....|....*
gi 502662315 191 NDSGQTIIMVTH------SSLAASHAKRVLFIKDG 219
Cdd:smart00382 113 SEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLI 147
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
2-228 |
2.45e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 2 LLEVKHLkkifktRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLE--KPTSGQVLLNKEDITAIkDKE 79
Cdd:PRK09580 1 MLSIKDL------HVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLEL-SPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 80 ISAFRRDHLGF--------VFQDFNLLDTLN-VRDNIYLPLVLSKSSVELMKSRLKILapKLNIENLLEKQPFELSGGQK 150
Cdd:PRK09580 74 DRAGEGIFMAFqypveipgVSNQFFLQTALNaVRSYRGQEPLDRFDFQDLMEEKIALL--KMPEDLLTRSVNVGFSGGEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 151 QRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSslaashaKRVL-FIK-DGVlyHQLYRG 228
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHY-------QRILdYIKpDYV--HVLYQG 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-221 |
3.07e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 51.10 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQD 94
Cdd:TIGR00957 1293 RYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL----RFKITIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 95 fNLLDTLNVRDNIYlPlvLSKSSVELMKSRLKILAPKLNIENLLEKQPFE-------LSGGQKQRVAVARALISQPDLVL 167
Cdd:TIGR00957 1369 -PVLFSGSLRMNLD-P--FSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502662315 168 ADEPTAALDFKnSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:TIGR00957 1445 LDEATAAVDLE-TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
26-202 |
1.27e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.98 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEkPTSGQVLlnkeditaIKDKEISAF---RRDHLGfvfqdfnlLDTLn 102
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRL--------TKPAKGKLFyvpQRPYMT--------LGTL- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 vRDNIYLPlvlskSSVELMKSR------LKILAPKLNIENLLEKQ---------PFELSGGQKQRVAVARALISQPDLVL 167
Cdd:TIGR00954 532 -RDQIIYP-----DSSEDMKRRglsdkdLEQILDNVQLTHILEREggwsavqdwMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*
gi 502662315 168 ADEPTAALDFkNSEDllNLFEEINDSGQTIIMVTH 202
Cdd:TIGR00954 606 LDECTSAVSV-DVEG--YMYRLCREFGITLFSVSH 637
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
145-220 |
1.30e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.97 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 145 LSGGQKQRVAVARALISQP----DLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH---SSLAASHAKRVLFIK 217
Cdd:cd03227 78 LSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHlpeLAELADKLIHIKKVI 157
|
...
gi 502662315 218 DGV 220
Cdd:cd03227 158 TGV 160
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
38-202 |
1.81e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 38 AIMGESGSGKTTLLNILS---TLEKPTSGQVLLNKEDITAIKDKEISAfrrdHLGF---------VFQDFNLLDtlNVrd 105
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyalTGELPPNSKGGAHDPKLIREGEVRAQV----KLAFenangkkytITRSLAILE--NV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 106 nIYLPLVLSKSSVELMKSRlkilapklnienllekqpfeLSGGQKQ------RVAVARALISQPDLVLADEPTAALDFKN 179
Cdd:cd03240 98 -IFCHQGESNWPLLDMRGR--------------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180
....*....|....*....|....*
gi 502662315 180 SED-LLNLFEEIN-DSGQTIIMVTH 202
Cdd:cd03240 157 IEEsLAEIIEERKsQKNFQLIVITH 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-202 |
2.13e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 27 IDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQDFNLLDTlNVRDN 106
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL----RRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 107 IYLPLVLSKSSV----ELMKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ-PDLVLADEPTA----ALDF 177
Cdd:PTZ00243 1404 VDPFLEASSAEVwaalELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATAnidpALDR 1483
|
170 180
....*....|....*....|....*
gi 502662315 178 KNSEDLLNLFeeindSGQTIIMVTH 202
Cdd:PTZ00243 1484 QIQATVMSAF-----SAYTVITIAH 1503
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
15-219 |
3.81e-06 |
|
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: 46.03 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 15 RFSKEETTALVDIDFG-VEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkeisafrrdhlgfvfq 93
Cdd:cd03222 5 DCVKRYGVFFLLVELGvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV-------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 94 dfnlldtlnvrdniYLPlvlskssvelmksrlkilapklnienllekQPFELSGGQKQRVAVARALISQPDLVLADEPTA 173
Cdd:cd03222 65 --------------YKP------------------------------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSA 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502662315 174 ALDfknSEDLLNLFEEIN----DSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03222 101 YLD---IEQRLNAARAIRrlseEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-176 |
4.29e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.43 E-value: 4.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 21 TTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITaikdkeiSAFRRDHLG----FVFQDF- 95
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-------DARHRRAVCpriaYMPQGLg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 96 -NLLDTLNVRDNIylplvlskssvELMkSRLKILAP---KLNIENLLEK---QPFE------LSGGQKQRVAVARALISQ 162
Cdd:NF033858 87 kNLYPTLSVFENL-----------DFF-GRLFGQDAaerRRRIDELLRAtglAPFAdrpagkLSGGMKQKLGLCCALIHD 154
|
170
....*....|....
gi 502662315 163 PDLVLADEPTAALD 176
Cdd:NF033858 155 PDLLILDEPTTGVD 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-201 |
7.97e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 1 MLLEVKHLkkifktrfSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLL------NKEDITA 74
Cdd:PRK10982 249 VILEVRNL--------TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhgkkinNHNANEA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 75 IKD--KEISAFRRDHLGFVFQD--FNLLDTlNVRDNIYLPLVLSKSSvelMKSRLKILAPKLNIENLLEKQPF-ELSGGQ 149
Cdd:PRK10982 321 INHgfALVTEERRSTGIYAYLDigFNSLIS-NIRNYKNKVGLLDNSR---MKSDTQWVIDSMRVKTPGHRTQIgSLSGGN 396
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502662315 150 KQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVT 201
Cdd:PRK10982 397 QQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
118-219 |
8.46e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 118 VELMKSRLKILA----PKLNIENLLEKqpfeLSGGQKQRVAVARAL---ISQPDLVLaDEPTAALDFKNSEDLLNLFEEI 190
Cdd:PRK00635 450 LQGLKSRLSILIdlglPYLTPERALAT----LSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVIKKL 524
|
90 100
....*....|....*....|....*....
gi 502662315 191 NDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:PRK00635 525 RDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-219 |
1.08e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.62 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKkifkTRFSKEETTALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKpTSGQVLLNKEDITAIKDKEIsa 82
Cdd:cd03289 3 MTVKDLT----AKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKW-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 frRDHLGFVFQDFNLLdTLNVRDNI-----YLPLVLSKSSVEL-MKSRLKILAPKLNIenLLEKQPFELSGGQKQRVAVA 156
Cdd:cd03289 76 --RKAFGVIPQKVFIF-SGTFRKNLdpygkWSDEEIWKVAEEVgLKSVIEQFPGQLDF--VLVDGGCVLSHGHKQLMCLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502662315 157 RALISQPDLVLADEPTAALDFKNSEDLLNLFEEiNDSGQTIIMVTHSSLAASHAKRVLFIKDG 219
Cdd:cd03289 151 RSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-204 |
1.50e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLL----------NIlstlekptSGQVLLNKEDIT------AIK--------Dkeis 81
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELAmsvfgrsygrNI--------SGTVFKDGKEVDvstvsdAIDaglayvteD---- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 afrRDHLGFvfqdfNLLDTlnVRDNIYLPLV--LSKSSV----------ELMKSRLKILAPklNIENLLEKqpfeLSGGQ 149
Cdd:NF040905 346 ---RKGYGL-----NLIDD--IKRNITLANLgkVSRRGVideneeikvaEEYRKKMNIKTP--SVFQKVGN----LSGGN 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 150 KQRVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVthSS 204
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI--SS 462
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-202 |
1.80e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 26 DIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQV----------------LLNKEDiTAI-------KDKEISA 82
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtklevayfdqhraELDPEK-TVMdnlaegkQEVMVNG 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 83 FRRDHLGFVfQDFnlldtlnvrdnIYLPlvlskssvelMKSRLKILApklnienllekqpfeLSGGQKQRVAVARALISQ 162
Cdd:PRK11147 416 RPRHVLGYL-QDF-----------LFHP----------KRAMTPVKA---------------LSGGERNRLLLARLFLKP 458
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502662315 163 PDLVLADEPTAALDFKNsedlLNLFEEINDSGQ-TIIMVTH 202
Cdd:PRK11147 459 SNLLILDEPTNDLDVET----LELLEELLDSYQgTVLLVSH 495
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
146-203 |
1.83e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 502662315 146 SGGQKQRVAVARALISQPDLVLADEPTAALDFknsEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKTFIVVSHA 400
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
144-202 |
2.45e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 2.45e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502662315 144 ELSGGQKQRVAVARALiSQPD----LVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:cd03271 169 TLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEH 230
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
59-219 |
3.33e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 59 KPTSGQVLLNKEDITAIKDKEIsafrRDHLGFvfqdFNLLDtLNVRDNIYLPLVLSKssvelMKSRLKILA----PKLNi 134
Cdd:TIGR00630 417 KPEALAVTVGGKSIADVSELSI----REAHEF----FNQLT-LTPEEKKIAEEVLKE-----IRERLGFLIdvglDYLS- 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 135 enlLEKQPFELSGGQKQRVAVARALISQPDLVL--ADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAKR 212
Cdd:TIGR00630 482 ---LSRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADY 558
|
....*..
gi 502662315 213 VLFIKDG 219
Cdd:TIGR00630 559 VIDIGPG 565
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-202 |
3.75e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.62 E-value: 3.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 145 LSGGQKQRVAVARALiSQPD----LVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:TIGR00630 830 LSGGEAQRIKLAKEL-SKRStgrtLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
99-202 |
1.54e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 99 DTLNVRDNIYL---PLVLSKSSVelmKSRLKILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAAL 175
Cdd:NF000106 99 ESFSGRENLYMigr*LDLSRKDA---RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGL 175
|
90 100
....*....|....*....|....*..
gi 502662315 176 DFKNSEDLLNLFEEINDSGQTIIMVTH 202
Cdd:NF000106 176 DPRTRNEVWDEVRSMVRDGATVLLTTQ 202
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
31-221 |
2.14e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 41.43 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 31 VEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEIsafrRDHLGFVFQDfNLLDTLNVRDNIYLP 110
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQD-PILFSGSIRFNLDPE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 111 LVLSKSSV--ELMKSRLKILAPKL--NIENLLEKQPFELSGGQKQRVAVARALISQPDLVLADEPTAALDFKnSEDLLNL 186
Cdd:cd03288 119 CKCTDDRLweALEIAQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQK 197
|
170 180 190
....*....|....*....|....*....|....*
gi 502662315 187 FEEINDSGQTIIMVTHSSLAASHAKRVLFIKDGVL 221
Cdd:cd03288 198 VVMTAFADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
47-205 |
2.31e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.61 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 47 KTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRDHLGFVFQDFNLLDTLNvrDNIYLPLVLSKSSVELMKSRLK 126
Cdd:pfam13304 141 GLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLAD--LNLSDLGEGIEKSLLVDDRLRE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 127 ILAPKLNIENLLEKQPFELSGGQKQRVAVARALISQ---PDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:pfam13304 219 RGLILLENGGGGELPAFELSDGTKRLLALLAALLSAlpkGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHS 298
|
..
gi 502662315 204 SL 205
Cdd:pfam13304 299 PL 300
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-203 |
2.71e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 23 ALVDIDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEdITAIKdkeISAfrrdhlgfvfqdfNLLDTLN 102
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-VSVIA---ISA-------------GLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 103 VRDNIYLPLVLskssVELMKSRLKILAPKL-NIENLLE--KQPFE-LSGGQKQRVAVARALISQPDLVLADEPTAALDFK 178
Cdd:PRK13546 102 GIENIEFKMLC----MGFKRKEIKAMTPKIiEFSELGEfiYQPVKkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*
gi 502662315 179 NSEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHN 202
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
31-256 |
1.04e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 31 VEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKEDITAIKDKEISAFRRDHLGFVF-------QDFNLLDTLNV 103
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdreyrQLEAQLHDANE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 104 RDN----IYLPLVLSKSSVELMKSRLKILAPKLNIENLLEKQPF-ELSGGQKQRVAVARALISQPDLVLADEPTAALDFk 178
Cdd:PRK10636 104 RNDghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVsDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL- 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502662315 179 nsEDLLNLFEEINDSGQTIIMVTHS-SLAASHAKRVLFIKDGVLYHqlYRGEKSSTEFAKEITLSMTAFLGASEDEEVS 256
Cdd:PRK10636 183 --DAVIWLEKWLKSYQGTLILISHDrDFLDPIVDKIIHIEQQSLFE--YTGNYSSFEVQRATRLAQQQAMYESQQERVA 257
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-176 |
1.10e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.10 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 3 LEVKHLKKIFKTRFskeettaLVD-IDFGVEEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLLNKediTAikdkeis 81
Cdd:PRK11819 325 IEAENLSKSFGDRL-------LIDdLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE---TV------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 82 afrrdHLGFVFQ--DfNLLDTLNV-------RDNIYLplvlskSSVElMKSRLKILApklnienllekqpF--------- 143
Cdd:PRK11819 388 -----KLAYVDQsrD-ALDPNKTVweeisggLDIIKV------GNRE-IPSRAYVGR-------------Fnfkggdqqk 441
|
170 180 190
....*....|....*....|....*....|....*.
gi 502662315 144 ---ELSGGQKQRVAVARALISQPDLVLADEPTAALD 176
Cdd:PRK11819 442 kvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
25-211 |
1.25e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 25 VDIDFgveEGEYIAIMGESGSGKTTLLNILSTLEKPTSGQVLlNKED---------------------ITAIKDKEISAF 83
Cdd:COG3593 17 LSIEL---SDDLTVLVGENNSGKSSILEALRLLLGPSSSRKF-DEEDfylgddpdlpeieieltfgslLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502662315 84 RRDHLGFVFQDFN-----LLDTLNVRDNIYLPLVLSKSSVEL--MKSRLKILAPKLNIE-NLLEKQPFELSG-GQKQRV- 153
Cdd:COG3593 93 DKEELEEALEELNeelkeALKALNELLSEYLKELLDGLDLELelSLDELEDLLKSLSLRiEDGKELPLDRLGsGFQRLIl 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 154 -AVARALI-----SQPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHSSLAASHAK 211
Cdd:COG3593 173 lALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVP 236
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
145-208 |
2.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.11 E-value: 2.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502662315 145 LSGGQKQ------RVAVARALISQPDLVLADEPTAALDFKNSEDLLNLFE-EINDSG---QTIIMVTHSSLAAS 208
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSdipQVIMISHHRELLSV 875
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
145-203 |
4.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502662315 145 LSGGQKQRVAVARALIS---QPDLVLADEPTAALDFKNSEDLLNLFEEINDSGQTIIMVTHS 203
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHN 871
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-202 |
8.90e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 8.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502662315 145 LSGGQKQRVAVARALiSQPD----LVLADEPTAALDFknsED---LLNLFEEINDSGQTIIMVTH 202
Cdd:COG0178 827 LSGGEAQRVKLASEL-SKRStgktLYILDEPTTGLHF---HDirkLLEVLHRLVDKGNTVVVIEH 887
|
|
| |
